Index

Major discussions and tabular citations are noted in bold type.

A acetyl 75-76 exchange reactions 75 Aasa, R. 41,42,58 kinetics 75 Abbott, S.l. 97 mechanism 75-76 Abdullah, M. 111 Acetyl-CoA carboxylase 220 Abeles, R.H. 9,24,28,34,54,55, 79, Acetyl-CoA synthetase 208-209,220 80, 151, 177, 178, 181, 185, 189, acetyl adenylate 208-209 190, 201 acetyl enzyme 208-209 Abramovitz, A.S. 77 exchange reaction 208 - 209 Abramson, R. 112 inversion of configuration on Acetaldehyde 177 -179 phosphorus 209 hydration 172 mechanism 208 - 209 Acetate Co A- 108 triple-displacement reaction 209 Acetate kinase 92-96, 108 Acetylesterase 147 exchange reactions 93 N-Acetylglucosamine 89-90 kinetics 94 Acetylglucosamine phosphomutase mechanism 95 108 mercuric ion, effects on 94, 96 f3-N- Acetylglucosaminidase 147 noncontiguous binding of Acetylium ion 18 substrates 94-96 N-Acetylneuraminate 182 nuc1eosidediphosphate kinase Acetyl phosphate 92-96, 202, 217 activity 93-94 Acid phosphatase 120-121, 147 phosphoenzyme 92-96 phosphoenzyme 120 steric inversion on phosphorus 92 Acid protease from Rhizopus surface walk 96 chinensis 149 triple displacement 92, 95 Aconitase 182 Acetoacetate decarboxylase 17, Aconitate ~- 200 157 -158, 182 Acrosin 148 exchange reactions 157 -158 Actinidin 148 mechanism 157 Activation of water 114, 119, 130-131, Schiff base intermediates 157 145-146,173,177 Acetoacetate, decarboxylation, [Acyl-carrier protein] nonenzymic 17 acetyltransferase 106 Acetoacetyl-CoA 75, 104-106, [Acy I-carrier -protein] 166-167 malonyltransferase 76-77, 106 Acetolactate synthase 182 malonyl enzyme 76-77 Acetyl adenylate 203 Acyl-CoA dehydrogenase 49 Acetylcholinesterase 147 Acyl-CoA 147 Acetyl-CoA 17,74,75,76, 166, 167, Adachi, K., 56 168-170, 208, 209, 214 Adair, Jr., W.L. 195 Acetyl-CoA acetoacetate Adams, C.A. 112 Co A-transferase 108 Adams, E. 184, 200 Acetyl-CoA acetyltransferase 75 -76, Adams, R.W. 152 106 Adenine 80-82 238 Index

Adenine phosphoribosyltransferase 10, retention of steric configuration of 80-83, 89, 107 phosphorus 119 mechanism 82 transferase activity 117 phosphoribosyl enzyme 81-82 Alkane-l-monooxygenase 51 steric inversion on carbon 10, 80-83 2-(5-n-)furoic acid, p-nitrophenyl surface walk 10 134 triple displacement 82-83 Allen, S.H.G. 33 Adenosine deaminase 149 Allison, AJ. 222 Adenosylhomocysteinase 148 Allothreonine 64 Adenylic acid 80-81 Alston, T.A. 54 Adenylysulfate reductase 18-29, SO Alworth, W.L. 174 sulfite-enzyme adduct 29 Ambrose-Griffin, M.C. 6, 110 Aerts, G.M. 151 w-Amidase 149 Ahmad, F. 65 Amidophosphoribosyltransferase 107 Airas, R.K. 153 oxidase (FAD) SO Akashi, K. 221 Amine oxidase (PLP) SO Akeson, A. 34 0-Amino-acid dehydrogenase SO Akhtar, M. 110 o-Amino-acid oxidase 23-27, SO f3- Alanine 207 - 208 o-alanine, as 23, 27 Alanine aminotransferase 107 D-f3-chloralanine, elimination of D-Alanine aminotransferase 108 HCI 24-25 D-Alanine carboxypeptidase 148 cyanide ion, as inhibitor 24-25 Alanine racemase 186-188, 199 nitroethane, as substrate 24-25 mechanism 186-188 reconstituted with 5-deaza Schiff base intermediate 186-188 FAD 26-27 suicide substrates 188 shielded proton 25 Albers, R.W. 144, 146 L-Amino-acid oxidase 49 Alberts, A.W. 110 Aminoacylase 149 Albery, W.J. 39, 196 p-Aminobenzoate synthase 182 Albizati, L 153 Aminobutyrate aminotransferase 108 Alcohol dehydrogenase 33-38,49 Aminolevulinate dehydratase 182 catalytic use of NAD 33-34 8-Aminolevulinate synthase 106 coordination of substrates with zinc 35 4-Aminovalerate 159-160 trans-4-N,N-dimethylaminocinnam- AMP deaminase 149 , as substrate 35 a-Amylase 147 dimutase activity 34 Amylo-l,6-glucosidase 148 mechanism 36-38 Amylosucrase 106 p--N,N-dimethylaniline, as Anan, F.K. 55 substrate 35-36 Andani, Z. 152 Aldehyde oxidase 32, 49 Anderson, B.M. 127 Alden, R.A. 152 Anderson, C.M. 20,90 Aldrich, F.L. 132 Anderson, J.R. 2 Aldridge, W.N. 118 Anderson, L. 99, 150 Aleman, V. 54 Anderson, P.M. 112,222 Alexander, D.R. 144 Anderson, W.F. 88 Alger, J.R. 119 Andreasson, L.E. 41,42 Alkaline phosphatase, 117-120,147 A4-Androstene-3, 17-dione 196 activated water 119 AS- Androstene-3, 17 -dione 196 mechanism 119 Anfinsen, C.B. 11,94 orthophosphate- exchange 118 Angelides, KJ. 6, 126, 137 phosphoenzyme 117 -120 Angelis, C.T. 35 Index 239

Anke, H. 208 Asparaginase 149 Ankel, E. 111 Asparagine synthetase 220 Ankel, H. 111,195 Aspartate aminotransferase 84-86, 107 Anraku, Y. 219 kinetics 84 Anthony, R.S., VII 92,93 mechanism 84-85 Anthranilate synthase 182 a-methylaspartate, as substrate 84-85 Anthropomorphism in enzymic phosphopyridoxamine-enzyme 84 - 85 13 -15 Schiff base intermediates 85-86 Antonini, E. 41, 54, 153 Aspartate ~-decarboxylase 182 Antonov, V.K. 138 D-Aspartate oxidase 49 Anwar, R.A. 111 Aspartate-semialdehyde Aparicio, P.J. 56 dehydrogenase 49 Apitz-Castro, R. 128 Aspergillus alkaline proteinase 148 Applebaum, J. 176 Aster, S.D. 183 Applebury, M. L. 119 Atkinson, R.F. 151 Appleby, C.A. 52 ATPase 144-147, 149 Arabinose isomerase 199 activation of water 145-146 L-Arabinose isomerase, 199 calcium-magnesium -dependent Araiso, T. 57 146-147 L-Arginine 69 electrogenic 147 182 exchange reactions 146 Arginine 2-monooxygenase 51 inversion of configuration of Arginine racemase 199 phosphorus 147 Argument from analogy 91-92, 144, mechanism 145 223-224 phosphoenzyme 144-147 Arigoni, D. 178, 201 sodium -potassium- Arion, W.J. 121 dependent 144-146 Armitage,I.M. 119, 173,214 ATP citrase lyase 92,168-170,182 Arnold, W.J. 81 acetyl enzyme 169-170 Amon, D.1. 58 citryl enzyme 169-170 Arnone, A. 85 exchange reaction 169 Aromatic L-amino-acid mixed anhydride intermediate 170 decarboxylase 182 phosphoenzyme 169 -170 Aronson, J.N. 153 Au, A. M.J. 35 Arthrobacter serine proteinase 148 Augustinsson, K.B. 150 Arvidsson, L. 97 Aull, J.L. 150 Aryl acyl amidase 149 Avaeva, S.M. 143 Arylamine acetyltransferase 18, 74-75, Averill, B.A. 28, 59 106 Avigad, G. 110, 164 acetylenzyme 18, 74-75 Avron, M. 112 exchange reactions 74 Awad, W.M. 150 kinetics 74-75 Axcell, B.C. 57 Arylsulfatase 123-124, 147 Axeirod, B. 120, 151 kinetics 124 Axeisson, K. 46 sulfonyl enzyme 123-124 Ayling, J.E. 86 transferase activity 124 Asada, K. 56 Asano, A. 53 B Ascorbate oxidase 42, 51 Ashman, L.K. 215 Babior, B.M. 185, 201 AskelOf, P. 46 Babu, U.M. 188 240 Index

Baumann, F. 151 Bachovchin, W.W. 178 Bayliss, R.S. 138 Bacitracin synthetase 220 Beachum, III, L.M. 53 Biickstrom, D. 58 Beaty, N.B. 30 Bacon, J.S.D. 110 Beaucamp, K. 156 Bacterialluciferase 49 Becker, M.A. 185 Baggott, J .E. 135 Beeler, T. 112 Bagirov, E.M. 112 Begard, E. 58 Bai, Y. 151 Begue-Canton, M.L. 136 Bailey, G.B. 184 Beinert, H. 54, 55, 56 Bailey, J.L. 55 Belasco, J.G. 154, 196 Baird, J.B. 152 Bell, R.M. 2 Bak, T.G. 53 Bendall, D.S. 58 Baker, 1.1. 201 Bender, M.L. 2, 133, 135, 136, 152 Bakuleva, N.P. 143 Benisek, W.F. 197 Balboni, G. 73, 164 Benjamin, W.B. 170 Baldwin, R.L. 185 Benkovic, S.J. 2, 19, 123, 124, 150 Balinsky, J .B. 221 Bennett, J. 153 Ballou, C.E. 111 Bennett, R. 54 Ballou, D.P. 30,31,48,58 Bennett, Jr., W.S. 88 Balls, A.K. 132 Benson, R. W. 104, 210 Balny, C. 31 Benzene 1,2-dioxygenase 51 Baltimore, B.G. 201 Benzil 116 Baltzinger, M. 207 Benzil monooxime 116 Bamforth, C.W. 55 Berg, P. 203, 208 Bandurski, R.S. 56 Bergamini, M.V.W. 110 Baratova, L.A. 143 Berger, A. 137 Baratti, J. 152 Bergmann, F. 150 Barden, R.E. 215 Bergsten, P.C. 173 Bardsley, W. G. 54 Bergstrom, B. 151 Barker, H.A. 8, 78, 201 Berman, K. 113 Barlow, C.H. 42,46 Berman, K.M. 91 Barman, T.E. 118 Berman, M. 144 Barnard, E.A. 120 Bernard, C. 9 Barnett, J.E.G. 184, 201 Bernath, P. 54 Barnett, R.E. 145 Berndt, M.C. 116 Barns, R.J. 162 Bernhard, S.A. 35, 53, 152 Baron, A. 150 Bernhardt, F.-H. 58 Baron, D. 184 Bernhardt, R. 54 Baron, J. 46, 58 Bessman, S.P. 74 Barra, D. 40 Bethge, P.H. 129 Barrett, H. 91,117 Bhaduri, A.P. 30 Barshevskaya, T.N. 138 Biellmann, J.-F. 35,53 Bartfai, T. 150 Bigbee, W.L. 153 Bartmann, P. 206 Bilirubin-glucuronoside Basu, M. 111 glucuronosyltransferase 107 Basu, S. 111 Billing, B.H. 111 Bates, D.L. 6 Bingham, A. 154 Battersby, A.R. 180 Binkley, S.B. 184 Bauer, C.-A. 153 Birch, M. 99 Baugn, R.L. 183 Birktoft,1.1. 131, 152 Index 241

Bisaz, S. 118 Boursnell, J .H. 115 Bis(4-nitrophenyl)phosphate 122-123 Bovier-Lapierre, C. 150 2,3-Bisphospho-D-glycerate 197 Boyer, P.D. 53,74,104,143,146,150, Bisphosphoglycerate phosphatase 147 177,210 Bisphosphoglycerate synthase 97, 108 Bradley, S. 150 Bisphosphoglyceromutase lOS Brady, F.O. 57 Black, M.K. 98 Bramlett? R.N. 56 Black, S. 55 Branched-chain-amino-acid Blackmore, P.F. 72 aminotransferase 108 Blackwell, L.F. 53 Brand, K. 73, 74, 109 Blake, R.C. 46 Branden, C.I. 34 Blakeley, R.L. 58, 136, 181 Branden, R. 41 Blankenhorn, G. 27,30 Brandt, K.G. 55 Blaschkowski, H.P. 110 Branlant, G. 35 BUittler, W.A. 11,87,92,112, 198 Branzoli, U. 32 Blattmann, P. 54 Braunshtein, A.E. 86, 159, 185 Blethen, S.L. 183 Bray, R.C. 31,32,53,56,58 Bloch, K. 221 Brayer, G.D. 153 Bloch, W. 53 Breathnach, R. 91, 198 Blood-group-substance Breaux, E.J. 152 a-D-galactosyltransferase 107 Breebaart-Hansen, J.C.A.E. 150 Bloom, B. 165 Brennan, P. 111 Blostein, R. 144, 146 Bresler, S.E. 56, 110 Blow, D.M. 131 Brevet, A. 97 Bloxham, D.P. 75 Bridger, W.A. 91,210,211 Blue oxidases Bright, H.I. 24,25,28,53,54,56,111 ascorbate oxidase 42 Briley, P.A. 85 ceruloplasmin 41-42 Brill, W.I. 59 laccase 40-41 Brillinger, G.-U. 185 Blumberg, P.M. 152 Bristow, A.F. 154 Blumberg, W. 58 Britton, H.G. 99, 100, 112, 198 Bobi, A. 184 Britton, L.N. 58 Boches, F.S. 102 Brocklehurst, K. 137, 153 Bock, J.L. 118, 119 Brodie, J.D. 61, 201 Boeker, E.A. 158, 183 Broman, L. 41, 58 Boeri, E. 53 Bromelain 148 Bogacheva, T.!. 110 Brons, D. 150 Boggaram, V. 55 Brot, N. 221 Boiwe, T. 34 Brown, C.M. 54 Boland, M.I. 153 Brown, C.R. 152 Boldingh, J. 57 Brown, F.C. 185 Bolognesi, M.C. 153 Brown, F.S. 44 Bond, G.C. 2,4 Brown, G.M. 156 Bone, D.H. 57 Brown, J.P. 165 Bonfils, C. 46 Brown, K.L. 150 Booth, A.G. 151 Brownson, C. 58 Borchers, R. 55 Brox, L.W. 165 Borri Voltattorni, C. 183 Broxmeyer, B. 110 Bossa, F. 40 Brubacher, L.J. 136 BoucHer, M. 160 Brudzynski, T.M. 153 Bourne, E.J. 110 Bruce, T.C. 2,28, 151 242 Index

Briihmiiller, M. 35 carbon dioxide, hydration 173 -174 Brunori, M. 56, 153 dimethyl 2,4-dinitrophenyl phosphate, 6ri.istlein, M, 30 hydrolysis 173 Bryant, F.R. 123 2 ,4-dinitrotl uorobenzene, Bryce, G.F. 221 hydrolysis 173 Buchanan,l.M. 53,222 mechanism, role of Zn 173-174 Buckel, W. 167, 168, 184 p-nitrophenyl acetate, hydrolysis 172 Buckingham, D.A. 131, 173 suitones, hydrolysis 172 Buckley, P.D. 53 Carboxyamidase 148 Buddecke, E. 151 f3- Carbox ymuconolactone Buffoni, F. 54 ~-isomerase 200 Bulargina, T. V. 112 Carboxylesterase 115-116, 147 Bull, H.G. 128 acyl enzyme 115-116 Bulos, B. 111 carbon-carbon cleavage by 116 Bunch, H. V inhibition 1I5-1I6 Burger, M.M. 111 transferase activity 1I5 Burgers, P.MJ. 102,123 Carboxypeptidase A 128-131, 148 Burgett, M.W. 54 activation of water 130-131 Burke, G.T. 61 trans-p-chlorocinnamoylenzyme 131 Burns, G.R.l. 124 mechanism 130 Burris, R.H. 59 mixed anhydride Burstein, Y. 152 intermediate 129-131 Burton, R.M. 38 Carboxypeptidase C 148 Buschmeier, V. 167, 168 Carboxyl phosphate 216 Butler, 1.R. 174, 175 Cardinale, G.1. 189, 201 Butler, L.G. 121,122, 143, 151 Cardinaud, R. III Butler, R. 91, 117 Cardini, G. 58, 110, III Butterworth, P.l. 110 Carlberg, I. 55 Butyryl-CoA dehydrogenase 49 Carlbom, U. 173 Byrne, W.L. 121 Carlson, D.M. 1I2 Carlson, G.L. 156 Carmichael, D.F. 56 c Carnie,1.A. 151 Carnosine synthetase 207 - 208, 220 Cabib, E. 110, 153 adenylyl enzyme 207-208 Cacciapuoti, G. 111 f3-alanyl adenylate 207 - 208 Calabrese, L. 40, 58 f3-alanyl enzyme 207 - 208 Campagnari, F. 208 exchange reaction 207 - 208 Camphor 45 mechanism 207 Camphor 5-monooxygenase 45-46, 51 Carpenter, D.E. 167 Cannella, C. 103 Carpenter, F.H. 153 Cantwell, A. 200 Carreras, 1. 1I2, 198 Capeillere-Blandin, C. 52 Carrico, RJ. 42 Caplow, M. 1I8, 150 Carson, F.W. 129 Capping enzyme 108 Carty, T.J. 185 Caprioli, R.M. 164 Cash, C. III Carbamyl phosphate 216 Cassidy, P.J. III Carbamyl phosphate synthetase 220 Castelfranco, P. 204 Carbonic anhydrase 172-174,182 Castric, P.A. 222 acetaldehyde, hydration 172 Caswell, M. 118, 150 activation of water 173 Catalase, 18,43-45, 51 Index 243

Catalysis Chen, F.T. 144 chemisorption in 3-4 Chen, K. 150 covalent 2, 8 Chen, K.C.S. 138 definition 21 Chen, M.S. 64 double displacement, definition 8 Cheng, C.C. 28 enzymic 8-9 Cheng, L.Y. 87 heterogeneous 2-5 Cheng, P.-W. 112 homogenous 2 Cheng, T. 73, 74, 164 mass-law 1, 225 Cheruy, A. 98 nonenzymic, resemblance to enzymic Cheshnovsky, D. 172 catalysis 2-7 Cheung, L. 0 . 57 of benzoin condensation by cyanide Cheung, Y.F. 184 ion 16 Chiang, R. 45 of oxidation by cupric ion 15-16 Chiba, H. 150 physisorption in 3-4 Chiba, S. 151 single displacement Chibata, I. 181 assumption of 8-9 Chien, J.R. 219 definition 1, 8 Chiriboga, J. 110 Cate, R.L. 6, 54 Chlebowski, J.F. 118, 119, 120 Catechol oxidase 51 O-(trans-p-chlorocinnamoyl)-L- Cathespin D. 149 (3-phenyl-lactate 128-129, 131 Cathou, R.E. 53 Chloroperoxidase 43-45, 51 Caughy, W.S. 42,46 Cholesterol oxidase 49 Cavallini, D. 103 Choline oxidase 49 CDP-4-keto-6-deoxY-D-glucose Cholinesterase 147 reductase 52 Choong, Y.S. 28 Cecil, R. 47 Christen, P. 85, 165, 166 Cedar, H. 153 Christensen, U. 152 Cellobiose:quinone 49 Christova, E. 152 Cellulase 147 Chu, J.W. 58 Cerra, M. 34 Chu, S.Y. 222 Ceruloplasmin 52 Chuang, M. 65 ferrous ion, oxidation of 41 Chung, A.E. 112 Ceulen, B.1. 150 Chung, K.H. 150 Cha, C.M. 221 Chung, S.1. 78 Cha, S. 221 Churchich, J.E. 112 Chakraburtty, K. 203 Chymotrypsin 131-135, 148 Chamber!, R. 110 acyl enzyme 132-135 Champoux, J.J. 198 deacylation 134-135 Chance, B. 42,43, 57 diisopropyl phosphoryl Chance, E.M. 42 chymotrypsin 134 Chang, H.-C. 162 insulin, as substrate 133 Chang, W.J. 153 mechanism 134 Chapus, C. 150 oxygen exchange reactions 133 Charles, M. 150 surface walk 135 Charnock, J.S. 144 Cid-Dresdner, H. 173 Chase, T. 152 Ciesielski, L. 111 Chatt, J. 15 trans- Cinnamate 179 - 181 Chaykin, S. 153 trans-Cinnamoyl imidazole 136 Chelsky, D. 83 Ciotti, C.J. 127 Chen, F.S. 104 Citramalate lyase 182 244 Index

Citrate 167, 168, 169 Conconi, F. 69 Citrate lyase 167 -168, 182, 211 Congdon, W.1. 124 acetyl enzyme 167 -168 Conjalka, M. 54 citryl enzyme 168 Conklin, K.A. 112 dephospho CoA, modified, as prosthetic Conn, E.E. 38, 185 group 167 Connellan, 1. 58 Citryl phosphate 92, 169-170, 216 Cook, P.F. 185 Claeyssens, M. 151 Coolen, R.B. 36 Clark, D.R. 150 Coon, MJ. 46, 201 Clark, M.G. 72, 75 Cooper, AJ.L. 111 Clarke, J.B. 99, 100 Cooper, D.Y. 58 Clegg, R.A. 56 Cooper, R.A. 91,113 Cleland, W.W. 84,97,98, Ill, 112, Cooper, T. 222 150, 201, 215 Copper 39-42 Clinkenbeard, K.D. 166 Copper ion, complexed with substrate in, Clodfelder, P. 53 superoxide dismutase 40 Clore, G.M. 42 Cordes, E.H. 128 Clostripain 148 Corina, D.L. 184, 201 Cobalt coordinated to substrate in Cornforth, J.W. 168 o-a-Lysine 199 Costa, M. 103 propranediol dehydrase 178 -179 Costa, M.T. 54 transcarboxylase 67 Costilow, R.N. 185,201 Cocoonase 148 Cottam, G. L. 170 Codini, M. 183 Cotton seed proteinase 148 Coenzyme A transferase 104-106, 108, Coulson, A.F.W. 56, 196 139, 212-214 Couri, D. 109 Co A-enzyme intermediate 104-106 Courtois, J .E. 151 exchange reactions 106 Coustal, S. 197 kinetics 106 Covalent catalysis mechanism 105 comparison with single-displacement mixed carboxylic anhydride catalysis 11-15 intermediates 105 criteria 52, 108-109, 149-150, 183, oxygen transfer 104-106 200,221 Coffey, R.L. 146 enthalpy of activation 14 Cogoli, A. 151 entropy of activation 14 Cohen, HJ. 56 one-at-a-time handling of Cohen, P.T. 55 substrates 12-13 Cohen, S.N. 74 noncontiguous binding of Cohn, M. 19,91,113, 118, 143, 175, substrates 13-14 177 stabilization of hypothetical Cole, P.G. 111 intermediates 15 - 20 Cole, P. W. 77, 153 steric inversion of Cole, R.D. 112 configuration 10-11 Coleman, J.E. 40, 118, 119, 120, 173 surface walks 14 Coles, C.J. 54 the swinging arm 14 Collins, J.H. 6, 110 Covalent enzyme-substrate intermediate Colman, R.F. 52 definition 2, 8 Colomb, M.G. 98 likeness to chemisorbed state 4 Colowick, S.P. 87,88,89, 112, 127 Cozzarelli, N.R. 201 Compound I 43-45 Crabbe, MJ.C. 55 catalase 18 Cranston, J.W. 222 Index 245

Crawford, LP. 185 Dalziel, K. 34 Cremona, T. 53 Dame, J.B. 150 Cretney, W.C. 59 Danenberg, P. V. 109 Cromartie, T.H. 53 Danowski, T.S. 54 Cronan, Jr., J.E. 214 Danson, MJ. 6, 110 Crook, E.M. 151,153 Danzin, C. 111 CTP synthetase 220 Dardinger, D.E. 122 Cunningham, L.W. 53 D'Ari, L. 84 Cunningham, M. 153 Dateo, G.P. 151 Curragh, E.F. 152 Datta, A.G. 70, 109 Curtis, C.G. 150 Daugherty, J.P. 99 Curtius, C.H. 150 Davidson, J.T. 28 Curtius, H. C. 151 Davidson, S.J. 54 Cutinase 147 Davie, E.W. 203 Cyanide ion 103-104 Davies, D.R. 153 J3-Cyanoalanine synthase 183 Davis, J.S. 221 eHJ3' ,5'-Cyclic AMP 123 Davis, L. 109, 184, 200 Cyclohexanone oxygenase 51 Davis, L.C. 165 Cyclohexylamine oxidase 50 Davis, P.S. 56 Cyclomaltodextrin Dawson, C.R. 42, 56 glucanotransferase 107 Dayan, J. 117 Cyclopentanone oxygenase 51 de Amaral, D.F. 55 J3-Cyclopiazonate oxidocyclase 49 5-Deaza FAD, as analogue of NAD, 27 Cyr, K. 117 Debaere, L.TJ. 138 Cystathionine y-Iyase 183 Debey, P. 46,58 Cystathionine y-synthase 183 De Bock, A. 151 Cysteine lyase 183 de Bony, J. 204 Cysteine synthase 183 Debrunner, P. G . 46 Cytochrome C3 hydrogenase 51 De Bruyne, A. 151 Cytochrome oxidase 51 De Bruyne, C.K. 126, 151 Cytochrome P-450 45 Decker, E.E. 184 Cytochrome peroxidase 51 Decker, K. 55 Cytochrome bs reductase 50 Dedonder, R. 110 Cytochrome c oxidase 51 Degani, C. 143 coordination of dioxygen to Fe 42 de Groot, JJ.M.C. 57 mechanism 42 De Gussem, R.L. 151 Dehydroquinase 174-175, 182 mechanism 174-175 D Schiff base intermediate 174-175 5- Dehydroquinate 174 -175 Dagley, S. 185 5-Dehydroshikimate 174-175 D'Agnolo, G. 110 Deinum, J. 41 Dahl, J.L. 144 de Jersey, 1. 116 Dahlquist, F. 151,153 De la Fuente, G. 89 Dahlqvist, A. 151 De La Rosa, M.A. 55 Dahlqvist, U. 133 Delbaere, L.T.J. 153 Dahms, A.S. 146 Delcambe, L. 57 Dai, V.D. 55 Del Campillo-Campbell, A. 112 Daidoji, H. 57 Deleyn, F. 151 Dalton, B.P. 55 de Meis, L. 146 Dalton, H. 32 Dempsey, W.B. 112 246 Index

Dennis, D. 200 2,3-Diphosphoglycerate 97 2-Deoxy-,B-o-galactose 126 enzymes 46-48 Deoxyribose-phosphate aldolase 182 dihydrolipoamide reductase 48 Deoxyuridylate hydroxymethylase 106 glutathione-cystine Depew, R.E. 198 trans hydrogenase 46-47 3' -Dephospho Co A 166, 208 glutathione reductase 47 -48 De Prijcker, 1. 151 thioredoxin reductase 48 DerVartanian, D. V. 54, 56 Dixon, G.H. 132, 152 DeSa, R.1. 55 Dixon, J.E. 56 Deschavanne, P.I. 126, 151 Dixon, N.E. 181 Desnuelle, P. 150, 152 DNA gyrase 200 Desvages, G. 91,97 DNA (ATP) 221 De Toma, F. 79 DNA ligase (NAD) 217-220,221 Deupree, 1. D . 200 adenylyl-DNA 218-219 Deus, B. 184 adenylyl enzyme 218-219 DeVries, G.H. 184 DNA-enzyme 218-220 Dextransucrase 106 mechanism 218 - 220 Dextrin dextranase 106 NMN-NAD exchange 219 Dey, P.M. 151 DNA polymerase 108 Dialkylamino-acid decarboxylase 182 DNA topoisomerase 198,200 2,4-Diaminobutyric acid 97 Doherty, D. 133 2,5-Diaminohexanoate 199 Dolin, M.l. 53, 56 Diamondstone, T.l. III Dolphin, D. 44 DiBello, C. 11, 94 Dondon, L. 112 Dickenson, F.M. 34 Donninger, C. 168 Dietrich, H. 35 Donoghue, N.A. 58 Diez, I. 55 Dopamine ,B-monooxygenase 51 Dignam, J.D. 55 Dorizzi, M. 204 Dihydrolipoamide reductase 48 Doubek, D.L. 43, 57 Dihydrolipoyl dehydrogenase 6 Doudoroff, M. 8, 78 Dihydrolipoyl transacetylase 6 Dougherty, I. P. 146 Dihydroorotate oxidase 49 Douzou, P. 31,46,57,58 Dihydropicolinate reductase 49 Doweyko, A.M. 39, 185 Dihydropicolinate synthase 183 Dowhan, Jr., W. 184 Dihydroxyacetone-P 163 -165, Drent, G. 104 195-196 Drenth, J. 137 2,3-Dihydroxybenzoylserine Dreyer, W.J. 132 synthetase 220 Drysdale, G.R. 55 2-6-Dihydroxypyridine oxidase 51 Duba, C. 77 di Iasio, A. 164 Dube, S. 97, 112 Diller, A. 64 Dudding, W.F. 146 Dimethylaniline oxidase 51 Duez, C. 152 Dimethyl 2,4-dinitrophenyl phosphate, Dunathan, H.C. 86 hydrolysis 173 Duncan, R.J.S. 34,53 Dirnroth, P. 9, 167, 168 Duncombe, G.R. 75 2,4-Dinitrofluorobenzene, hydrolysis Dunford, H.B. 57 173 . Dunlop, P.C. 153 Dinovo, E.C. 177 Dunn, B.M. 11,94 Dionne, R. 110 Dunn, F.J. 56 Dioxygen, and catalase 18 Dunn, M.F. 35 Dipeptidylpeptidase 148 Dunstone, J.R. 116 Index 247

Dye, J.L. 36 Enolase 175-177,182 Dymowski,1.1. 131 activated water 177 magnesium ion as prosthetic group 176-177 E mechanism 176 -177 Enoylpyruvate transferase 107 Eady, R.R. 59 Enterokinase 148 Eagar, Jr., R.G. 178 Entsch, B. 30 Eager, Jr., R.G. 201 Enzymes, as Easterbrook-Smith, S.B. 215 energy reservoirs 21, 77, 133 Easterday, R.L. 162 energy transducers, 20, 132 Ebashi, S. 146 phase transfer catalysts 20 Ebel, J.P. 206, 207 22 Eberwein, H. 44 Erbes, D.L. 59 Eckstein, F. 102, 123 Eriksson, K.E. 53 Edelman, J. 110, 151 Eriksson, S. 46 Edlund, B. 98 Erman, J.E. 56 Edmondson, D. 31, 53, 54 Ernster, L. 46, 58 Edsall, J.T. 172, 173 Erwin, V.G. 54 Edstrom, R.D. 111 Erythrose-4-P 72 - 74 Eggerer, H. 9, 167, 168 Essenberg, M.K. 178 Egmond, M.R. 57 Estabrook, R.W. 46,58 Ehrenberg, A. 58 Ethanolamine ammonia-lyase 183 Ehrenfeld, E. 142 Ethyleneglycol 177 -179 Ehrlich, J.H. 184 Ettlinger, M.G. 151 Ehrman, M. 153 Evans, H.G. 102 Eichele, E. 57 Evans, H.1. 91 Eichele, G. 85 Evans, P.S. 129 Eid, P. 53 Evans, S.A. 35 Eisenberg, S. 198 Evans, W.R. 112 Eisenstein, L. 46 Eisenthal, R. 85 Eklund, H. 34 F Elastase 148 E1bein, A.D. 111 Fahn, S. 144, 146 Elce, J.S. 110 Falcone, A.B. 104 E1ey, M.H. 110 Farver, O. 41 Elion, G.B. 53 Fasella, P. 85 Elmore, D.T. 152 FaseIla, P.M. 57 Elmorsi, E.A. 58 Fasolio, F. 206 Elwell, M. 221 Fastrez, J. 133 Emi, S. 53 Favorova, 0.0. 204, 205 Endo, A. 111 Feder, 1. 136 Endo-l ,3-0:-D-glucanase 148 Feder, J.M. 124 Endothia acid proteinase 149 Fee, J.A. 58, 193 Engelhardt, L.M. 131, 173 Feigelson, P. 57 Engelman, D.M. 88 Feingold, D.S. 52, 110, 184 Englard, S. 164 Feldberg, R. 30 Engle, J.L. 112 Feldman, F. 121 Engstrom, L. 98,117,118,153 Feldmann, R.1. 112 Enoch, H.G. 53 Felton, R.H. 44, 57 248 Index

Femfert, U. 152 Fowler, F. 38 Fenner, H. 27 Fowler, L.J. 111 Fernley, H.N. 118 Franz, W. 115 Ferraz, J.P. 128 Freedman, T.B. 41 Ferredoxin-NADP reductase 52 Free energy relationships for single- and Ferredoxin-nitrite reductase 50 double-displacement catalysis 12 Ferreira, N. P. 54 Freer, S.T. 152 Fersht, A.R. 133, 206 Frere, J.M. 151, 152 Fetterolf, D. 110 Frerman, F.E. 54, 75, 113 Fewson, C.A. 55 Frey, P.A. 11,94,98, 100, 102, 110, Fibrinoligase 147 112, 178 Ficin 148 Fridborg, K. 173 Fiedler, F. 152 Fridovich, I. 39, 40, 56, 58 Fiero, M.K. 55 Friedman, S. 58 Finazzi Agro, A. 40,41,54,57 Friedmann, H. C. 54 Findlay, J.B. 134 Frigerio, N.A. 53 Findlay, T.H. 178 Frissel, W.R. 55 Fink, A.L. 126,137, 151, 152 Fritz, H. 152 Fink, N.Y. 143 Froede, H.C. 150 Finkle, B.J. 135 Froelich, J.P. 144 Finlay, T.H. 200 Fr~yshov, 0. 222 Fiori, A. 183 {3-o-Fructose 78-79 Firsov, L.M. 110 Fructose-1,6-diphosphatase 147 Fish, S. 151 Fructose 1,6-diphosphate 163-165 Fisher, H.F. 38 Fructose-diphosphate aldolase-class Fisher, J. 27,28, 154 I 163-165, 182 Fisher, R.R. 55 exchange reaction 165 Fishman, W.H. 151 mechanism 164-165 Flatmark, T. 58 Schiff base intermediates 164 - 165 Flavin, M. 185 Fructose-diphosphate aldolase-class Flavoenzymes 23-33,62-63 II 164, 165, 182 adenylylsulfate reductase 28 - 29 o-Fructose-6-P 72-74 o-amino-acid oxidase 23 - 27 Fruton, J.S. 115, 135, 137, 151 L-amino-acid oxidase 27 Frydman, R.B. 111 glucose oxidase 27 - 28 Fucose isomerase 200 lactate monooxygenase 28 - 29 Fucosyl-galactose N-methylglutamate synthase 62-63 acetylgalactosaminyltransferase 107 reduced, reaction with Fujii, S. 137 dioxygen 30-31 Fujikawa, K. 190 xanthine dehydrogenase 32 Fujimoto, A. 112 xanthine oxidase 31-32 Fujiwara, K. 109 Flohe, L. 57, 221 Fukami, H. 54 Floss, H.G. 172,185 Fukui, S. 53 Folk, J.E. 77,78 Fukunishi, K. 170 Forgac, M.D. 152 Fukushima, M. 151 Forget, P. 56 Fukuyama, M. 53 Formate acetyltransferase 106 Fulton, Jr., J.E. 150 Formate dehydrogenase (FMN) 49 Fung, C.-H., 215 Formate dehydrogenase () 49 Fung, M.J. 160 Forstrom, J.W. 57 Furneaux" H. 112 Foust, G.P. 30, 55 Futai, M. 53 Index 249

G Gellert, M. 201, 219 Genghof, D.S. 150 Gabriel, O. 184, 185 George, S.G. 151 Gadd, R.E.A. 81, 153 Georgopapadakou, N. 152 o-Galactal 126 Gershman, H. 34,52 Galactinol-raffinose Gertler, A. 152 galactosyltransferase 107 Gevers, W. 190, 191, 207, 221 Galactinol-sucrose Ghisla, S. 28, 30, 53 galactosyltransferase 107 Ghysen,I.M. 151, 152 ,B-o-Galactose 124-125 Giartosio, A. 85 a-o-Galactose-l-P 100-102 Gibbs, R. 144 Galactose-l- P Gibian, M.J. 57 uridylyltransferase 100-102, 108 Gibson, D. 152 exchange reactions 102 Gibson, Q.H. 53, 55, 56, 57 kinetics 102 Giesemann, W. 184 mechanism 101 Gillam, S.S. 153 retention of steric configuration on Gillard, B.K. 151 phosphorus 102 Gilmer, P.J. 112 uridylyl enzyme 101-102 Gilvarg, C. 185 a-Galactosidase 147 Ginodman, L.M. 138, 139 ,B-Galactosidase 124-127, 147 Giovagnoli, C. 40, 58 2-deoxygalactosylenzyme 126-127 Givot, T.L. 181 a-galactosylenzyme 125-126 Gladner,I.A. 152 mechanism 125-126 Glaser, L. Ill, 194,200 retention of steric configuration of Glazer, A.N. 135 carbon 124-125 1,4-a-Glucan branching enzyme 107 transferase activity 125 1,4-a-o-Glucan Galanopoulou, E. 124 6-a- o-glucosyltransferase 107 Galaway, R.A. 57 4-a-o-Glucanotransferase 107 Gaily, H.U. 214 Glucosamine-6-phosphate isomerase 199 Galsworthy, P.R. 144 o-Glucose 87 -90 Ganther, H.E. 57 ,B-o-Glucose 79-80 Garancis, 1. C . III Glucose dehydrogenase 49 Garces, E. 98 Glucose-l,6-DiP 97,99-100 Garfinkel, D. 110 Glucose-l,6-diphosphate synthase 97, Garland, P.B. 56 108 Garrett, C. 109 Glucose-6-phosphatase 121, 147 Garrett, R.H. 55, 56 exchange reactions, 121 Gastricsin 149 glucose-l-P 97 Gatehouse, 1. A. 198 phosphoenzyme 121 Gaucher, G.M. 152 transferase activity 121 Gay, P. 112 a-o-Glucose-l-P 78-80, 100-102 Gazzola, C. 181 o-Glucose-6-P 87-90 GDPmannose Glucose-6-P isomerase, hydride transfer a-o-mannosyltransferase 107 by 38-39, 199 G D Pmannose-phosphatidy l-myo-inositol Glucose oxidase 27-28,49 a-o-mannosyltransferase 107 ,B- o-glucose as substrate 27 Geary, P.I. 57 nitroethane anion as substrate 28 Gebb, C. 184 reconstituted with 5-deaza FAD 28 Gehring, U. 75 a-Glucosidase 147 Geller. D.M. 54 ,B-Glucosidase 147 250 Index

o-Glucoside 3-dehydrogenase 49 Goldberg, M. 41 f3-Glucuronidase 147 Goldberg, M.E. 185 Glusker, J.P. 184 Goldberg, M.1. 115 L-Glutamate 62-63 Goldberg, M.L. 184 158-160, 182 Goldman, D.S. 75 mechanism 158-160 Goldstein, M. 58 pyridoxamine-P 159-160 Gonzy-Treboul, G. 110 Schiff base intermediates 158-160 Good, N.E. 151 Glutamate synthase 49 Gorenstein, D.G. 134 Glutaminase 142, 149 Goryachenkova, E. V. 185 exchange reactions 142 Goto, T. 54 glutamyl enzyme 142 Goto, Y. 184 Glutamine-oxo-acid Gottikh, B. P. 204 aminotransferase 108 Gottschalk, G. 168 y-Glutamyl-cysteine synthetase 220 Gounaris, A.D. 100 y-Glutamyl phosphate 203 Gracey, R.W. 165 y-Glutamyltransferase 106 Gramicidin A synthetase 220 Gluthathione 39, 46-47 Gramicidin S 190,192,207 Glutathione-cystine Gramicidin S synthetase 220 transhydrogenase 46-47, 50 Graslund, A. 58 gl utathione-enzyme 46 - 47 Graves, DJ. 110 mechanism 46-47 Graves, J. L. 54 Glutathione, oxidized 46-47 Graves, P. V. 204 Glutathione peroxidase 51 Graves, S.W. 185 Glutathione reductase 47 -48, 50 Gray, A. 150 Glutathione synthetase 220 Grazi, E. 69, 73, 164, 184 o-Glyceraldehyde-3-P 70, 72-74, Green, J.R. 103 163-165, 195 -196 Green, S. 151 Glyceraldehyde-3-P dehydrogenase 49 Greenberg, L.B. 82 Glycerol dehydratase 182 Greenspan, M. D. 110 Glycerol-3- P dehydrogenase 49 Greenwood, C. 56 Glycine 64, 69 Greenzaid, P. 115 Glycine amidinotransferase 68-69, 106 Gregolin, C. 53 amidinated enzyme 69 Gregory, R.P.F. 58 exchange reactions 69 Gresser, M. 75 kinetics 69 Greull, G. 70, 156 Glycine synthase 106 Griffin, M. 58 Glycogen synthase 107 Griffin, W.G. 6, 110 Glycolate oxidase 49 Griffith, J. 198 Glycosyl-cation 18 Griffith,O.W. viii Glyoxalase 183 Grinnell, F.L. 212 Glyoxalase, hydride transfer by 39 Grisaro, V. 139 Glyoxylate carbo-ligase 182 Grisebach, H. 184 GMP synthetase 220 Grisham, C. M. 145 G MP synthetase Grisolia, S. 112, 198 (glutamine-hydrolysing) 220 Grabner, P. II 0 Godin, C. 138 Gross, M. 78 Goebel, R. 144 Grosskopf, W. R. 152 Goedde, H.W. 54 Groth, D.P. 81 Gaggel, K.-H. 54 Grubmeyer, C. 150 Goitein, R.K. 83 Grunberg-Manago, M. 112 Index 251

Guanidinoacetate 69 Hardman, M.J. 153 Guengerich, F.P. 58 Hargis,1.H. 43,57 Guggenheim, S. 185 Harington, 1.S. 221 Guidotti, G. 173 Harkness, D.R. 117 L-Gulonolactone oxidase 49 Harris, J.1. 53, 75, 166 Gumport, R.l. 219 Harrison, R. 85 Gundry, P. M. 5 Harting, 1. 53 Gunsalus, I.e. 46 Hartley, B.S. 131, 132, 152 Gunter, C.R. 136 Hartman, F.C. 165, 196 Gunter, H. 201 Hartman, S. 111 Gunter,1.B. 178 Hartman, S.C. 142,222 Gunther, S. 77 Hartree, E.F. 53, 152 Gunzler, W.A. 57 Hartsuck, 1.A. 129 Gupta, N.K. 34, 52 Haschemeyer, R.H. 54 Gupta, R.K. 145 Hasegawa, S. 151 Guseinov, F.T. 138 Hashimoto, H. 201 Gustafsson, I.-A. 46, 58 Hashimoto, T. 100 Gutfreund, H. 118 Hass, L.F. 121 Gutteridge, S. 31 Hassall, H. 185 Hasselbach, W. 146 Hassid, W.Z. 8,78,111 H Hastings, J.W. 31 Hata, T. 151 Haas, E. 55 Hatanaka, M. 185 Haas, W. 30 Hatano, H. 42 Haffner, P.H. 40 Havir, E.A. 180, 181, 185 Hager, L.P. 43,44,45,53,54,57 Hayaishi, O. 57,58, 151, 184 Hainline, B.E. 31 Hayano, K. 53 Hale, G. 6, 110 Hayashi, K. 56 Hall, A. 196 Hayashi, R. 151 Hall, C.L. 54 Hayes, Jr., LE. 53 Hall, R.L. 55 Haylock, S.J. 53 Hall, S.S. 39, 185 Hays,1.B. 91,112 Hall, Z.W. 219 Healy, M.J. 165 Halonbrenner, R. 85 Hearn, V. M. III Halpern, J. 15 Heath, E. e. 111 Hamilton, G.A. 158 Hedrick, 1.L. 153 Hamilton, L. 110 Hegeman, G.D. 193 Hamilton, M.D. 59 Hehre, E.J. 110, 111, 150 Hammarstrom, S. 152 Heidelberger, e. 109 Hammer, R.A. 142 Heinen, W. 54 Hammes, G.G. 6,85 Heinrich, e.P. 151 Hammons, G. 158 Heinrickson, R. L. 104, 184 Handler, P. 32,53,54,99,100,111, Heistand, R.H. 57 142 Heitmann, P. 143 Handschumacher, R.E. 153 Hell, R. 152 Hanke, T. 206 Hellerman, L. 54 Hansen, B.A. 184 Heimreich, EJ.M. 110 Hansen, J. 109 Heme enzymes 43-46 Hanson, K.R. 175, 180, 181, 185, 197 camphor 5-monooxygenase 45-46 Harbury, H.A. 53 catalase 43-44 252 Index

Heme enzymes (cant.) pyruvyl prosthetic group 160-161 chloroperoxidase 43 -45 Schiff base intermediates 160-161 peroxidase 43 -44 Histidinol-phosphate Hemmerich, P. 24,25,27,30,58 aminotransferase 108 Henderson, EJ. 184 Ho, P.P.K. 57 Henderson, 1. F. 81, 222 Hochstein, L.L 55 Hendrickson, H. R. 185 Hodgins, D.S. 180 Hengstenberg, H. 91, 112 Hodson, J. 112 Henkart, P. 173 Hoffee, P. 165, 184 Henkin, 1. 9 Hoff-Jorgensen, E. 111 Henry, A.C. 136 Hofmann, T. 138, 141, 153 Henson, C.P. 84 Hogenkamp, H.P.C. 58 Herbst, M.M. 201 Hogness, D.S. 194 Herlihy,1.M. 39, 196 Hogness, T.R. 55 Heron, E.J. 164 Hogstedt, S. 170 Herreid, R.M. 183 Hohne, W.E. 143 Hersh, L.B. 27,53,55,62,63,104, Hokin, L.E. 144 109, 153, 154, 221 HoI, W.GJ. 104 Hestrin, S. 110 Holland, M.J. 53 Hevesi, L. 28 Holland, P.e. 75 Hevey, R. 55 Hollebone, B.R. 55 Hevey, R.C. 123 Hollenberg, P. 43 Hexokinase 20,87-91, 108 Holler, E. 206 N-acetylglucosamine, inhibitor 89-90 Hollis D.P. 119 exchange reactions 88-89 Hollocher, T.C. 54 phosphoenzyme 87 - 90 Holloway, M.R. 153 steric inversion on phosphorus 87 Holmes, P.E. 58 triple displacement 87, 91 Holzapfel, C.W. 54 X-ray findings 90-91 Holzer, H. 54, 153, 156, 184 D-xylose, inhibitor 87-88 Homocysteine 61 Heymann, E. 153 Homoserine acetyItransferase 106 Heyse, D. 104 Hong, B.-H. 222 Hickey, M .. E. 120 Hooper, E.A. 6 Higgins, U. 58 Hopner, T. 53 Hildebrand, 1.G. 203, 210 Hopper, D J . 58 Hildebrandt, A.G. 58 Hopper, S. 111 Hill, A. 154 Horecker, B.L. 55,73,74,109,111, Hill, H.A.O. 166 164, 165, 184 Hill, R.A. 201 Horgan, D.1. 116 Himes, R.H. 222 Horiuti, Y. 53 Hinshelwood, C.N. 1,3,21 Horowitz, B. 222 Hirata, F. 57 Horton, H.R. 99, 100 Hiromi, K. 42, 151, 184 Hosoda, S. 56 Hirth, C. 53 Houchins, J.P. 52 Histamine 160-161 Houmard, J. 152 Histidine 160-161, 181, 207 -208 Houslay, M.D. 54 Histidine ammonia-lyase 181, 183 Hoving, H. 91 amino-enzyme 181 Howard, J.B. 153 metal ion as prosthetic group 181 Howell, L.G. 30,55 160-161, 182 Hrycay, E.G. 46,58 mechanism 160-161 Hsu, LN. 138 Index 253

Hsu, R.Y. 150 acetyl-enzyme 166-167 Hu, J.H.J. 53 a second acyl-enzyme Huang, J.S. 152 intermediate 167 Huang, S.-Y. 212 exchange reaction 166 Huang, T.C. 59 4- Hydroxy-4-methyl-2-oxoglutarate Huang, Y.Z. 184 aldolase 182 Hubbard, C.D. 134 6-Hydroxy-o-nicotine oxidase 50 Huber, R.E. 151 6-HydroxY-L-nicotine oxidase 50 Hubta, K. 54 Hydroxyproline epimerase 199 Hudgins, W.R. 185 Hylin, J.W. 113 Hudson, B. 55 Hypoxanthine Huebner, G. 54 phosphoribosyltransferase 107 Huneens, F.e. 75 Hunkapiller, M.W. 152 Hunneman, D.H. 123 I Hunt,1.B. 129 Huntley, T.E. 159 Igarashi, M. 120 Hurwitz, J. 112, 198,222 Iglestrom, M. 136 Husain, M. 30 Ihle, 1.N. 153 Hutchison, J.S. 35 Ikawa, M. 188 Huth, W. 75 Ikeda, B.H. 110 Hydride ion transfer, separation of proton Ikeda, J.-E. 198 from electrons 38-39 Ikura, K. 150 Hydrogenase 52 Ikuta, S. 53 Hydrogenation of ethylene 5 Illig, H.K. 151 Hydrogen dehydrogenase 51 Imae, Y. 190 Hydrogen peroxide, and catalase 18 Imagawa, T. 56 Hydrogen peroxide, coordination to metal Imai, Y. 55 ion in, Imamura, S. 53 catalase 43-44 Imidazoleacetate oxygenase 51 ceruloplasmin 42 Inagami, T. 87, 153 chloroperoxidase 43 Inamasu, M. 54 cytochrome c oxidase 42 Indoleamine 2,3-dioxygenase 51 laccase 41 Ingelman-Sundberg, M. 46, 58 peroxidase 43 Ingram, J. 151 superoxide dismutase 40 Inokuchi, H. 57 Hydroxonium ion 18 myo-Inositol-1-phosphate synthase 200 o-2-Hydroxyacid dehydrogenase 49 Inoue, H. 169 L-2-Hydroxyacid oxidase' 49 Inoue, K. 184 p-Hydroxybenzoate hydroxylase 51 Inouye, H. 54 flavin-oxygen adduct 31 Inulosucrase 106 5-Hydroxycamphor 45 Invertase 147 trans-p-Hydroxycinnamate 179-181 Ionized glycolaldehyde 70-71 5-(2-Hydroxyethyl)-4-methylthiazole 83 Iron coordinated to substrate in, 4-Hydroxyisophthalate hydroxylase 51 camphor 5-monooxygenase 46 4-Hydroxy-2-ketoglutarate aldolase 182 catalase 43-44 Hydroxylamine oxidase 50 chloroperoxidase 43, 45 Hydroxylamine reductase 50 cytochrome c oxidase 42 Hydroxymethylglutaryl-CoA lyase 182 peroxidase 43 3-Hydroxy-3-methylglutaryl-CoA Isherwood, F .A. 55 synthase 166-167, 182 Ishibashi, T. 111 254 Index

Ishimura, Y. 57 Jomain-Baum, M. 162 Isocitrate dehydrogenase 49 Jonas, R. 75 Isomaltase 147 Jones, M.E. 208 Isopentenylpyrophosphate isomerase 200 Jones, M.M. 129 Isophenoxazine synthase 51 Jones, S.R. 119 Itada, N. 113 Jones, T.L. 59 Itoh, T. 201 Jordan, F. 39, 185 Ives, D.H. 112 Jordan, P. M. 110 Iwasaki, H. 56 Joms, M.S. 27,53,63 Iwatsubo, M. 53 Jomvall, H. 53 Iyanagi, T. 55 Joshi, LG. 99 Joshi, V.c. 76,77 Jung, M.J. 111 J Jungermann, K.A. 110 Jurtshuk, P. 58 Jack, R.S. 166 Jutting, G. 222 Jackson, K.W. 153 Jackson, R. C. 153 Jacobs, E. 55 K Jacobson, B. 65 Jacobson, G.R. 110 Kaback, H.R. 53 Jaenicke, L. 61, 109, 184 Kafatos, F.C. 153 Jaffer, S. 131 Kagi, A. 88 Jagannathan, V. 99 Kahan, F.M. 111 Jakoby, W.B. 111 Kaiser, E.T. 112, 128, 141, 151, 152, James, M.N.G. 138, 153 172 Jameson, G.W. 152 Kakimoto, T. 181 Jansen, E.F. 132 Kakuda, Y. 110 Janson, C.A. 97, 143 Kalckar, H.M. 111,195 Jansonius, J.N. 85, 137 Kalk, K.H. 104 Jansz, H.S. 150 Kallen, R.G. 100, 102, 109 Jarup, L. 173 Kallikrein 148 Jeffcoat, R. 185 Kalyankar, G.D. 208 Jencks, W.P. 2, 13,74,75, 104, 109, Kambe, M. 190 115, 151 Kamin, H. 55, 56, 57, 58 Jenkins, LA. 110 Kanazawa, T. 144, 146 Jenkins, W.T. 64,84,111,112 Kandler, O. 111 Jenne, LW. 74 Kanfer, J.N. 151 Jerfy, A. 124 Kannan, K.K. 173 John, R.A. 111 Kapke, G. 184 Johnson, A.L 153 Kaplan, H. 152 Johnson, B.P. 119 Kaplan, M.M. 185 Johnson, F.A. 137 Kaplan, N.O. 38,55, 127 Johnson, Jr., J. 150 Karabatsos, G. L. 178 Johnson, LL. 31,56 Karabelnik, D. 85 Johnson, K. 151 Karasek, M. 204 Johnson, L.N. 110 Karkowski, A. M. 110 Johnson, P.E. 97 Karlsson, B. 42 Johnson, W.L. 153 Kashima, N. 184, 188 Johnston, R.B. 135, 188 Katagiri, M. 57 Jolles, G.R. 99 Katchalski, E. 137 Index 255

Katunuma, N. III Kieschke, K. 28 Katz, A.M. 146 Kijimoto, S. III Katzen, H.M. 56 Kikuchi, G. 109, 110 Kaufman, D.L. 152 Kilby, B.A. 132 Kaufman, S. 53, 58, 88 Killheffer, Jr., J. V. 136 Kauss, H. III Kilsheimer, G.S. 120 Kawahara, F.S. 197 Kimble, B.K. 110 Kawamura, M. 184 Kimura, K. 54, 57 Kazbekov, E.N. 56 Kimura, T. 58 Kaziro, Y. 222 Kindman, L.A. 119 Kearney, E.B. 54 Kingdon, H.S. 203 Keay, L. 53 King Sun, L.-H. 141 Keech, D.B. 162, 215 Kinoshita, N. 150 Keefe, M. 56 Kirby, E.P. 153 Keilin, D. 53 Kirby, G.W. 201 Keilova, H. 153 Kirchniawy, F.H. 110 Keirn, P. 104, 184 Kirkegaard, K. 198 Kelleher, M.H. 139 Kirkwood, S. 52,150,151,195 Kelleher, WJ. 184 Kirsch, J.F. 112, 134, 136, 151, 154 Keller, E. B. viii Kisselev, L.L. 204,205 Kelley, SJ. 122 Kitson, T.M. 53 Kelley, W.N. 81 Kjellen, K.G. 58 Kellogg, P.D. 55 Klapper, M.H. 135 Kemp, K.C. 133 Klein, H.W. 110 Kenimer, J .G. 81 Klein, S.M. 109 Kennedy, E.P. 99, 184 Kleinkauf, H. 190,191,207,221 Kenney, W.C. 55 Kleinschuster, 1.1. 150 Kenny, A.J. 151 Klingman, J.D. 142 Kenyon, G.L. 177, 193,222 Klinman, J. P . 201 Kershaw, D. 151 Klotz, I. M. 124 Kester, W.R. 153 Klug, D. 58 3-Ketoacid Co A-transferase 108 Kluger, R. 158 3-Ketoacid Co A-transferase , see Klug-Roth, D. 40, 58 Coenzyme A transferase Knaff, D.B. 56 2-Keto-3-deoxY-L-arabonate Knappe, J. 110, 222 dehydratase 182 Knappe, W.R. 30 5-Keto-4-deox y -D-glucarate Knappenberger, M.H. 137 dehydratase 182 Knowles, A.F. 146 monooxygenase 51 Knowles, J.R. 11, 19,39,87,91,92, Kettner, C. 153 97,112,119,138,141,154,196,198 Keyes, W.E. 57 Knowles, P.F. 31 Kezdy, F J. 136, 152 Kobes, R.D. 184 Khachatryan, L.L. 112 Koch, J. 184 Khailova, L.S. 54 Kochetkov, S.N. 112 Kharasch, N. 47 Kochi, H. 109 Khedouri, E. 112 Kochkina, L.L. 204 Khosla, S. 154 Koekoek, R. 137 Kido, T. 56 Koerber, S.C. 35 Kiefer, H.C. 124 Kohlhaw, G. 184 Kienle, M.G. 160 Kohn, L.D. 53 Kierstan, M. P.J. 137 Kokesh, F.C. 110 256 Index

Kolattukudy, P.E. 150 Kyle, W.S.A. 152 Kolb, H. 112 Kynureninase 149 Kolinska, J. 150 Komura, S. 221 Kornberg, A. 111, 198 L Kornberg, H. L. 91, 113 Kornberg, S.R. 111 Labat, J. 151 Kornblatt, J. 75 Labeyrie, F. 53 Kortt, A.A. 153 Labouesse, B. 204 Koshland, D.E. 2,79,99, 100,203, Labouesse, J. 204 222 Laccase 40-41, 51 Koval, G.1. 144, 146 mechanism 41 Kovaleva, G.K. 204, 205 reduction of oxygen to water 41 Koyama, T. 201 Lachance, J.P. 222 Kozarich, I.W. 152 Lactate dehydrogenase 49 Kozlov, L. V. 139 D-Lactate dehydrogenase 49 Kraemer, W.F. 99 Lactate-malate transhydrogenase 33, Kraevski, A.A. 204 49 Krakow, G. 54 Lactate mono oxygenase 28-29,51 Krampitz, L.O. 53, 70, 156, 183, 184 {3-chloro-L-lactate, elimination of Krasna, A.I. 59 HC1 28 Kraus, E. 152 glycolate, oxidation of 28-29 Kraus, R.J. 57 glycolyl enzyme 28-29 Kraut, J. 57, 152 L-lactate, decarboxylation of 28 Kredich, N.M. 185 reconstituted with 5-deaza FAD 28 Kreil, G. 210 shielded proton 28 Krenitsky, T. A. 111 Lactate racemase 199 Kreuzer, K.N. 201 S-Lactylglutathione 39 Krimsky, I. 53 Ladenstein, R. 57 Krisch, K. 115 La Du, B.N. 150 Krishnaswamy, P.P. 204 Lagunas, R. 89 Krodel, E. 24,178 Lagwinska, E. 146 Kroneck, P.M.H. 56 Lai, C.Y. 164,165 Krongelb, M. 185 Lai, H.Y.L. 151 Krouwer, I.S. 185 Lake, A.W. 135 Kubo, S. 150 Laki, K. 152 Kuhn, E. 73, 109 Lambeth, I.D. 54, 58 Kuhn, R. 150 Laminarinase 147 Kumagai, H. 54, 55, 184, 188 Lancet, D. 41 Kumar, A. 110 Landt, M. 122 Kume, S. 144 Lane, M.D. 162, 166, 167 Kumura, K. 57 Lane, R.S. 184 Kung, H.F. 201 Lang, G. 57 Kunitani, M.G. 109 Langdon, S.P. 102 Kunz, F. 201 Langenbach, R.J. 109 Kuo, C.H. 125 Lapworth, A. 16 Kuo, L.c. 131 Lardy, H.A. 215 Kurahashi, K. 190, 221 Large, PJ. 55 Kurosawa, A. 184 Lamer, J. 151 Kurz, G. 124 Larroque, C. 46, 58 Kusarnrarn, T. 184 Larson, K. 55 Index 257

Larsson-Raznikiewicz, M. 97 Liepnieks, 1.1. 152 Lathe, G.H. 111 Light, A. 152 Latt, S. A. 129 Liljas, A. 173 Laturaze, J.G. 98 Limburg, J.A. 52 Lau, S.J. 152 Lin, M. 200 Lauber, E. 58 Lindahl, S. 144 Laughter, A.H. 146 Lindahl, T. 222 Lauppe, H.F. 91,112 Lindenmayer, G.E. 146 Laursen, R.A. 157 Linder, R. 151 Law, J.H. 153 Lindmark, D.G. 110 Layne, P.P. 99, 100 Lindstrom, A. 55 Leaback, D.H. 151 Lipase 147 Lebar, R. 57 Lipmann, F. 54,74,110,112,118,146 Lederer, F. 52,53 190,191,207,208,221 Lee, B.H. 222 Lipoamide reductase 50 Lee, G.D. 124 Lipoate acetyltransferase 106 Lee, H. A. 34, 178 Lipoate succinyltransferase 106 Lee, N. 200 Lipoxygenase 51 Lee, S.G. 191 Lipoyl network 6 Lee, T.J. 153 Lippert, B. 160 Lee, T.T. 57 Lipscomb, J.D. 46,57 Lee, T.Y. 153 Lipscomb, W.N. 129 Lee, Y.C. 111 Little, C. 57 LeGall, J. 56 Little, J .W. 219 Legler, G. 151 Litwack, G. 111 Lehle, L. 111 Liu, L.F. 198 Lehman, J. 126 Liu, M.C. 56 Lehmann, I.R. 217, 219 Liu, T.Y. 153 Leigh, Jr., J.S. 19,42,177 Ljones, T. 58 Leininger, K.R. 104 Ljungdahl, L. 109 Leloir, L.F. 110 Ljungstrom, O. 170 Lenz, H. 168 Lo, K. 172 LePeuch, C. 31 Lo, S. 43 Lester, R.L. 53 Lobb, R.R. 166 Levansucrase 106 Lochmiiller, H. 65 Levenberg, B. 222 Lockridge, O. 28,57,150 Levin, Y. 137 Loeb, L.A. 112 Levintow, L. 203 Loehr, J.S. 41,57,58 Levitski, A. 222 Loehr, T.M. 41,57,58 Levulinic acid, 159-160 Lofqvist, B. 153 Levy, M. 153 Lolkema, J.S. 91 Levy, R.S. 52 London, J.W. 110 Lewis, S.D. 137 Long-chain fatty acyl-CoA Leyh-Bouille, M. 151 synthetase 212-214,220 Lhoste, J.-M. 53 adenylyl enzyme 212-214 Li, Y.T. 151 analogy with Co A-transferase Libertini, LJ. 150 action 212-214 Lichtenberger, F. 46 Co A-enzyme 212-213 Liebman, K. 58 comparison with acetyl-CoA Liener, I.E. 152 synthetase 214 Lienhard, G.E. 84 exchange reaction 212 258 Index

Long-chain fatty acyl-CoA synthetase Mahler, H.R. 53, 54, 55 (cont.) Main, A.R. 150 mixed anhydride Maister, S.G. 39, 196 intermediate 212 - 214 Maitra, U.S. 195 oxygen transferase activity 214 Maitre, M. 111 Lorand, L. 150, 152 Maki, Y. 58 Lorch, E. 222 Makinen, M.W. 128, 131 Lorimer, G.H. 55 Makino, R. 45 Losada, M. 55 Makinose, M. 146 Loschen, G. 57 Makita, A. III Louie, D.D. 55 Malakhova, E. A. III Lovgren, S. 173 Malathi, V.G. 222 Lowe, A.G. 144 Maleyl acetone ciS-frans-isomerase 199 Lowe, DJ. 32,56,58,59 Malhotra, O.P. 53, 125 Lowe, G. 19, 92, 102, 135, 136, 153 Malhotra, S.K. 197 Loyal, R. 9 Malkin, R. 41,56 Lu, T.H. 153 Mallaby, R. 168 Lucas, E.C. 136 Malmstrom, B.G. 40,41,42,54,58 Luciferase, bacterial, flavin-oxygen Malonyl-acyl-carrier-protein 76-77 adduct 31 Malonyl-CoA 76-77 Luck, J.M. 99 Malonyl-O-serine 77 Ludowieg, J. 54 Malthouse, J.P.G. 137 Lugay,I.C. 153 Malyl-CoA synthetase 220 Luminiferous aether 225 Manabe, N. 42 Lutsenko, N.G. 138 Manabe, T. 42 Lynen, F. 65,75,77, 110,222 Mandel, P. 111 D-a-Lysine 199 D- and L-Mandelate 192-194 f3-Lysine 5,6-aminomutase 200 Mandelate racemase 192-194, 199 D-Lysine 5,6-aminomutase 200 mechanism 193-194 L- Lysine 6-aminotransferase 108 a-pheny1glycidate, inhibitor 193 Lysine 2-monooxygenase 51 shielded proton transfer 193 D-a-Lysine mutase 199, 200 swinging arm 193 cobalamin as hydrogen carrier 199 Mangum, J.H. 61 Schiff base intermediate 199 Mann, D.R. 172 Lysophospholipase 147 Mannervik, B. 46, 55, 150 Lysozyme 147 Mannosephosphate isomerase 199 a-Lytic proteinase 148 a-Mannosidase 147 Manzocchi, A. 160 Mapson, L.W. 55 M Marble, S.I. 142 Marchesini, A. 56 Mabry, T.J. 151 Marcus, A. 184 MacGibbon, A.K.H. 53 Mar-dh, S. 144, 170 Mackenzie, C.G. 55 Maret, W. 35 Mackler, B. 53 Miirki, F. 56 Macnutt, W.S. III Markovetz, A.J. 58 MacQuarrie, R.A. 53 Markus, H.B. 102 Maggio, E. T. 193 Maroux, S. 152 Magnesium coordinated to substrate in Marquet, A. 197 enolase 176 - 177 Marshall. R.D. 111 Index 259

Marshall, T.H. 136, 152 Mehta, S. 172 Marshall, V. 46 Meister, A. 54,110,111,112,142,183, Martin, D.S. 85 203,204,208,210,221,222 Martin, J.C. 43,57 Mekhanik, M.L. 159 Martin, R.G. 111 Mela, L. 54, 111 Martinez, G. 184 Melander, W.R. 154 Martinez-Carrion, M. 112 Melilotate hydroxylase 51 Martius, C. 56 Mellman, W.J. 100, 102 Martonosi, A. 146 Meloche, H.P. 184 Maruyama, H. 162 Menezes, L.C. 87 Marx, M. 54 3- Mercaptopyruvate Mascaro, K. 172 sulfurtransferase 108 Mascaro, L. 185 Mercuric ion, effect on acetate kinase 90 Mason, H.S. 55, 58 Meriwether, B.P. 53 Massey, V. 24,27,28,30,31,32,47, Metaphosphate, monomeric, and 53, 54, 55, 57, 58 creatine kinase 19 Masters B.S.S. 55 pyruvate kinase 92 Masuda, H. 146 Metcalf, B.W. 111 Mather, 1. H. 54 Methionine 61 Mathison, R.D. 151 Methionine synthase, methyl enzyme 61 Matsubara, T. 56 4-Methoxybenzoate O-demethylase 52 Matsui, H. 55, 184 Methylamine 62-63 Matthews, B.W. 153 a-Methylaspartate 85-86 Matthews, D.A. 152 Methylaspartate mutase 200 Matthews, R.G. 30,48, 53, 54, 55 Methy1crotonyl-CoA carboxylase 221 Matveeva, L.N. 211 2-Methylene-glutarate mutase 200 Maurel, P. 46 5,10- Methy lenetetrahydrofolate Maxwell, E.S. 194 reductase 49 Maxwell, 1.c. 42,46 a-Methyl-DL-glutamate 159-160 May, Jr., S.C. 132 N-Methylglutamate 62-63 May, S.W. 57,141 N-Methylglutamate dehydrogenase 50 Maycock, A.L. 183 N-Methylg1utamate synthase 62-63, Mayer, H.R. 57 106 Mayhew, S.G. 30 glutaryl enzyme, 62-63 Maylie, M.F. 150 mechanism 63 Mazat, J.P. 204 methy 1amine-N -methy 19lutamate McBride-Warren, P.A. 153 exchange 62 McClure, W.R. 215 redox activity 62-63 McDonald, R.C. 88 shielded proton 62-63 McDonough, M.W. 200 Methylglyoxal 39 McFerran, N. 154 Methylhydroxypyridine-carboxylate McGrath, T.F. 142 dioxygenase 51 McHenry, C.S. 109 S-Methylmalonyl-CoA 65-67 McKean, M.C. 54 Methylmalonyl-CoA McLaughlin, A.C. 19 carboxyltransferase 106 Meany, F.E. 172 Methylmalonyl-CoA mutase 200 Medina, R. 201 N- Methyl-2-oxoglutaramate Meehan, P. 152 hydrolase 149 Meers, 1. L. 54 5-Methyl THF 61,63 Mehler, A.H. 203 Metridium proteinase A 148 260 Index

Metrione, R.M. 135 Mizobuchi, K. 222 Metzler, C. M. 85 Mizuchi, K. 201 Metzler, D.E. 85, 159, 188 Mizumoto, K. 112 Meussdoerffer, F. 153 Mizuno, N. 144 Meyer,O.M. 153 Mizusawa, K. 152 Michaelis-Menten complex, likeness to Model, P. 164 chemisorbed state 4 Modrich, P. 219 Michaels,O.B. 28, 102 Moe,O.A. 143 Michelakis, A.M. 153 Moffet, F.J. 211 Michelson, A.M. 112 Mohler, H. 55 Middleton, B. 75, 166 Molinari, R. 53, 55 Midelfort, C. F. 201, 203, 209 Moll, Jr., O.W. 112 Mihara, K. 57 Mondovi, B. 40,54,58 Mikeladze, D.O. 211 Moore, E.C. 55 Mikes, O. 152 Moore, K.W. 177, 178, 181 Mildvan, A.S. 19, 100, 112, 145, 162, Moore, S. 151 177, 178, 181, 184, 185, 193 Morgan, T. V. 56 Millen, W.A. 210 Mori, K. 190 Miller, C.O. 133, 136 Mori, Y. 57 Miller, J.C. 196 Moriguchi, M. 154 Miller, K.D. 152 Morino, Y. 170, 188 Miller, R.E. 54 Moriyama, A. 153 Miller, R.S. 162 Morley, C.O.D. 200 Miller, R.W. 54 Moroff, O. 55 Miller, S.L. 59 Moroz, S.O. 205 Miller, W.W. 201 Morpurgo, L. 40, 58 Milner, Y. 91, 102 Morris, D.B. 58 Milner-White, E.J. 19 Morris, D.R. 44,57 Milstein, C. 99 Morrison, A. 201 Minamiura, N. 151 Mortenson, L.E. 59 Minelli, A. 183 Mortlock, R.P. 201 Mintel, R. 104 Morton, R.K. 52 Misaka, E. 56 Motokawa, Y. 109 Misaki, H. 53 Mourad, N. 98 Misono, H. 112, 200 Muchmore, D.C. 35 Misono, K. 153 Muirhead, H. 201 Mitchell, C.H. 58 Muller, B. 152 Mixed carboxylic anhydride as Muller, F. 28, 30 intermediate, Muller, M. 150 A TP citrate lyase 170 Mullooly, J.P. 77 carboxypeptidase A 129-131 Mumford, R.A. 151 coenzyme A transferase 105 Munck, E. 57 long-chain fatty acyl-CoA Munck, E. 46 synthetase 212-214 Munk, P. 110 pepsin 140-142 Murachi, T. 153 tryptophanyl-tRN A synthetase 205 Murakami, K. 153 Mixed-function oxidase 51 Murayama, A. 207 Miyajima, R. 110 Muro, T. 184 Miyake, Y. 53 Muth, W.L. 185 Miyoshi, K. 57 Mutterties, E.L. 5 Miziorko, H.M. 166, 167 Mycek, M.J. 135 Index 261

N Negative evidence, use of 9 Neilsen, J. 89 Nachmansohn, D. 150 Neish, A.C. 181 NAD 127-128 Nelsestuen, G.L. 195 N ADase 127 -128, 148 Nelson, T.E. 151 ADPribosylenzyme 127 -128 Nester, E.W. 111 exchange reaction 127 Netter, K.J. 58 retention of configuration of Neujahr, H.Y. 58 carbon 128 Neumann, H. 117, 137, 139 transferase activity 128 Neumann, R. 55 NAD enzymes 33-38 Neurath, H. 132, 152 NADH dehydrogenase (FAD) 50 Newman, R. 85 NADH dehydrogenase (FMN) 50 Newmark, A.K. 141 NAD kinase 108 Newton, I. 21 NAD peroxidase 51 Nicholas, D.J.D. 55, 56, 112 NADPH-cytochrome reductase 50 Nicholls, R.G. 112 NADPH dehydrogenase 50 Nicotinamidase 149 NAD(P) transhydrogenase 50 Nicotine dehydrogenase 50 Nagai, S. 185 Niederman, R.A. 184 Nagano, H. 184 Niedermeier, R. 110 Nagano, K. 144 Niemann, R. 151 Nagate, T. 54 Nieto, M. 151 Nagelschneider, G. 24 Niewiarowski, S. 153 Nair, P.M. 56 Niimura, T. 55 Najjar, V.A. 99, 100 Nikolaeva, Z.K. 111 Nakagawa, H. 53 Nishigaki, I. 144 Nakagawa, Y. 141, 151 Nishimura, J.S. 183,210,212 Nakai, Y. 57 Nishimura, S. 111 Nakamoto, T. 103 Nishino, N. 153 Nakamura, T. 56,57 Nishino, T. 152 Nakamura, W. 56 Nitrate reductase (cytochrome) 51 Nakamura, Y. 146 Nitrate reductase (Mo,F-S) 50 Nakanishi, K. 56 Nitrate reductase (NADH) 50 Nakano, M. 54 Nitrate reductase [NAD(P)H] 50 Nakao, M. 144 Nitrate reductase (NADPH) 50 Nakao, T. 144 Nitrite reductase (cytochrome) 50 Nakaoka, K. 158 Nitrite reductase (FAD) 50 Nakatani, H. 184 Nitrite reductase ( c and d) 50 Nakazawa, A. 184 Nitrite reductase (NADPH) 50 Nakazawa, K. 57 p-Nitroacetanilide 74 Nakazawa, T. 91, 112 Nitroethane oxidase 50 Namihira, G. 110 Nitrogenase 52 Nandi, D.L. 110, 185 p-Nitrophenylester, substrate for, 2-Naphthyl phenylphosphonate 122 arylamine acetyltransferase 74-75 Narindrasorasak, S. 91 carbonic anhydrase 172 Narita, H. 150 carboxyl esterase 115 Nason, A. 55, 56 chymotrypsin 132, 134 Nastainczyk, W. 46 trans glutaminase 77 Naughton, M.A. 152 Nitrocatechol sulfate 123-124 Navon, G. 131, 172 4-Nitrophenyl phenylphosphonate 122 Nazarova, T.I. 143 Nixon, J.E. 77 262 Index

Noble, N.L. 150 Ohta-Fukuyama, M. 53 Noce, P.S. 162 Oi, S. 54, 104 Noller, H. 152 Okada, G. 110,150 Noncontiguous binding in covalent Okada, N. 111 catalysis 13-14, 94-96 Okada, S. III Nordin, I.H. 151 Okada, Y. 184 Nordlie, R.C. 121 Okamura, K. 109 Nordstrom, B. 34 Okayama, H. 151 Norman, A.W. 98 O'Leary, M.H. 52, 160, 183 Normore, W.M. 54 Olinescu, R. 57 Northrop, D.B. 66, 109 Oliva, A. 111 Notrand, B. 173 Olivard, I. 188 Novogrodsky, A. 183 Oliver, M. 146 Nowak, T. 177 Olivera, B.M. 219 Nozaki, M. 57,58 Olomucki, A. 57 Nucleoside deoxyribosyltransferase 107 Olson, I.S. 31 Nucleosidediphosphate kinase 98, 108 Olson, S. 53 Nucleoside phosphotransferase 108 Olsson, B. 55 5' -Nucleotide Olsson, P. 98 phosphodiesterase 122-123 Ong, E.B. 153 adenylyl enzyme 123 Onishi, H. 150 retention of steric configuration of Ooms, A.J.I. 150 phosphorus 123 Oosterbaan, R.A. 132 Nugent, M.J. 174, 175 Oppenheimer, N.J. 167 Numa, S. 222 Orcinol hydroxylase 51 Niissler, C. 110 Ordman, A.O. 52 Nygaard, A.P. 53 Orekhovich, V.N. 139 Nyns, E.J. 57 Orii, Y. 56 Orlowski, M. 110 Orlowski, R.C. 152 o Orme-Johnson, W.H. 54. 59 L-Ornithine 69 O'Brien, P.J., 57 D-Ornithine 4,5-aminomutase 200 Ochoa, S. 222 Ornithine cyclase 183 Ochs, R.S. 55 182 O'Connell, E.L. 39,66,175,184,196, Ornithine - oxo-acid 201 aminotransferase 108 Oda, Y. 41 Oro tate phosphoribosyltransferase O'Dea, M.H. 201 81-83,107 Oesper, P. 53 exchange reactions 82 Offerd, R.E. 196 kinetics 82 Ogata, K. 55, 184 phosphoribosyl enzyme 82-83 Ogura, K. 201 steric inversion on carbon, 81-83 Ogura, Y. 55, 56 triple displacement 83 Ohkishi, H. 184 Orotate reductase(NAD) 49 Ohlsson, A. 173 Orotate reductase(NADP) 49 Ohlsson, I. 34 Orotic acid, 81-82 Ohnishi, M. 151 Orotidylic acid, 81-82 Ohnishi, T. 57 Orr, G.A. 97 Ohnoki, S. 222 Orr, I.C. 185 Ohta, Y. 58 Orringer, B.P. 112 Index 263

Orsi, B.A. 154 Parsons, S.M. 83 Osaki, S. 58 Parvin, R. 121 Osborn, M.J. 111 Pascal, M. 127, 128 Oshimura, Y. 46 Patchett, A. A. 183 Oshinsky, C.K. 219 Patil, J.R. 33 Ostrowski, W. 120 Pauli, W.1. 129 O'Sullivan, W.J. 162 Paulus, H. 110 Otvos, J.D. 119 Pawlik, R.T. 32 Oxaloacetate 167, 168, 169 Payne, M. 53 3-0xyoacyl-[acyl-carrier-protein]- Payne, W.J. 56 synthase 106 Pazur,1.H. 111 3-0xo-5f3-steroid 114-dehydrogenase 49 Pearson, J.E. 175 Pearson, P.H. 210, 211 Pecci, L. 103 p Pecht, I. 41 Peck, E.J. 99 Pacaud, M. 152 Peck, Jr., H.D. 28,56 Pace, M. 56 Pedersen, P.L. 98 Pachowsky, H. 58 Peebles, C.L. 201 Page, M.A. 166 Peisach, 1. 58 Page, M.l. 13 Penefsky, H.S. 150 Pai, E.F. 47 Penicillinase 149 Pain, R.H. 154 Penicillopepsin 149 Palcic, M.M. 57 Pensa, B. 103 Palmer, G. 30,31,53,54,56 PEP-fructose-l-phosphotransferase 108 Palmer, J.L. 151 Pepsin 137-142, 148 Palmer, T.N. 151 acyl enzyme 140-142 Palmityl-CoA 212-214 amino-enzyme 13 7 - 140 Panet, R. 146 CoA-transferase, analogy with 139 Pangburn, M.K. 153 exchange reactions 137 Panteleeva, N.S. 146 mechanism 140-141 Pantothenase 149 mixed anhydride Paolella, P. 110 intermediates 140-142 Papadakis, N. 36 oxygen transfer 139 Papain 135-137,148 sulfite , as substrate 141-142 NU-carbobenzoxY-L-lysyl papain 137 transpeptidation reactions 137 -141 trans-cinnamoyl papain 136-137 Peraino, C. III kinetics 135-136 Perham, R.N. 6, 110 thiolate-imidazolium ion-pair in active Perkins, H.R. 151 site 137 Peroxidase 43-45,51 thionohippuryl papain 136 Perret, 1. 112 transamidations by 135 Petef, M. 173 Papaioannou, R. 111 Peterkofsky, A. 181 Park, J.H. 53 Peters, J. 110 Parker, A.J. 47 Peterson, J.A. 46, 55 Parker, M.J. 135 Petersson, L. 58 Parkhurst, J.R. 180 Petkov, D. 152 Park Kim, 1.-1. 54 Petrovskii, G.G. 56 Parks, Jr., R.E. 98, 221 Petterson, G. 55, 153 Parshall, G.W. 2 Pettet, F.H. 110 Parsons, P. 212 Pfenninger, o. 53 264 Index

Phenol 2-monooxygenase 51 phosphoglycerate phosphomutase 91 o-Phenylalanine 190-192 pyruvate, phosphate dikinase 91 L-Phenylalanine 179-180,205 Phosphoenolypyruvate-protein Phenylalanine phosphotransferase 108 ammonia-lyase 179-181, 183 Phosphoenolpyruvate synthase 108 amino-enzyme 180 - 181 99-100, 108 dehydroalanyl residue in catalysis 180 mechanism 99-100 exchange reactions 181 phosphoenzyme 99-100 kinetics 181 2-Phospho-o-glycerate 97,175-177, mechanism 180 197 transition metal ion as prosthetic 3-Phospho-o-glycerate 97, 197 group 180-181 Phosphoglycerate kinase 96-98, 108 Phenylalanine racemase 190-192, 199 phosphoenzyme 96 - 98 mechanism 191 - 192 steric inversion on phosphorus 97 phenylalanyl enzyme 191-192 197 -198, 200 shielded proton transfer 191 phosphoenzyme 197 -198 Phenyl alanyl adenylate 191,205-207 retention of configuration on Phenylaianyl-tRNA phosphorus 198 synthetase 205 - 207, 220 Phosphoglyceromutase 108 adenylyl enzyme 205 3-Phosphoglyceryl phosphate 96-97 exchange reactions 206 Phospho-2-keto-3-deoxygluconate phenylalanyl enzyme 205 - 207 aldolase 182 O-p-phenylazophenylphosphorothioate Phosphoketolase 182 118 Phosphonacetate 216 a-Phenylglycidate 193 Phosphoramidate-hexose .B-Phenylserine 64 phosphotransferase 108 Philipp, D.G. 212 Phosphoribosylformylglycinamide Philipp, M. 152 synthetase 220 Phillips, D.C. 150 5- Phosphoribosyl-1-pyrophosphate Phillips, G.T. 77 80-83 Phillips, R.S. 57 Phosphorylase 106 Phlogiston 225 Piccinini, F. 77 Pho, D.B. 57,91 Pickart, C.M. 109 Phosphatidylserine decarboxylase 182 Piette, L.H. 56 2-Phospho-3-butenoic acid 176 Pilz, W. 57 Phosphodiesterase I 147 Ping-pong kinetics, hybrid 66 (Z)-Phosphoenol-a-ketobutyrate 176 Pinkus, L.M. 112 Phosphoenolpyruvate Pisareva, L.N. 146 carboxykinase 162-163, 182 Pizer, L.1. 112, 197 coordination of substrates to Plasmin 148 Mn 162-163 Plate, C.A. 77 exchange reactions 162-163 Platzer, K.E.B. 54 mechanism 162-163 Ploegman, 1.H. 104 phosphoenzyme 163 PM-3-chloropyridinium 83-84 pyruvyl-enzyme intermediate 162 PM-quinoline 83-84 Phosphoenolpyruvate, phosphoryl donor Pocker, Y. 172, 173 to, Pogolotti, A.L. 109 alkaline phosphatase 91 Pojarlieff, 1. 152 PEP-histidinoprotein Polgar, L. 137 phosphotransferase 91 Pollock, 1.1. 151 PEP synthase 91 Pollock, R.J. 62 Index 265

Polymyxin synthetase 220 Purich, D.L. 92, 93 Pompon, D. 53 Putidaredoxin 45 Ponticorvo, L. 164 Putnam, E.W. 78 Pontoni, G. 111 Putrescine oxidase 50 Pontremoli, S. 74 Pyridoxamine-oxaloacetate Porteous, J.W. 151 transaminase 108 Porter, D.J.T. 24,25,28,53,54,56, Pyridoxamine-pyruvate 111 transaminase 108 Porter, J.W. 77, 201 Pyrithiamine 83 - 84 Portsmouth, D. 185 Pyrocatechase 51 Post-proline cleaving enzyme 148 Pyrophosphatase (inorganic) 143-144, Post, R.L. 144, 146 149 Potts, R. 172, 185 Pyrophosphate, hydrolysis by, Poulos, T. L. 57 acid phosphatase 120, 143 Poulson, L.L. 58 alkaline phosphatase 118, 143 Powers, J.C. 153 glucose-6-phosphatase 121, 143 Pradel, L.-A. 91, 97 Pyrrol-2-carboxylate 188-190 Prakash, O. 56 Pyruvate carboxylase 215-217,220 Prasher, D. C. 112 ADP-ATP exchange 217 Presswood, R.P. 56 biotin as CO2 carrier 215 Prestegard, J.H. 214 carbamyl-P, as substrate 216 Prihar, H.S. 52 carboxy enzyme 215-216 Prince, R.H. 173 kinetics 215, 217 D- and L-Proline 188-190 phosphoenzyme 216-217 Proline racemase 188-190, 199 phosphonacetate, as inhibitor 216 mechanism, 189-190 swinging arm 215-216 pyrrol-2-carboxylate, 155-156, inhibitor 188 - 190 182 Propanediol 177 - 178 mechanism 155-156 Propanediol dehydrase 177 - 179, 182 Pyruvate dehydrogenase cobalamin as hydrogen (cytochrome) 49 carrier 178 - 179 Pyruvate dehydrogenase 6-7,49 free radicals in catalysis 178 Pyruvate kinase 91-92 mechanism 177 - 179 metaphosphate, as intermediate 92 shielded proton transfer 178 oxygen scrambling by 92 Propionaldehyde 177 -178 steric inversion on phosphorus 92 Propionyl-CoA 65 -67 triple displacement 92 Propionyl-CoA carboxylase 220 Pyruvate, orthophosphate Protease I 148 dikinase 102-103, 108 Protease VI of Mucor miehi 149 exchange reactions 103 Proteinase A 149 phosphoenzyme 102 - 103 Proteinase K 148 pyrophosphoenzyme 102 -103 Protein-disulfide reductase 50 Pyruvate oxidase 49 Protein kinase 108 Pyruvate synthase 49 Prothrombinase 148 Protocatechuate 3,4-dioxygenase 51 Pseudorotation 94 Q Pudles, J. 87 Pugh, E.L. 165 Que, Jr., L. 57 Pullman, M.E. 99 Quenelle, A.C. 154 Purdy, R.E. 150 Quinoline 83-84 266 Index

Quinone reductase 50 Retey,1. 54, 178,201 Quiocho, F.A. 129 Rhodanese 103-104, 108 exchange reaction 104 kinetics 104 R sulfur-enzyme intermediate 103-104 Ribbi, A. 128 Rabani,1. 40, 58 Ribbons, D.W. 58 Rabate, M.J. 151 Ribereau-Gayon, G. 165 Rabinowitz, J.e. 54 Ribonucleoside-diphosphate Rabinowitz, K.W. 184 reductase 52 Race, e. 111 Ribonucleoside-triphosphate Racker, E. 53,70,74,109, 146, 184 red uctase 52 Raffin, 1. P. 207 o-Ribose-5-P 70-71 Raftery, M. A. 150, 151 Ribose 5-phosphate adenylyl Raghavan, S.S. 151 transferase 108 Rajagopalan, K.V. 31,32,53,54,56, Ribosephosphate isomerase 199 57 Ribulosephosphate 3-epimerase 199 Ramakrishna, S. 170 L-Ribulosephosphate 4-epimerase 199 Ramaley, R. 98 Ricci, C. 74 Rand-Meir, T. 45, 150, 151 Richard,1.P. 11,94,98, 112 Rando, R.R. 112 Richards, E. G. 167 Rapoport, G. 110 Richards,1.H. 152, 177, 178,201 Rapoport, S. 143 Richards,1.W. 197 Rapoport, T.A. 143 Richardson, C.C. 222 Rasheed, A. 201 Rickert, W.S. 153 Rask, L. 98 Riddle, B. 74 Rasmussen, 1.R. 152 Ridley, W.P. 52 Rasool, G. 184 Rieder, S. V . 165, 196 Ratner, S. 69 Riepe, M.E. 173 Raw, I. 55 Riepertinger, C. 65, 75 Ray, Jr., W.1. 99, 100 Rigo, A. 40, 58 Recsei, P.A. 161 Riley, W.D. 161 Redlington,1.W. 143 Rilling, H.C. 201 Redmond, 1.W. 168 Ringelmann, E. 222 Reed, D. 80 Ringler, R.L. 53 Reed, LJ. 6, 54, 110 Ringold, H. 1. 197 Reed, T.A. 184 Riordan,1.F. 165, 166 Reed, W.D. 166 Ritchie, G.A.F. 56 Reeke, Jr., G.N. 129 Rittenberg, D. 59, 133, 164 Rees, M.K. 56 Rittenberg, S.C. 58 Reichard, P. 55, 58 Ritter, E. 77 Reichel, K.B. 93 Rix, H. 153 Reid, K.G. 57 tRNAPhe.

Reingold, I.D. 183 3 I -deox y 206 Reinhammar, B. 41, 56 periodate-oxidized 206 Relyea, N.M. 183 RN A ligase 221 Remy, P. 206,207 tRNA transglycosylase 107 Rendina, A.R. 54 Robbins, K.e. 152 Renin 149 Roberts, D.V. 152 Rennin 149 Robertus, 1.D. 152 Resorcinol hydroxylase 51 Robillard, G.T. 91 Index 267

Robins, DJ. 201 Rutter, W.J. 164, 184 Robinson, J.C. 53 Ryan, G. 221 Robinson, J.L. 210 Robinson, W.G. 34,52 Robyt, J.F. 110 s Rocca, E. 54 Roche, R.S. 152 Sachse, E. 152 Roche, T.E. 6,54, 110 Sachsenheimer, W. 47 Rochovansky, O. 69 Sad ana , J. C. 56 Roddy, P.M. 144 Sagers, R.D. 109 Rodnight, R. 144 Saito, M. 144 Roe, A.L. 57 Sakamoto, Y. 190 Roeser, K.R. 151 Salicylate hydroxylase 51 Roeske, R. W. 136 Salton, M.R.J. 151 Rogers, F.N. 146 Sampaio, S. 152 Rogers, P. 85 Sands, R.H. 54 Romano, M. 34 Sanger, F. 99, 152 Ronca, G. 69 Sanny, C.G. 53 Ronchi, S. 55 San Pietro, A. 38, 112 Roon, R.J. 153 Santaniello, E. 160 Roscelli, G. A. 100 Santi, D.V. 109,203 Rose, LA. 39,66,89,90,97,112,165, Santiago, D. 52 175,184,196,197,200,201 50 Rose, S.P.R. 144 50 Rose, Z.B. 97, 112, 197 Sarkanen, S. 173 Roseman, S. 91, 112 Saronio, C. 42 Rosen,O.M. 184 Sarton- Miller, I. 209 Rosenberg, S. 151 Sasaki, R. 150 Rosenfeld, LS. 110 Sashchenko, L.P. 112 Rosenthal, A.S. 144 Sastry, P.S. 144 Rosenthal, O. 58 Sato, E. 190 Roskoski, Jr., R. 207, 221 Sato, K. 178, 185 Ross, M.E. 110 Sato, R. 53,56 Rossi, N. 69 Sato, S. 201 Rosso, R.G. 184 Satre, M. 184 Roszell, J.A. 185 Satterthwait, A. 19 Rothfield, L. 111 Sawatzki, G. 57 Rotilio, G. 40, 54, 58 Scarborough, G.A. 150 Roustan, C. 91, 97 Scarpa, LS. 124 Rowley, P.T. 73, 164 Schabort, J.C. 54 Roy, A.B. 123,124 Schack, P. 35 Rubenstein, P.A. 58 Schaffer, N.K. 132 Rubredoxin-NAD reductase 52 Schiessler, H. 152 Ruch, F.E. 76 Schiff base formation by, Rudiger, H. 61, 109 acetoacetate decarboxylase 17, Rudney, H. 75, 166 157 -158 Rudnick, G. 190 acetyl-CoA acetyltransferase 75 -76 Rueger, D. C. 56 alanine racemase 186-188 Rumsh, L.D. 138 ami~o acid decarboxylases 17 Russell, 1. 104 aspartate aminotransferase 84 - 86 Rutter, R. 57 dehydroquinase 174-175 268 Index

Schiff base formation by, (cont.) Semeriva, M. 97,150 fructose diphosphate Sen, A.K. 144, 146 aldolase 164-165 Sepulveda, P. 153 glutamate decarboxylase 158-160 L-Serine 64 histidine decarboxylase 160-161 o-Serine dehydratase 182 o-o:-lysine mutase 199 Serine hydroxymethyltransferase 63-65, serine hydroxymethyltransferase 63 -65 106 transaldolase 72-74 glycyl enzyme 64 170-171 mechanism 64-65 Schirch, L. 64 Seubert, W. 75 Schirmer, R.H. 47 Severin, E.S. 112, 211 Schleicher, E. 172, 185, 201 Seydoux, F. 53 Schlesinger, P. 104 Shadrin, V.N. 56 Schleuning, W.D. 152 Shafer, J.A. 137 Schleyer, H. 58 Shah, D.H. 201 Schmidt, Jr., D.E. 157 Shah, V.K. 59 Schmitt, T. 110 Shannon, L.M. 184 Schnabel, K.H. 58 Shapiro, S.S. 200 Schnackerz, K.D. 184 Sharon, N. 139, 151 Schobert, B. 111 Sharp, S.L. 166 Schoellmann, G. 153 Sharp, T.R. 193 Schonbrunn, A. 24, 28, 54 Sharpe, T.S. 134 Schonbrunn, G.R. 43 Sharrock, M. 46 Schopfer, L.M. 30 Shaw, D.C. 152 Schramm, V.L. 162 Shaw, E. 152, 153 Schray, K.J. 19 Shaw, L.M. 110 Schrecker, O. 91,112 Shaw, P.J. 201 Schroeder, D.D. 222 Sheard, B. 119 Schropfer, L.M. 57 Shedlarski, J.G. 185 Schroter, E. 126 Shemin, D. 110, 185 Schroter, W. 184 Shen, T.Y.S. 177 Schuler, F. 127, 128 Shepherd, G.B. 6 Schulman, M. 113 Shepherd, J.B. 221 Schultz, G.E. 47 Shetlar, M.R. 151 Schumann, M. 30 Sheu, K.-F.R. 11,94, 98, 102 Schutzbach, J.S. 111,184 Shibasaka, M. 156 Schwartz, A. 146 Shibatani, T. 181 Schwartz, J.H. 118, 153 Shigekawa, M. 146 Schweitzer, E. 77 Shiio, I. 110 Scott, E. M. III Shimada, H. 56 Scrutton, M.C. 215,217 Shimada, K. 54 Sedmark, J. 98 Shimamoto, N. 134 o-Sedoheptulose-7-P 70, 11 Shin, M. 58 Segal, H.L. 53,111, 121 Shindler, J.S. 55 Seibl. J. 178 Shinomura, T. 151 Sekura, R. 221 Shinra, M. 56 Selinger, Z. 146 Shipton, M. 137 Sellers, H.W. 183 Shizuta, Y. 184 Sellers, L. 185 Shkarenkova, L.S. 139 Seltzer, S. 200 Shoham, M. 90 Semenza, G. 150, 151 Shore, J.D. 35, 52 Index 269

Shortie, D. 167 Solomonson, L.P. 55 Shotton, D.M. 152 Sols, A. 89 Shulman, R.G. 131 Somack, R. 201 Shuman, S. 112 Somova, V. V. 138 Siegel, GJ. 146 Sone, N. 53 Siegel, L.M. 56 Sorbo, B. 104 Silber, R. 222 Sorm, F. 152 Silver, M.S. 139 Souchard,I.1.L. 126 Silverman, D.N. 173 Soucie, W.G. 150 Silverman, R.B. 185 Sparrow, L. G. 57 Silverstein, R.M. 43,57,80 Spartalian, K. 57 Simmons, W.H. 151 Speckhard, D.C. 110 Simon, H.S. 201 Spector, L.B. vii, 11, 12,60,88,92,93, Simoni, R.D. 91,112 169, 203, 204, 208, 210 Simpson, I. 150 Spector, T. 30, 57 Singer, T.P. 53, 54, 55 Spencer, A.K. 214 Singh, M. 167 Spencer, R. 27,28 Single-displacement catalysis, possibility Spermidine dehydrogenase SO of 226 Spermidine synthase 107 Sinnott, M.L. 126 Sperow,l.W. 143 Sireix, R. 57 Spiegel, MJ. 55 Sizer, F. W. 84 Springate, C.F. 112 Sizer,I.W. 53 Sprinson, D.B. 133 Sjoberg, B.-M 58 Sproat, B.S. 19,92 Skotland, T. 58 Spronk, A.D. 103 Skvortsevich, E.G. 146 Sramek, S.l. 113 Skye, G.E. 185 Srere, P.A. 167, 168,170 Slater,l.P. 112 Srinivasan, P.R. 184 Slaughter, C. 185 Stadtman, E.R. 54 Sloan, D.L. 82, 112 Stadtman, T.C. 200,201 Smallcombe, S.H. 152 Stahl, W.L. 146 Smart,l.W. 144 Stambolieva, N. 153 Smith, B.E. 58 Staphylococcal serine proteinase 148 Smith, E.L. 135 Starch (bacterial glycogen) synthase 107 Smith, G.D. 85 Stark, MJ. 55 Smith, R.A. 112, 121 Staudinger, H. 58 Smith, R.L. 152 Staunton, 1. 180 Smith, S. 150 Stavrianopoulos, 1. 61 Smith, S.B. 197 Steenkamp, DJ. 54,55 Smith, T.A. 181,185 Steeves, T. 112 Smith, Z.G. 111 Stein, R. 91, 112 Snell, E.E. 57, 84, 86, 112, 158, 161, Stein, W.H. 151 170, 183, 184, 188 Steinberg, M.S. 74 Snipes, C.E. 185 Steinberger, R. 66 Snoke, I.E. 221 Steinschneider, A. 203 Soberano, M.E. 153 Steitz, T.A. 20, 88, 90 Soda, K. 56, 112, 154, 200 Stenberg, P. 150 Sodek, 1. 138, 153 Stenesh, 1 J. 207 Soderhiill, S. 222 Steric configuration of carbon, inversion by, Soderlund, G. 34 adenine phosphoribosyltransferase 10, Solomon, F. 66, 89, 109 80-81 270 Index

Steric configuration of carbon, inversion Strandberg, B. 173 by, (cant.) Strange, P.G. 180 orotate phosphoribosyltransferase 81-83 Streptococcal proteinase 148 sucrose phosphorylase 8-9, 79-80 Streptomyces griseus proteinase 149 Steric configuration of carbon, net Strickland, S. 30, 57 retention by, Strittmatter, P. 55 ,B-galactosidase 124-125 Strobel, H.W. 55 NADase 128 Strominger, J.L. 58, 152 sucrose phosphorylase 8-9, 79-80 Str\iJmme, J.H. 110 Steric configuration of phosphorus, Strothkamp, R.E. 42 inversion by, Strumeyer, D.H. 221 acetate kinase 92 Stubbe, J. 176, 177 acetyl-CoA synthetase 209 Stuchbury, T. 137 ATPase 147 Stura, E.A. 110 hexokinase 87 Sturtevant, J.M. 52 phosphoglycerate kinase 97 Su, S. 153 pyruvate kinase 92 SubbaRao, P.V. 181 Steric configuration of phosphorus, Subramanian, E. 153 retention by, Substrate synergism 162, 212 alkaline phosphatase 119 Subtilisin 148 galactose-I-phosphate Succinate dehydrogenase 49 uridylyltransferase 102 Succinyl-CoA 104-106, 209-212 nucleosidediphosphate kinase 98 Succinyl-CoA synthetase 92, 209-212, 5'-nucleotide phosphodiesterase 123 220 phosphoglycerate mutase 198 exchange reaction 211-212 Steric inversion on phosphorus and covalent kinetics 211 catalysis 10-11 mechanism 210-211 Stem, A.I. 112 phosphoenzyme 210-211 Stem, E. 16 subunits 211 Steroid ~-isomerase 1%-197,200 succinyl enzyme 210-211 mechanism 197 succinyl phosphate 210-211 shielded proton transfer, 197 Succinyl-CoA synthetase steroid 11,B-monooxygenase 51 (GDP-forming) 220 Stesina, L.N. 185 Succinyl phosphate 92,203,210-211, Stevanato, R. 58 214, 216 Stevens-Clark, J.R. 112 Succinic thiokinase 89; see Stewart, P.R. 166 Succinyl-CoA synthetase Stiefel, E.I. 32 Sucrose 78-80 Stockell, A. 135 Sucrose a-glucohydrolase 148 Stocker, K. 153 Sucrose-phosphate synthase 107 Stoddard, M. 139 Sucrose phosphorylase 8-9,78-80,106 Stoinova, I. 152 exchange reactions 78 Stokes, A.M. 166 ,B-glucosyl enzyme 8, 78-80 Stokes, T.M. 126 inversion and net retention of steric Stone, B.A. 151 configuration 8-9, 79-80 Stone, J.T. 172 mechanism 79 StoolmilJer, A.C. 185 mode of action in single- and double- Stoops, J.K. 116, 136 displacement catalysis 12-13 Storm, C.B. 129 Sucrose synthase 107 Stotter, D.A. 31 Sudbury, Jr., J.B. 99 Straat, P.A. 56 Suelter, C.H. 36 Index 271

Suga, K 151 Swoboda, B.E.P. 28, 53 Suganuma, T. 151 Synzyme 124 Sugimoto, E. 150 Sugino, A. 201 Sukhareva, V.S. 159 T Sukhodolova, A. T. 56 Sulfate adenylyltransferase 108 Tabor, C.W. 55 Sulfite 103-104 Tagaki, W. 158 Sulfite oxidase 50 Takahashi, H. 120, 190 Sulfite reductase 50 Takahashi, K. 56, 153 Sulfite reductase (NADPH) Takahashi, M. 141 Sullivan, P.A. 30, 57 Takamura, F. 55 Suitones, hydrolysis 172 Takeda, H. 57 Summaria, L. 152 Takeda, Y. 169,170 Summer, W.H. 132 Takemori, S. 57 Sundaram, T.K. 57 Talalay, P. 54, 197 Sung, S.-J. 167 Talmadge, P. 110 Superoxide dismutase 39-40,52 Tamir, H. 184 cyanide ion, as inhibitor 40 Tamir, 1. 112 hydrogen peroxide, coordination 40 Tamiya, N. 59 mechanism 40 Tamura, G. 56 superoxide ion, as substrate 40 Tamura, M. 57 Surface walk 4-6, 14 Tamura, S. 57 Surface walk, on, Tanabe, T. 184 acetate kinase 11, 96 Tanaka, A. 151 adenine phosphoribosyltransferase 10, Tang,J. 138,153 82-83 Taniguchi, H. 110 ATP citrate lyase 170 Taniguchi, K. 146 chymotrypsin 134-135 Tanioka, H. 169 metal catalyst 4-5 Tanizawa, K. 154 orotate phosphoribosyltransferase 83 Tanner, S.J. 31 pyruvate dehydrogenase 6-7 Tanner, W. 111 tryptophanyl tRNA synthetase 205 Tappel, A.L. 57 Surks, M. 112 Tarkan, E. 150 Sutton, W.B. 57 Tartakoff, A.M. 153 Suva, R.H. 55 Tashima, Y. 144 Suzuki, A. 57 Tashjian, A.H. 151 Suzuki, F. 169, 170 Tate, S.S. 110, 183 Suzuki, H. 55, 110 Taylor, M.L. 57 Suzuki, 1. 56, 70, 156 Taylor, R.T. 61,109, 112 Suzuki, K. 57 Tchola, O. 73, 164 Suzuki, T. 56 dTDPglucose 4,6-dehydratase 182 Swan,1.D.A. 153 Tedesco, T.A. 100, 102 Swann, J.C. 31 Tempest, D.W. 54 Swanson, A.L. 111 Templeton, D.M. 55 Sweeley, C.C. 167 Tetrahydropteroylglutamate Swen, H.M. 137 methyltransferase 106 Swinging arm, use of by, Thauer, R.K. 110 mandelate racemase 193 Thelander, L. 55, 58 pyruvate carboxylase 215-216 Theodersen, L. 110 transcarboxylase 66, 68 Theorell, H. 43, 57 272 Index

Thermolysin 149 Tortora, P. 153 Thermomycolase 148 Tosi, L. 54 Thermophilic Streptomyces alkaline Tot, A.N.T. 91 proteinase 148 Toulouse, E. 110 Thiamine 83 Touster, O. 151 Thiaminase I 83-84, 107 Towers, G.H.N. 181 ( 4-amino-2- methy 1-5-pyrimidiny I) Transaldolase 72-74, 106 methyl enzyme 84 dihydroxyacetonyl-enzyme 73 -74 maximal velocity kinetics 84 mechanism 73 -74 Thiebe, R. 206 Transcarboxylase 65-68, 106, 211, 103-104 216 Thioglucosidase 148 biotinyl subunit 65 Thiolase, see Acetyl-CoA acetyl transferase carboxyl-enzyme 65 -68 Thionohippurate, methyl ester, 136 hybrid ping-pong kinetics 66 Thioredoxin reductase 48, 50 mechanism 65-68 Thiosulfate 103 -104 role of cobalt 67 Thomas, C.B. 81 swinging arm 66, 68 Thomas, I.A. 57 Transglutaminase 77 -78, 106 Thompson, A. 222 exchange reactions 78 Thompson, C.P. 151 kinetics 78 Thompson, R.C. 153 trimethylacetyl enzyme 77 -78 Thomeley, R.N.F. 59 Transketolase 69-72, 106 Thorpe, C. 48, 54, 55 a ,{3-dihydroxyethyl-TPP-enzyme Three-body interaction in 70-72 catalysis 13-14,96 exchange reaction 72 Threonine dehydratase 182 mechanism 70-72 Thrombin 148 Trapnell, B.M.W. 5 Thrombocytin 148 Trautwein, A. 53 Thymidylate synthase 106 Travers, F. 57 Tietze, F. 56 Travo, P. 127, 128 Tikhodeeva, A.G. 138 Treboul, G. 110 Tipton, K.F. 34, 54 a,a-Trehalase 147 Titovets, E.P. 56 a,a-Trehalose-phosphate synthase 107 Titus, E. 144 a,a-Trehalose-phosphate synthase Toan, N.B. 152 (GDP-forming) 107 Tobin, T. 146 Trentham, D.R. 97, 150 Toda, G. 146 Trimethylamine dehydrogenase 50 Todhunter, 1.A. 92, 93 Triosephosphate isomerase 195-196, Tokieda, T. 55 199 Tokushiga, M. 184 Triple-displacement catalysis by, Tolosa, E.A. 185 acetate kinase 11, 92 - 96 Tomioka, S. 151 acetyl-Co A synthetase 209 Tomizawa, I. 201 adenine phosphoribosyltransferase Tompkins, F.C. 5 82-83 Tompkins, G.M. 185 hexokinase 87 Tonomura, Y. 144, 146, 150 orotate phosphoribosyltransferase 83 Topper, Y.I. 165 phosphoglycerate kinase 97 Toraya, T. 178 pyruvate kinase 92 Torchinskii, Yu. M. 111, 159 Triple-displacement catalysis, Torii, H. 184 definition 6 Index 273

Trombetta, G. 164 u Trotta, P.P. 54 Trudgill, P.W. 58 Udaka, S. 54 Truitt, C.D. 222 UD Pacety Igalactosamine-globoside Trusted, J. 226 a-N-acetyl- 0-galactosaminyltrans• Trypsin 148 ferase 107 L-Tryptophan 203 - 204 UDPacetylgalactosamine-protein Tryptophanase 170-172, 182 acetylgalactosaminyltransferase 107 mechanism 170-172 UDP-o-apiose synthase 182 Schiff base intermediates 170-171 UDPgalactose 100-101,194-195 shielded proton transfer 172 UDPgalactose-sn-glycerol-3-phosphate Tryptophan 2,3-dioxygenase 51 galactosyltransferase 107 Tryptophan synthase 182 U D Pgalactose-lipopol ysaccharide Tryptophanyl adenylate 203-204 galactosyltransferase 107 Tryptophanyl-tRN A U D Pgalactose-tetragl ycosylceramide synthetase 203-205,220 a-o-galactosyltransferase 107 adenylyl enzyme 204 U D Pgalacturonate-polygalacturonate mechanism 203 - 205 a-o-galacturonosyltransferase 107 mixed anhydride intermediate 205 UDPglucose 100-102, 194-195 tryptophanyl enzyme 204-205 UDPglucose dehydrogenase 49 Tsai, C.S. 54, 55, 110 UDPglucose-DNA Tsai, H. 111 a-o-glucosyltransferase 107 Tsai, I.-H. 152 UDPglucose 4-epimerase 194-195, Tsai, L. 201 199 Tsai, M.-D. 172, 185 mechanism 194 - 195 Tse, Y.C. 198 N A D as prosthetic group 194 -195 Tso, M.Y. 59 UDPglucose-lipopolysaccharide Tsolas, O. 73, 74, 109 glucosyltransferase I 107 Tsuda, M. 57 U D Pglucose-lipopolysaccharide Tsukada, K. 55 glucosyltransferase II 107 Tsuru, D. 152 UDPg)ucose-po)y(g)ycero) phosphate) Tsuyama, N. 120 a-o-glucosyltransferase 107 Tu, C.K. 173 UDPglucuronate decarboxylase 182 Tu, J.1. 110 Ueda, K. 151 Tu, S.c. 31 Ueda, T. 58 Tubbs, P.K. 53, 166 Uiterkamp, A.J.M.S. 173 Tung, K.K. 113 Ulane, R.E. 153 Turano, C. 183 Ulevitch, RJ. 109 Turkova, J. 152 Ullrey, D. 195 Tusa, P.P. 119 Ullrich, V. 46, 58 Two-body interaction in covalent Ulrich, B. 54 catalysis 13, 96 Umani-Ronchi, A. 178 Tyramine oxidase 50 Umbreit, J.N. 151 Tyrocidine 190, 192,207 Urea carboxylase 220 Tyrocidine synthetase 220 Urease 149 Tyrosinase 51 trans- Urocanate 181 L - Tyrosine 179 - 180 Uric acid 31-32 Tyrosine aminotransferase 108 Urokinase 148 Tyrosine decarboxylase 182 Utter, M.F. 110,162,215,217 Tyrosine phenol-lyase 182 Uyeda, K. 54 274 Index v Vining, L.C. 56 Vinylacetyl-CoA d-isomerase 200 Vachek, H. 113 Viratelle, O.M. 126, 151 Vagelos, P.R. 76, 110 Virden, R. 154 Valentino, D. 113 Vitols, E. 58 Valenzuela, M.S. 75 Vliegenhart, J.F.G. 57 Valinsky, J.E. 178 Voet, J. 9,24,25,80 Vallee, B.L. 129 Volini, M. 104 Vallogini, M.P. 54 Volpe, J.A. 42 Valueva, T. 138, 139 von Balthazar, A.K. 151 van Andrichem, M.E. 132 Voordouw, G. 152 Van Beeumen, J. 151 Votaw, R. 184 Vandekerkhove, J. 152 Vuttivej, K. 184 van den Bosch, H. 150 van den Heusden, G.P.H. 150 van der Drift, C. 201 w van der Groen, G. 126 Van Etten, R.L. 120, 124 Waara, I. 173 van Eys, J. 36 Wada, H. 84, 112 van Gelder, B.F. 57 Wagner, M. 215 van Heuvelen, A. 31 Wagner, O.H. 178 van Heyningen, S. 152 Wiihlby, S. 133, 152, 153 van Leuven, F. 111 Waite, M. 222 van Lier, J.E. 46, 58 Wakil, S.J. 76,77, 1l0, 222 Viinngard, T. 41,42,58 Walaas, O. 58 Van Sweringen, B. 104 Waley, S.G. 196 van Thoai, N. 57,91,97 Walinder, O. 98, 99 Van Wart, H.E. 129 Walker, G.C. 56 Varner, J.E. 221 Walker, 1.B. 69 Vasiliev, V. Yu. 111 Walker, P.G. 151 Vaslow, F. 133 Wallace, J.C. 215 Vavra, J. 84 Wallace, W.J. 42,46 Vaz, A.D.N. 175 Wallen, L. 35 Vederas,1.C. 172, 183 Wallenfels, K. 124, 125 Veeger, C. 24, 54, 55 Wallin, B.K. 121 Vega, J.M. 55, 56 Walseth, T.F. 110 Veldink, G.A. 57 Walsh, C.T. 24,27,28,30,53,54,88, Velick, S.F. 53, 55, 84 169, 184, 185, 188, 203 Venkataraman, R. 74 Walsh, K.A. 153 Vennesland, B. 38, 54 Walter, R. 151,152 Vergara, E. V. 123 Wang, C.C. 151 Verpoorte, J.A. 172 Wang, E. 188 Vervoort, A. 151 Wang, J.C. 198,219 Victor, J. 82 Wang, J.H. 173 Viger, A. 197 Wang, S.F. 104, 185, 197 Vigi, V. 69 Wang, T.T. 141,153 Viglino, P. 40, 58 Wang, V.S. 197 Vignais, P.V. 98 Ward, L. 194 Villafranca, 1.1. 52, 150, 184 Ward, R.L. 58 Villemez, C.L. 111 Warms, J.V.B. 97,112 Vincent, S.P. 56 Warren, S. 157 Index 275

Warren, W.A. 34 White, R.C. 151 Warring a , M.G.P.1. 150 White-Stevens, R.H. 57 Watanabe, T. 170 Whitfield, C.J. 53 Wataya, Y. 109 Whitney, P. A. 222 Watkins, W.M. 111 Wickner, R.B. 181 Watson, H.C. 152 Wiegand, U. 222 Watson, J.G. 153 Wightman, R.H. 180 Watts, D.C. 19 Williams, A. 136, 153 Waygood, E.B. 112 Williams, Jr., C.H. 47,48,54,55 Waymack, P.P. 120 Williams, F.R. 53 Webb, B.C. 92 Williams, J.F. 72 Webb, E.C. 115, 116 Williamson, I.P. 110 Webb-; M.R. 97, 150, 196 Williamson, W.T. 184 Weber, J.P. 151 Willms, C.R. 110 Weber, W.W. 74 Willoughby, E. 152 Webster, G.C. 221 Wilson, D.B. 194 Webster, Jr., L.T. 203,208 Wilson,I.B. 91,117,126, 150 Webster, Jr., R.W. 203 Wilson, K.S. 110 Wedding, R.T. 98",185 Wilson, M.T. 56 Weigel, H. 110 Wiltshire, H. R. 180 Weigent, D.A. 111 Wimmer, M.J. 90 Weill, C. 109 Wing, R.M. 35 Weiner, H. 53 Winnick, T. 207 Weinstock, L. T. 28 Winter, C.G. 146 Weiss, B. 222 Wolcott, R.G. 150 Weiss, Y. 152 Wolfenden, R. 127, 153, 154 Weissbach, H. 61, 109 Wolochow, H. 78 Wellner, D. 54 Wolthers, B.G. 137 Wellner, V.P. 112,222 Womack, F.C. 89 Wells, W.W. 125 Wong, C.H. 153 Wendel, A. 57, 221 Wong, L.-1. 97, 100, 102, 112 Wener, R. 57 Wong, S.c. 152 Weng, L. 104 Wong, S.S. 110 Wenger, B. 222 Wood, E.J. 151 Wentworth, D.F. 127 Wood, H.G. 65, 66, 91, 102, 103, Werkman, C.H. 110 109 Werle, E. 152 Wood, H.N. 132 Weser, U. 57 Wood, J.L. 113 Westerik, 1.0. 153 Wood, J.M. 57 Westerrnark, U. 53 Wood, N.P. 110 Westhead, E.W. 53,177 Wood, W.A. 113,184,200 Westheimer, F.H. 11, 19,38,66,94, Woodams, A.D. 201 157, 158 Woolley, P. 131, 173 Westley, 1. 103, 104 Worthen, S. 55 Whalen, R.G. 97,112 Wouters-Leysen, J. 126 Wharton, C.W. 153 Wren, E.A. 153 Wharton, D.C. 56 Wu, J.W. 100, 102 Whelan, W.1. 111 Wunderlich, I. 75 Whitaker, D.R. 150, 152 Wunderwald, P. 168 Whitaker, 1.R. 135 Wybrandt, G.B. 138 White, H. 109 Wyluda, B.J. 131 276 Index

Wyman, A. 110 Yoshida, F. 152 Wynn, C.H. 124 Yoshida, H. 103 Yoshimoto, A. 56 Yoshimoto, T. 152 x Yoshimura, 1. 56 Young, A.R. 151 Xanthine 31-32 Young, D.L. 222 Xanthine dehydrogenase 32, 49 Young, L.G. 81 Xanthine oxidase 31-32,49 Young, M.R. 181 electron transport by 31 Young, P.R. 151 mechanism 31-32 Yu, E.H. 152 D-Xylose 87-88 Yuan, C.Y. 138 Xylose isomerase 199 Yudelevich, A. 198 Exo-1,4-D-xylosidase 148 D-Xylulose-5-P 70-71 z y Zach, D. 57 Yagi, T. 57 Zagalak, B. 151,178,185 Yamada, H. 54, 55, 160, 184, 188 Zalkin, H. 184, 222 Yamada, M. 190 Zanetti, G. 55 Yamaha, T. 55 Zannis, V.1. 134 Yamamoto, S. 58 Zanotti, G. 110 Yamamoto, T. 146, 151 Zappia, V. 111 Yamamura, K. 128 Zasman, Z. 110 Yamana, T. 131 Zatman, LJ. 127 Yamanaka, T. 56 Zemell, R.1. 111 Yamano, T. 53 Zeppezauer, E. 34, 35 Yamazaki, I. 56, 57 Zerner, B. 116, 157, 181 Yang, I.H. 153 Zetterqvist, O. 98, 144, 170 Yang,I.Y. 184 Zeylemaker, W.P. 54 Yang, S.L. 102 Ziderman, D. 111 Yankeelov, Jr., J.A. 99 Ziegenhorn, 1. 110 Yasuda, H. 57 Ziegert, K. 168 Yasukochi, Y. 55 Ziegler, D.M. 58 Yasunobu, K.T. 54 Zimmerman, S.B. 111,219 Yates, J.T. 4 Zinc, coordinated to substrate in, Yde, M. 126 alcohol dehydrogenase 35 Yeast proteinase B 148 alkaline phosphatase 119-120 Yocum, R.R. 152 carbonic anhydrase 173 -174 Yoda, A. 144 carboxypeptidase A 128 -131 Yon, J.M. 126, 151 Zuber, M. 152 Yonaha, K. 112 Zucker, F.H. 20, 90 Yonetani, T. 56,57 Zukin, R.S. 119 Yorifugi, T. 200 Zumft, W.G. 58