DOCSLIB.ORG

Inhibition of Amino Acid Decarboxylases*

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text
Inhibition of Amino Acid Decarboxylases* CHAPTER 9 Inhibition of Amino Acid Decarboxylases* William Gilbert Clark I. Introduction 316 II. Pyridoxal Kinase 318 III. Apoenzyme-Coenzyme Dissociation 319 IV. Transport, Uptake, Binding, Release 320 V. Inanition 322 VI. Tissue Damage, Growth, Neoplasms, Organectomy 322 VII. Apoenzyme Synthesis 323 VIII. Inhibition by Apoenzyme Antibody 326 IX. Metals, Chelators, and Metal Complexers 327 X. Cyanide 330 XI. Pyridoxal-5-Phosphate (Codecarboxylase), Vitamin B6, Be-Deficien- cy, Be-Antagonists 331 A. Ββ-Deficiency and Antagonists 331 B. B6-P04 Hydrazones 334 C. Toxopyrimidine 335 D. Steroids 337 XII. Activators, Stabilizers, and Cofactors Other Than Be-P04 337 A. Metals 337 B. Surfactants 337 C. Solvents 337 D. Phosphates and Arsenate 338 E. Miscellaneous 338 XIII. Carbonyl Reagents and Inhibitors Acting on Coenzyme Other Than Cyanide, Substrate Analogues, and Pyridoxine Antagonists 339 A. Hydroxylamine, Hydrazides, Semicarbazide, Sulfite, Hydrazine, Oximes, etc 339 B. Cycloserine (4-Amino-3-isoxazolidone) 343 C. Penicillamine 345 D. Sulfonylureas 345 E. Cysteine, 2,3-Dimercapto-l-propanol (BAL), Glutathione 346 F. Ascorbic Acid 346 * Supported by Grants from the National Mental Health Association, U.S. Public Health Service, American Heart Association, Los Angeles County Heart Association, U.S. Army Chemical Center, American Cancer Society, Office of Naval Research, Helen Hay Whitney, Jr. Foundation, Life Insurance Medical Research Fund. 315 316 W. G. CLARK XIV. Hormones 346 A. Insulin 347 B. Pituitary 347 C. Adrenal Cortex 347 D. Thyroid 349 E. Sex Hormones 352 XV. Miscellaneous 354 A. Antibiotics 354 B. Antihistamines 354 C. Reserpine 354 D. Tranquilizers 354 E. Tetrahydroisoquinolines 354 F. Folic Acid Antagonists 355 XVI. Substrate Analogues 356 A. Bacterial and Plant Decarboxylases 356 B. Mammalian (and Fowl) Decarboxylases in vitro 357 C. Mammalian Dopa Decarboxylase in vitro 358 D. Mammalian 5-HTP Decarboxylase in vitro 358 E. Glutamic Acid Decarboxylase in vivo 359 F. Dopa Decarboxylase in vivo 359 G. Quinones and Potential Quinoids 360 H. Ketonuria 361 I. α-Alkyl Substrate Analogues 363 References 366 I. INTRODUCTION Although enzymic decarboxylation plays a minor role quantitatively ni metabolism fo amino acids, ti si na important one because fo the critical nature, marked pharmacological activity, and function fo the end products. The physiological significance fo most, fi not all, fo these end products still remains ot eb clarified, but many fo them probably are essential for a num­ ber fo homeostatic regulatory and adaptive mechanisms ni all living organ­ isms. tI was not until 1936-1937 that amino acid decarboxylases were de­ scribed yb Okunuki (1937) ni plants (glutamic acid decarboxylase) and yb Werle (1936) and Holtz and Heise (1937, 1938) [histidine and 3,4-dihy- droxyphenylanine (dopa) decarboxylase]. This and other work, including data no inhibitors fo these decarboxylases, have been reviewed yb Gale (1940b, 1946, 1953), Holtz (1941), Storck (1951), Janke (1951), Karrer (1947), Mardashew (1949), Schales (1951), Mèister (1955, 1957), Werle (1943a,b, 1947, 1951), and Ruiz and Zaragoza (1959). It si the purpose fo this review ot discuss inhibition fo the amino acid decarboxylases ni general, with some emphasis no more recent contribu­ tions (up ot early 1961 ni most cases). Inhibition yb general enzyme "poisons" ro dénaturants in vitro, such sa trichloroacetate and alkylat- 9. INHIBITION OF AMINO ACID DECARBOXYLASES 317 ing agents, will not be included. Clark (1959) and Clark and Pogrund (1961) recently reviewed the subject of dopa decarboxylase inhibition in vitro and in vivo, and Sourkes and D'lorio discuss the subject in Volume II of this treatise. Since many inhibitors of these enzyme systems exert their effects directly or indirectly through pyridoxal-5-phosphate (B6-P04), the coenzyme of amino acid decarboxylases, some aspects of the vitamin B6-dependent enzymes in general must be considered. Ref­ erence should be made to the extensive reviews available of the pyri- doxine-dependent enzymes by Blaschko (1945a), Gunsalus (1951), Wil­ liams et al. (1950), Sherman (1954), Tower (1956, 1959, 1960), Umbreit (1954), Meister (1957), Mathews (1958), Snell (1958), Snell and Jenkins (1959), Siliprandi (1960), Roberts and Eidelberg (1959), Roberts et al (1960), Braunstein (I960), and Axelrod and Martin (1961). Braunstein's review, "Pyridoxal Phosphate" (1960), and that of Snell (1959), "Chemical Structure in Relation to Biological Activities of Vitamin B6," are particu­ larly exhaustive. The amino acid decarboxylases described so far catalyze the following reactions: (1 Glycine —> methylamine (2; L-Alanine —> ethylamine (3: L-Serine —> ethanolamine (4; α-Aminobutyric acid —• propylamine (5; L-Methionine —> 3-methylthiopropylamine (β: L-Valine —> isobutylamine (7; L-Norvaline —• butylamine (s: L-Leucine —> isoamylamine (9: L-Isoleucine —* 3-methylbutylamine do: L-Aspartic acid —> L-alanine (11 L-Arginine —> agmatine (12: L-Histidine —> histamine (13 L-Aspartic acid —• /3-alanine (14 L-Ornithine —> putrescine (15 L-Lysine —> cadaverine (16 meso-δ-6-Diaminopimelic acid —> L-lysine (17 α-Aminomalonic acid —* glycine (is: δ-Hydroxy-L-lysine —» hydroxycadaverine (i9: L-Glutamic acid —> 7-aminobutyric acid (20 Allo-jS-hydroxy-L-glutamic acid —• 7-amino-/3-hydroxybutyric acid (21 7-Hydroxy-L-glutamic acid —• a-hydroxy-7-aminobutyric acid (22 7-Methylene-L-glutamic acid —> 7-amino-a-methylene butyric acid (23 L-Cysteic acid —> taurine (24 L-Cysteinesulfinic acid —> hypotaurine (25: L-Tryptophan -> tryptamine (26 4-Hydroxy-L-tryptophan —* 4-hydroxytryptamine (27 5-Hydroxy-L-tryptophan (^δ-ΗΤΡ") -> 5-hydroxytryptamine (serotonin, "5HT") 318 W. G. CLARK (28) 6-Hydroxy-L-tryptophan —» 6-hydroxytryptamine (29) α-Methyl-L-tryptophan —» a-methyltryptamine (30) a-Methyl-5-hydroxy-L-tryptophan —» a-methyl-5-hydroxytryptamine (31) a. L-Phenylalanine —> phenylethylamine Ring-substituted hydroxy-L-phenylalanines to corresponding amines, e.g. : b. L-Tyrosine —» tyramine c. Diiodo-L-tyrosine —* diiodotyramine (Werle, 1947; not confirmed) d. 2-Hydroxy-L-phenylalanine (o-tyrosine) —> 2-hydroxyphenylethylamine (o-tyramine) e. 3-Hydroxy-L-phenylalanine (ra-tyrosine) —• ra-tyramine f. a-Methyl-3-hydroxy-L-phenylalanine (α-methyl-m-tyrosine) —> a-methyl- 3-hydroxyphenylethylamine (a-methyl-ra-tyramine) g. 3,4-Dihydroxy-L-phenylalanine (dopa) —• 3,4-dihydroxytyramine (dopa­ mine) (32) a. L-Phenylserine —• phenylethanolamine b. 2-Hydroxy-L-phenylserine —• 2-hydroxyphenylethanolamine c. 3-Hydroxy-L-phenylserine —> 3-hydroxyphenylethanolamine d. 4-Hydroxy-L-phenylserine —• 4-hydroxyphenylethanolamine (octopamine, norsynephrine) e. 3,4-Dihydroxy-L-phenylserine (dops) —> 3,4-dihydroxyphenylethanol- amine (arterenol, norepinephrine) Some of these reactions have been shown to be catalyzed by one and the same enzyme, and possibilities of this kind should be borne in mind in considering this section. Further discussion of this point, classifying and documenting the individual enzymes by their distribution in micro­ organisms, plants, and animals, the structures and stereospecificity of their substrates, their kinetics, apoenzyme-coenzyme affinity and dissoci­ ation must be sought in the reviews cited. Since the introduction of tracer techniques and amine catabolic enzyme inhibitors, many decarboxylations formerly thought to be absent in animals are being announced. II. PYRIDOXAL KINASE Snell (1959) and McCormick et al (1961; McCormick and Snell, 1961) have discussed codecarboxylase kinase (pyridoxal phosphokinase) and have reviewed the literature. Chevillard and Thoai (1951) and Thoai and Chevillard (1951a,b) showed that Mg+ + and Mn+ + activate it, ATP or ADP are necessary, and thiamine inhibits it. Hurwitz (1952, 1953, 1955) showed that some pyridoxine analogues inhibit tyrosine decarboxylase in bacteria, while others inhibit the phosphorylation of pyridoxal in the presence of ATP. Some adenine and purine derivatives inhibit competi­ tively and several metal cations activate (cf. McCormick et al., 1961; McCormick and Snell, 1961). Hurwitz suggested that the adenines and purines act through the activating metallic ions. McCormick and Snell 9. INHIBITION OF AMINO ACID DECARBOXYLASES 319 (1959, 1961) and McCormick et al. (1960, 1961) showed that purified pyridoxal phosphokinase from brain is markedly inhibited by a variety of condensation products formed from pyridoxal and hydroxylamine, O-sub- stituted hydroxylamines, hydrazine, and substituted hydrazines; they questioned former explanations of the convulsive effects of such carbonyl reagents which causally related the seizures to lowered brain 7-amino­ butyric acid (gaba) through interaction with B6-PO4. Dubnick and co­ workers (1960c) postulated that pyridoxal hydrazones are formed from hydrazines and B6-P04 in vivo and exert toxic effects by inhibiting the phosphokinase (cf. Balzerei al., 1960a,b,c; and Baxter and Roberts, 1960). Recently, Wada and Snell (1961), Turner and Happold (1961), and Wada et al. (1961) described an enzyme which oxidizes pyridoxine and pyri- doxamine phosphates to B6-PO4. Evidently, the primary pathway of the formation of B6-P04 is phosphorylation by the kinase, followed by the action of the oxidase. The oxidase, a flavoprotein with riboflavin-5'- phosphate as a cofactor, is sensitive to thiol reagents, heavy metals, and some phosphorylated analogues of Be, especially pyridoxal phosphate oxime. Greenberg et al. (1959) observed that chlorpromazine had little or no effect
Load more

Recommended publications
  • Aliphatic 1-Amino Acid Decarboxylase from Ferns (Filicopsida) Thomas Hartmann
    Aliphatic 1-Amino Acid Decarboxylase from Ferns (Filicopsida) Thomas Hartmann. Klaus Bax. and Renate Scholz Institut für Pharmazeutische Biologie der Technischen Universität Braunschweig, Mendels- sohnstr. 1, D-3300 Braunschweig. Bundesrepublik Deutschland Z. Naturforsch. 39c, 2 4 -3 0 (1984); received Septem ber 26, 1983 Ferns, Filicopsida, Polypodium vulgare. Aliphatic 1-Amino Acid Decarboxylase, Occurrence and Distribution A screening of 27 fern species (Filicopsida) out of 9 families revealed that 25 species were able to decarboxylate 1-leucine to 3-methylbutylamine (isoamylamine). The enzyme of Polvpodium vulgäre has partially been purified and characterisized. All attempts to solubilize it from acetone preparations failed; however, approx. 50% of total activity could be extracted from dry material in the presence of detergents at high concentration. The soluble enzyme was purified 132-fold. 1-Methionine was found the best substrate followed by norvaline, leucine, norleucine, isoleucine, homocysteine, valine. It has been confirmed that these substrates are decarboxylated by a single enzyme. The pH-optimum was at pH 5.0 (particulate preparation) and pH 4.5 (soluble enzyme). Decarboxylation is dependent on pyridoxal-5'-phosphate (PLP). A strictly substrate dependent coenzyme dissociation was observed which could largely be prevented by addition of 2 -oxo-acids, such as glyoxylate or pyruvate. Apodecarboxylase prepared by prolonged substrate incubation was found to be extremely labile at pH 4.5 but stable at pH 6.5. A comparison of the fern enzyme with bacterial valine decarboxylase (EC 4.1.1.14) and leucine decarboxylase of red algae revealed great similarities especially in substrate specificity. It is suggested to unify these activities as “aliphatic 1-amino acid decarboxylase”.
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2009/0292100 A1 Fiene Et Al
    US 20090292100A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2009/0292100 A1 Fiene et al. (43) Pub. Date: Nov. 26, 2009 (54) PROCESS FOR PREPARING (86). PCT No.: PCT/EP07/57646 PENTAMETHYLENE 1.5-DIISOCYANATE S371 (c)(1), (75) Inventors: Martin Fiene, Niederkirchen (DE): (2), (4) Date: Jan. 9, 2009 (DE);Eckhard Wolfgang Stroefer, Siegel, Mannheim (30) Foreign ApplicationO O Priority Data Limburgerhof (DE); Stephan Aug. 1, 2006 (EP) .................................. O61182.56.4 Freyer, Neustadt (DE); Oskar Zelder, Speyer (DE); Gerhard Publication Classification Schulz, Bad Duerkheim (DE) (51) Int. Cl. Correspondence Address: CSG 18/00 (2006.01) OBLON, SPIVAK, MCCLELLAND MAIER & CD7C 263/2 (2006.01) NEUSTADT, L.L.P. CI2P I3/00 (2006.01) 194O DUKE STREET CD7C 263/10 (2006.01) ALEXANDRIA, VA 22314 (US) (52) U.S. Cl. ........... 528/85; 560/348; 435/128; 560/347; 560/355 (73) Assignee: BASFSE, LUDWIGSHAFEN (DE) (57) ABSTRACT (21) Appl. No.: 12/373,088 The present invention relates to a process for preparing pen tamethylene 1,5-diisocyanate, to pentamethylene 1,5-diiso (22) PCT Filed: Jul. 25, 2007 cyanate prepared in this way and to the use thereof. US 2009/0292100 A1 Nov. 26, 2009 PROCESS FOR PREPARING ene diisocyanates, especially pentamethylene 1,4-diisocyan PENTAMETHYLENE 1.5-DIISOCYANATE ate. Depending on its preparation, this proportion may be up to several % by weight. 0014. The pentamethylene 1,5-diisocyanate prepared in 0001. The present invention relates to a process for pre accordance with the invention has, in contrast, a proportion of paring pentamethylene 1,5-diisocyanate, to pentamethylene the branched pentamethylene diisocyanate isomers of in each 1.5-diisocyanate prepared in this way and to the use thereof.
    [Show full text]
  • 12) United States Patent (10
    US007635572B2 (12) UnitedO States Patent (10) Patent No.: US 7,635,572 B2 Zhou et al. (45) Date of Patent: Dec. 22, 2009 (54) METHODS FOR CONDUCTING ASSAYS FOR 5,506,121 A 4/1996 Skerra et al. ENZYME ACTIVITY ON PROTEIN 5,510,270 A 4/1996 Fodor et al. MICROARRAYS 5,512,492 A 4/1996 Herron et al. 5,516,635 A 5/1996 Ekins et al. (75) Inventors: Fang X. Zhou, New Haven, CT (US); 5,532,128 A 7/1996 Eggers Barry Schweitzer, Cheshire, CT (US) 5,538,897 A 7/1996 Yates, III et al. s s 5,541,070 A 7/1996 Kauvar (73) Assignee: Life Technologies Corporation, .. S.E. al Carlsbad, CA (US) 5,585,069 A 12/1996 Zanzucchi et al. 5,585,639 A 12/1996 Dorsel et al. (*) Notice: Subject to any disclaimer, the term of this 5,593,838 A 1/1997 Zanzucchi et al. patent is extended or adjusted under 35 5,605,662 A 2f1997 Heller et al. U.S.C. 154(b) by 0 days. 5,620,850 A 4/1997 Bamdad et al. 5,624,711 A 4/1997 Sundberg et al. (21) Appl. No.: 10/865,431 5,627,369 A 5/1997 Vestal et al. 5,629,213 A 5/1997 Kornguth et al. (22) Filed: Jun. 9, 2004 (Continued) (65) Prior Publication Data FOREIGN PATENT DOCUMENTS US 2005/O118665 A1 Jun. 2, 2005 EP 596421 10, 1993 EP 0619321 12/1994 (51) Int. Cl. EP O664452 7, 1995 CI2O 1/50 (2006.01) EP O818467 1, 1998 (52) U.S.
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2009/0163376 A1 Li Et Al
    US 200901 63376A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2009/0163376 A1 Li et al. (43) Pub. Date: Jun. 25, 2009 (54) KETOL-ACID REDUCTOISOMERASE USING Related U.S. Application Data NADH (60) Provisional application No. 61/015.346, filed on Dec. (75) Inventors: Yougen Li, Lawrenceville, NJ (US); 20, 2007, provisional application No. 61/109,297, Der-Ing Liao, Wilmington, DE filed on Oct. 29, 2008. (US); Mark J. Nelson, Newark, DE Publication Classification (US); Daniel P. Okeefe, Ridley Park, PA (US) (51) Int. Cl. C40B 30/04 (2006.01) Correspondence Address: CI2N 9/90 (2006.01) E DUPONT DE NEMOURS AND COMPANY CI2N IS/II (2006.01) LEGAL PATENT RECORDS CENTER CI2N 5/06 (2006.01) BARLEY MILL PLAZA 25/1122B, 4417 LAN CI2P 7/16 (2006.01) CASTER PIKE (52) U.S. Cl. ............ 506/9: 435/233: 536/23.2; 435/325: WILMINGTON, DE 19805 (US) 435/160 (57) ABSTRACT (73) Assignee: E. DUPONT DE NEMOURS AND COMPANY Methods for the evolution of NADPH binding ketol-acid reductoisomerase enzymes to acquire NADH binding func (21) Appl. No.: 12/337,736 tionality are provided. Specific mutant ketol-acid reductoi Somerase enzymes isolated from Pseudomonas that have (22) Filed: Dec. 18, 2008 undergone co-factor switching to bind NADH are described. Glucose O Y O O Pyruvate CO-acetolate syn thase NXbhOH O 5 valine S-Acetolactate O decarboxylase f p NADPH + H ch isobutylarine NADP Aerof acid reductoisamerase (KAA) valine , co, NH 8 onega transanitase a 2. NH; valine NH3. -- OH 22 Hi / "h"gehydrogenase or 2 e, 2 OH frtisatinase O O OHO OH branched chain keto acid 2,3-Dihydroxy isowalerate acetohydroxy acid dehydratase aecarboxylase H "c" O "d" ) H2 O ci-Ketoisowalerate CO isobutyraldehyde "f 2e.
    [Show full text]
  • (12) United States Patent (10) Patent No.: US 9.273,330 B2 Bramucci Et Al
    US00927.333 OB2 (12) United States Patent (10) Patent No.: US 9.273,330 B2 Bramucci et al. (45) Date of Patent: Mar. 1, 2016 (54) BUTANOL TOLERANCE IN 8,206,970 B2 6/2012 Eliot et al. MCROORGANISMS 8,222,017 B2 7/2012 Li et al. 8,241,878 B2 8/2012 Anthony et al. (71) Applicant: Butamax Advanced Biofuels LLC, 3. E: 858: Ration s al Wilmington, DE (US) 8,372,612 B2 2/2013 Larossa et al. 8,389,252 B2 3/2013 Larossa (72) Inventors: Michael G. Bramucci, Boothwyn, PA 8,455,224 B2 6/2013 Paul (US); Vasantha Nagarajan, 8,455.225 B2 6/2013 Bramucci et al. Wilmington,s DE (US) - E.Kw E. E. E.a 8,557.562 B2 10/2013 Bramucci et al. (73) Assignee: Butamax Advanced Biofuels LLC, 8,614,085 B2 12/2013 Van Dyk Wilmington, DE (US) 8,637,281 B2 1/2014 Paul et al. 8,637,289 B2 1/2014 Anthony et al. (*)c Notice:- r Sibi tO E. site th still 8,669,0948,652,823 B2 3/20142/2014 AnthonyFlint et al. et al. patent 1s extended or adjusted under 8,691,540 B2 4/2014 Bramucci et al. U.S.C. 154(b) by 2 days. 8,735,114 B2 5/2014 Donaldson et al. 8,765,433 B2 7/2014 Satagopan et al. (21) Appl. No.: 14/045,506 8,785,166 B2 7/2014 Anthony 8,795,992 B2 8/2014 Bramucci et al. (22) Filed: Oct. 3, 2013 5%.
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2012/0266329 A1 Mathur Et Al
    US 2012026.6329A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2012/0266329 A1 Mathur et al. (43) Pub. Date: Oct. 18, 2012 (54) NUCLEICACIDS AND PROTEINS AND CI2N 9/10 (2006.01) METHODS FOR MAKING AND USING THEMI CI2N 9/24 (2006.01) CI2N 9/02 (2006.01) (75) Inventors: Eric J. Mathur, Carlsbad, CA CI2N 9/06 (2006.01) (US); Cathy Chang, San Marcos, CI2P 2L/02 (2006.01) CA (US) CI2O I/04 (2006.01) CI2N 9/96 (2006.01) (73) Assignee: BP Corporation North America CI2N 5/82 (2006.01) Inc., Houston, TX (US) CI2N 15/53 (2006.01) CI2N IS/54 (2006.01) CI2N 15/57 2006.O1 (22) Filed: Feb. 20, 2012 CI2N IS/60 308: Related U.S. Application Data EN f :08: (62) Division of application No. 1 1/817,403, filed on May AOIH 5/00 (2006.01) 7, 2008, now Pat. No. 8,119,385, filed as application AOIH 5/10 (2006.01) No. PCT/US2006/007642 on Mar. 3, 2006. C07K I4/00 (2006.01) CI2N IS/II (2006.01) (60) Provisional application No. 60/658,984, filed on Mar. AOIH I/06 (2006.01) 4, 2005. CI2N 15/63 (2006.01) Publication Classification (52) U.S. Cl. ................... 800/293; 435/320.1; 435/252.3: 435/325; 435/254.11: 435/254.2:435/348; (51) Int. Cl. 435/419; 435/195; 435/196; 435/198: 435/233; CI2N 15/52 (2006.01) 435/201:435/232; 435/208; 435/227; 435/193; CI2N 15/85 (2006.01) 435/200; 435/189: 435/191: 435/69.1; 435/34; CI2N 5/86 (2006.01) 435/188:536/23.2; 435/468; 800/298; 800/320; CI2N 15/867 (2006.01) 800/317.2: 800/317.4: 800/320.3: 800/306; CI2N 5/864 (2006.01) 800/312 800/320.2: 800/317.3; 800/322; CI2N 5/8 (2006.01) 800/320.1; 530/350, 536/23.1: 800/278; 800/294 CI2N I/2 (2006.01) CI2N 5/10 (2006.01) (57) ABSTRACT CI2N L/15 (2006.01) CI2N I/19 (2006.01) The invention provides polypeptides, including enzymes, CI2N 9/14 (2006.01) structural proteins and binding proteins, polynucleotides CI2N 9/16 (2006.01) encoding these polypeptides, and methods of making and CI2N 9/20 (2006.01) using these polynucleotides and polypeptides.
    [Show full text]
  • All Enzymes in BRENDA™ the Comprehensive Enzyme Information System
    All enzymes in BRENDA™ The Comprehensive Enzyme Information System http://www.brenda-enzymes.org/index.php4?page=information/all_enzymes.php4 1.1.1.1 alcohol dehydrogenase 1.1.1.B1 D-arabitol-phosphate dehydrogenase 1.1.1.2 alcohol dehydrogenase (NADP+) 1.1.1.B3 (S)-specific secondary alcohol dehydrogenase 1.1.1.3 homoserine dehydrogenase 1.1.1.B4 (R)-specific secondary alcohol dehydrogenase 1.1.1.4 (R,R)-butanediol dehydrogenase 1.1.1.5 acetoin dehydrogenase 1.1.1.B5 NADP-retinol dehydrogenase 1.1.1.6 glycerol dehydrogenase 1.1.1.7 propanediol-phosphate dehydrogenase 1.1.1.8 glycerol-3-phosphate dehydrogenase (NAD+) 1.1.1.9 D-xylulose reductase 1.1.1.10 L-xylulose reductase 1.1.1.11 D-arabinitol 4-dehydrogenase 1.1.1.12 L-arabinitol 4-dehydrogenase 1.1.1.13 L-arabinitol 2-dehydrogenase 1.1.1.14 L-iditol 2-dehydrogenase 1.1.1.15 D-iditol 2-dehydrogenase 1.1.1.16 galactitol 2-dehydrogenase 1.1.1.17 mannitol-1-phosphate 5-dehydrogenase 1.1.1.18 inositol 2-dehydrogenase 1.1.1.19 glucuronate reductase 1.1.1.20 glucuronolactone reductase 1.1.1.21 aldehyde reductase 1.1.1.22 UDP-glucose 6-dehydrogenase 1.1.1.23 histidinol dehydrogenase 1.1.1.24 quinate dehydrogenase 1.1.1.25 shikimate dehydrogenase 1.1.1.26 glyoxylate reductase 1.1.1.27 L-lactate dehydrogenase 1.1.1.28 D-lactate dehydrogenase 1.1.1.29 glycerate dehydrogenase 1.1.1.30 3-hydroxybutyrate dehydrogenase 1.1.1.31 3-hydroxyisobutyrate dehydrogenase 1.1.1.32 mevaldate reductase 1.1.1.33 mevaldate reductase (NADPH) 1.1.1.34 hydroxymethylglutaryl-CoA reductase (NADPH) 1.1.1.35 3-hydroxyacyl-CoA
    [Show full text]
  • (12) Patent Application Publication (10) Pub. No.: US 2015/0240226A1 Mathur Et Al
    US 20150240226A1 (19) United States (12) Patent Application Publication (10) Pub. No.: US 2015/0240226A1 Mathur et al. (43) Pub. Date: Aug. 27, 2015 (54) NUCLEICACIDS AND PROTEINS AND CI2N 9/16 (2006.01) METHODS FOR MAKING AND USING THEMI CI2N 9/02 (2006.01) CI2N 9/78 (2006.01) (71) Applicant: BP Corporation North America Inc., CI2N 9/12 (2006.01) Naperville, IL (US) CI2N 9/24 (2006.01) CI2O 1/02 (2006.01) (72) Inventors: Eric J. Mathur, San Diego, CA (US); CI2N 9/42 (2006.01) Cathy Chang, San Marcos, CA (US) (52) U.S. Cl. CPC. CI2N 9/88 (2013.01); C12O 1/02 (2013.01); (21) Appl. No.: 14/630,006 CI2O I/04 (2013.01): CI2N 9/80 (2013.01); CI2N 9/241.1 (2013.01); C12N 9/0065 (22) Filed: Feb. 24, 2015 (2013.01); C12N 9/2437 (2013.01); C12N 9/14 Related U.S. Application Data (2013.01); C12N 9/16 (2013.01); C12N 9/0061 (2013.01); C12N 9/78 (2013.01); C12N 9/0071 (62) Division of application No. 13/400,365, filed on Feb. (2013.01); C12N 9/1241 (2013.01): CI2N 20, 2012, now Pat. No. 8,962,800, which is a division 9/2482 (2013.01); C07K 2/00 (2013.01); C12Y of application No. 1 1/817,403, filed on May 7, 2008, 305/01004 (2013.01); C12Y 1 1 1/01016 now Pat. No. 8,119,385, filed as application No. PCT/ (2013.01); C12Y302/01004 (2013.01); C12Y US2006/007642 on Mar. 3, 2006.
    [Show full text]
  • Comparative Modelling of a Novel Enzyme: Mus Musculus Leucine Decarboxylase
    Turkish Journal of Chemistry Turk J Chem (2020) 44: 817 – 832 http://journals.tubitak.gov.tr/chem/ © TÜBİTAK Research Article doi:10.3906/kim-2003-63 Comparative modelling of a novel enzyme: Mus musculus leucine decarboxylase Arif Sercan ŞAHUTOĞLU∗ 1Department of Chemistry, Faculty of Science and Arts, Canakkale Onsekiz Mart University, Canakkale, Turkey Received: 30.03.2020 • Accepted/Published Online: 10.05.2020 • Final Version: 01.06.2020 Abstract: Leucine decarboxylase (LDC) is a recently proposed enzyme with no official enzyme commission number yet. It is encoded by the Mus musculus gene Gm853 which is expressed at kidneys, generating isopentylamine, an alkylmonoamine that has not been described to be formed by any metazoan enzyme yet. Although the relevance of LDC in mammalian physiology has not been fully determined, isopentylamine is a potential modulator which may have effects on insulin secretion and healthy gut microbiota formation. The LDC is a stable enzyme that specifically decarboxylates L-leucine but does not decarboxylate ornithine or lysine as its paralogues ornithine decarboxylase (ODC; EC: 4.1.1.17) and lysine decarboxylase (KDC; EC: 4.1.1.18) do. It does not act as an antizyme inhibitor and does not decarboxylate branched amino acids such as valine and isoleucine as it is another paralogue valine decarboxylase (VDC; EC: 4.1.1.14). The crystal structure of the enzyme has not been determined yet but there are homologous structures with complete coverage in Protein Data Bank (PDB) which makes LDC a good candidate for comparative modelling.In this study, homology models of LDC were generated and used in cofactor and substrate docking to understand the structure/function relationship underlying the unique selectivity of LDC enzyme.
    [Show full text]
  • Supplementary Material (ESI) for Natural Product Reports
    Electronic Supplementary Material (ESI) for Natural Product Reports. This journal is © The Royal Society of Chemistry 2014 Supplement to the paper of Alexey A. Lagunin, Rajesh K. Goel, Dinesh Y. Gawande, Priynka Pahwa, Tatyana A. Gloriozova, Alexander V. Dmitriev, Sergey M. Ivanov, Anastassia V. Rudik, Varvara I. Konova, Pavel V. Pogodin, Dmitry S. Druzhilovsky and Vladimir V. Poroikov “Chemo- and bioinformatics resources for in silico drug discovery from medicinal plants beyond their traditional use: a critical review” Contents PASS (Prediction of Activity Spectra for Substances) Approach S-1 Table S1. The lists of 122 known therapeutic effects for 50 analyzed medicinal plants with accuracy of PASS prediction calculated by a leave-one-out cross-validation procedure during the training and number of active compounds in PASS training set S-6 Table S2. The lists of 3,345 mechanisms of action that were predicted by PASS and were used in this study with accuracy of PASS prediction calculated by a leave-one-out cross-validation procedure during the training and number of active compounds in PASS training set S-9 Table S3. Comparison of direct PASS prediction results of known effects for phytoconstituents of 50 TIM plants with prediction of known effects through “mechanism-effect” and “target-pathway- effect” relationships from PharmaExpert S-79 S-1 PASS (Prediction of Activity Spectra for Substances) Approach PASS provides simultaneous predictions of many types of biological activity (activity spectrum) based on the structure of drug-like compounds. The approach used in PASS is based on the suggestion that biological activity of any drug-like compound is a function of its structure.
    [Show full text]
  • Springer Handbook of Enzymes
    Dietmar Schomburg Ida Schomburg (Eds.) Springer Handbook of Enzymes Alphabetical Name Index 1 23 © Springer-Verlag Berlin Heidelberg New York 2010 This work is subject to copyright. All rights reserved, whether in whole or part of the material con- cerned, specifically the right of translation, printing and reprinting, reproduction and storage in data- bases. The publisher cannot assume any legal responsibility for given data. Commercial distribution is only permitted with the publishers written consent. Springer Handbook of Enzymes, Vols. 1–39 + Supplements 1–7, Name Index 2.4.1.60 abequosyltransferase, Vol. 31, p. 468 2.7.1.157 N-acetylgalactosamine kinase, Vol. S2, p. 268 4.2.3.18 abietadiene synthase, Vol. S7,p.276 3.1.6.12 N-acetylgalactosamine-4-sulfatase, Vol. 11, p. 300 1.14.13.93 (+)-abscisic acid 8’-hydroxylase, Vol. S1, p. 602 3.1.6.4 N-acetylgalactosamine-6-sulfatase, Vol. 11, p. 267 1.2.3.14 abscisic-aldehyde oxidase, Vol. S1, p. 176 3.2.1.49 a-N-acetylgalactosaminidase, Vol. 13,p.10 1.2.1.10 acetaldehyde dehydrogenase (acetylating), Vol. 20, 3.2.1.53 b-N-acetylgalactosaminidase, Vol. 13,p.91 p. 115 2.4.99.3 a-N-acetylgalactosaminide a-2,6-sialyltransferase, 3.5.1.63 4-acetamidobutyrate deacetylase, Vol. 14,p.528 Vol. 33,p.335 3.5.1.51 4-acetamidobutyryl-CoA deacetylase, Vol. 14, 2.4.1.147 acetylgalactosaminyl-O-glycosyl-glycoprotein b- p. 482 1,3-N-acetylglucosaminyltransferase, Vol. 32, 3.5.1.29 2-(acetamidomethylene)succinate hydrolase, p. 287 Vol.
    [Show full text]
  • (12) United States Patent (10) Patent No.: US 8,044,166 B2 Fiene Et Al
    USOO80441 66B2 (12) United States Patent (10) Patent No.: US 8,044,166 B2 Fiene et al. (45) Date of Patent: Oct. 25, 2011 (54) PROCESS FOR PREPARING (56) References Cited PENTAMETHYLENE 1.5-DIISOCYANATE U.S. PATENT DOCUMENTS (75) Inventors: Martin Fiene, Niederkirchen (DE); 5,103,045 A * 4/1992 Robin et al. .................. 560,335 Eckhard Stroefer, Mannheim (DE); 2005, OOO3497 A1* 1/2005 Nishi et al. .................... 435/128 Wolfgang Siegel, Limburgerhof (DE); Stephan Freyer, Neustadt (DE); Oskar FOREIGN PATENT DOCUMENTS DE 1900 514 8, 1970 Zelder, Speyer (DE); Gerhard Schulz, DE 26 25 O75 A1 12, 1977 Bad Duerkheim (DE) DE 2625 O75 * 12, 1977 EP O 259 233 A2 3, 1988 (73) Assignee: BASF Aktiengesellschaft, EP O 161419 B1 8, 1989 Ludwigshafen (DE) EP 1482 055 A1 12, 2004 GB 1 225 450 3, 1971 (*) Notice: Subject to any disclaimer, the term of this WO WOO3,O99768 A1 12/2003 patent is extended or adjusted under 35 WO WO 2006.005603 A1 1, 2006 U.S.C. 154(b) by 336 days. OTHER PUBLICATIONS (21) Appl. No.: 12/373,088 Database Caplus Chemical Abstracts Service, Columbus, Ohio, US 1979, T. Lesiak etal "Preparation of Aliphatic diisocyanates without (22) PCT Fled: Jul. 25, 2007 using phosgene” XP002456997.* Enzyme Handbook, Dec 1, 1982, by Asakura Shoten.* (86) PCT NO.: PCT/EP2007/057646 Preparation of Aliphatic Diisocyanates without using Phosgene, Jun. 1969, by Sea Lesiak.* S371 (c)(1), T. Lesiak, et al., “Preparation of aliphatic diisocyanates without using (2), (4) Date: Jan. 9, 2009 phosgene'. Journal f. prakt. Chemie. Band 321, XP002456997.
    [Show full text]