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The Enzyme Database: New Enzymes 06/27/2006 05:11 PM The Enzyme Database: New Enzymes 06/27/2006 05:11 PM Home Search Enzymes by Class New/Amended Enzymes Statistics Forms Advanced Search Information Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB) Proposed Changes to the Enzyme List The entries below are proposed additions and amendments to the Enzyme Nomenclature list. They were prepared for the NC- IUBMB by Keith Tipton, Sinéad Boyce, Gerry Moss and Hal Dixon, with occasional help from other Committee members, and were put on the web by Gerry Moss. Comments and suggestions on these draft entries should be sent to Professor K.F. Tipton and Dr S. Boyce (Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland) by 20 May 2006, after which, the entries will be made official and will be incorporated into the main enzyme list. To prevent confusion please do not quote new EC numbers until they are incorporated into the main list. Many thanks to those of you who have submitted details of new enzymes or updates to existing enzymes. An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry. Contents *EC 1.1.1.262 4-hydroxythreonine-4-phosphate dehydrogenase EC 1.1.1.289 sorbose reductase EC 1.1.1.290 4-phosphoerythronate dehydogenase EC 1.1.99.19 transferred *EC 1.2.1.10 acetaldehyde dehydrogenase (acetylating) EC 1.2.1.71 succinylglutamate-semialdehyde dehydrogenase EC 1.2.1.72 erythrose-4-phosphate dehydrogenase EC 1.2.99.1 transferred *EC 1.3.99.19 quinoline-4-carboxylate 2-oxidoreductase *EC 1.4.3.5 pyridoxal 5′-phosphate synthase *EC 1.4.4.2 glycine dehydrogenase (decarboxylating) EC 1.7.1.13 queuine synthase *EC 1.8.1.4 dihydrolipoyl dehydrogenase *EC 1.11.1.14 lignin peroxidase EC 1.11.1.16 versatile peroxidase *EC 1.13.11.11 tryptophan 2,3-dioxygenase *EC 1.13.11.19 cysteamine dioxygenase EC 1.13.11.42 deleted EC 1.13.11.52 indoleamine 2,3-dioxygenase EC 1.13.11.53 acireductone dioxygenase (Ni2+-requiring) EC 1.13.11.54 acireductone dioxygenase [iron(II)-requiring] EC 1.13.11.55 sulfur oxygenase/reductase EC 1.13.12.14 chlorophyllide-a oxygenase EC 1.14.13.65 deleted EC 1.14.13.101 senecionine N-oxygenase *EC 1.14.99.3 heme oxygenase EC 1.17.99.4 uracil/thymine dehydrogenase *EC 2.1.2.10 aminomethyltransferase *EC 2.3.1.11 thioethanolamine S-acetyltransferase *EC 2.3.1.38 [acyl-carrier-protein] S-acetyltransferase *EC 2.3.1.39 [acyl-carrier-protein] S-malonyltransferase *EC 2.3.1.41 β-ketoacyl-acyl-carrier-protein synthase I *EC 2.3.1.109 arginine N-succinyltransferase EC 2.3.1.177 biphenyl synthase EC 2.3.1.178 diaminobutyrate acetyltransferase EC 2.3.1.179 β-ketoacyl-acyl-carrier-protein synthase II EC 2.3.1.180 β-ketoacyl-acyl-carrier-protein synthase III EC 2.3.1.181 lipoyl(octanoyl) transferase *EC 2.4.1.195 N-hydroxythioamide S-β-glucosyltransferase http://www.enzyme-database.org/newenz.php?sp=off Page 1 of 48 The Enzyme Database: New Enzymes 06/27/2006 05:11 PM EC 2.4.1.243 6G-fructosyltransferase EC 2.4.1.244 N-acetyl-β-glucosaminyl-glycoprotein 4-β-N-acetylgalactosaminyltransferase *EC 2.6.1.52 phosphoserine transaminase *EC 2.6.1.76 diaminobutyrate—2-oxoglutarate transaminase EC 2.6.1.81 succinylornithine transaminase EC 2.6.99.2 pyridoxine 5′-phosphate synthase *EC 2.7.1.151 inositol-polyphosphate multikinase EC 2.7.1.158 inositol-pentakisphosphate 2-kinase EC 2.7.1.159 inositol-1,3,4-trisphosphate 5/6-kinase EC 2.7.4.22 UMP kinase EC 2.7.7.63 lipoate—protein ligase *EC 2.8.1.6 biotin synthase EC 2.8.1.8 lipoyl synthase EC 3.1.3.76 lipid-phosphate phosphatase EC 3.1.13.5 ribonuclease D *EC 3.1.26.3 ribonuclease III *EC 3.2.1.81 β-agarase *EC 3.2.1.83 κ-carrageenase EC 3.2.1.155 xyloglucan-specific exo-β-1,4-glucanase EC 3.2.1.157 ι-carrageenase EC 3.2.1.158 α-agarase EC 3.2.1.159 α-neoagaro-oligosaccharide hydrolase EC 3.2.1.161 β-apiosyl-β-glucosidase EC 3.3.2.3 transferred *EC 3.3.2.6 leukotriene-A4 hydrolase *EC 3.3.2.7 hepoxilin-epoxide hydrolase EC 3.3.2.9 microsomal epoxide hydrolase EC 3.3.2.10 soluble epoxide hydrolase EC 3.3.2.11 cholesterol-5,6-oxide hydrolase EC 3.4.21.87 transferred EC 3.4.23.49 omptin EC 3.5.1.94 γ-glutamyl-γ-aminobutyrate hydrolase EC 3.5.1.95 N-malonylurea hydrolase EC 3.5.1.96 succinylglutamate desuccinylase *EC 3.5.2.1 barbiturase EC 3.5.3.23 N-succinylarginine dihydrolase *EC 3.6.3.5 Zn2+-exporting ATPase *EC 3.6.3.44 xenobiotic-transporting ATPase EC 3.6.3.45 deleted *EC 4.1.1.21 phosphoribosylaminoimidazole carboxylase EC 4.1.1.86 diaminobutyrate decarboxylase *EC 4.1.2.8 indole-3-glycerol-phosphate lyase EC 4.1.3.39 4-hydroxy-2-oxovalerate aldolase *EC 4.2.1.60 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase EC 4.2.1.108 ectoine synthase *EC 4.2.3.9 aristolochene synthase EC 4.2.3.22 germacradienol synthase EC 4.2.3.23 germacrene-A synthase EC 4.2.3.24 amorpha-4,11-diene synthase EC 4.2.3.25 S-linalool synthase EC 4.2.3.26 R-linalool synthase EC 4.4.1.24 sulfolactate sulfo-lyase EC 4.4.1.25 L-cysteate sulfo-lyase EC 5.3.3.14 trans-2-decenoyl-[acyl-carrier protein] isomerase EC 5.4.99.18 5-(carboxyamino)imidazole ribonucleotide mutase *EC 6.3.2.6 phosphoribosylaminoimidazolesuccinocarboxamide synthase *EC 6.3.2.27 aerobactin synthase EC 6.3.4.18 5-(carboxyamino)imidazole ribonucleotide synthase *EC 1.1.1.262 Common name: 4-hydroxythreonine-4-phosphate dehydrogenase Reaction: 4-(phosphonooxy)-L-threonine + NAD+ = (2S)-2-amino-3-oxo-4-phosphonooxybutanoate + NADH + H+ For diagram of pyridoxal biosynthesis, click here Other name(s): NAD+-dependent threonine 4-phosphate dehydrogenase; L-threonine 4-phosphate dehydrogenase; http://www.enzyme-database.org/newenz.php?sp=off Page 2 of 48 The Enzyme Database: New Enzymes 06/27/2006 05:11 PM 4-(phosphohydroxy)-L-threonine dehydrogenase; PdxA Systematic name: 4-(phosphonooxy)-L-threonine:NAD+ oxidoreductase Comments: The product of the reaction undergoes decarboxylation to give 3-amino-2-oxopropyl phosphate. In Escherichia coli, the coenzyme pyridoxal 5′-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4- phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4- hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5′-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5′-phosphate as substrate). Links to other databases: BRENDA, ERGO, EXPASY, GO, IUBMB, KEGG, PDB References: 1. Cane, D.E., Hsiung, Y., Cornish, J.A., Robinson, J.K and Spenser, I.D. Biosynthesis of vitamine B6: The oxidation of L-threonine 4-phosphate by PdxA. J. Am. Chem. Soc. 120 (1998) 1936– 1937. 2. Laber, B., Maurer, W., Scharf, S., Stepusin, K. and Schmidt, F.S. Vitamin B6 biosynthesis: formation of pyridoxine 5′-phosphate from 4-(phosphohydroxy)-L-threonine and 1-deoxy-D- xylulose-5-phosphate by PdxA and PdxJ protein. FEBS Lett. 449 (1999) 45–48. [PMID: 10225425] 3. Sivaraman, J., Li, Y., Banks, J., Cane, D.E., Matte, A. and Cygler, M. Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway. J. Biol. Chem. 278 (2003) 43682–43690. [PMID: 12896974] [EC 1.1.1.262 created 2000, modified 2006] EC 1.1.1.289 Common name: sorbose reductase Reaction: D-glucitol + NADP+ = L-sorbose + NADPH + H+ For diagram of reaction, click here Glossary: L-sorbose = L-xylo-hex-2-ulose Other name(s): Sou1p Systematic name: D-glucitol:NADP+ oxidoreductase Comments: The reaction occurs predominantly in the reverse direction. This enzyme can also convert D- fructose into D-mannitol, but more slowly. Belongs in the short-chain dehydrogenase family. References: 1. Greenberg, J.R., Price, N.P., Oliver, R.P., Sherman, F. and Rustchenko, E. Candida albicans SOU1 encodes a sorbose reductase required for L-sorbose utilization. Yeast 22 (2005) 957–969. [PMID: 16134116] 2. Greenberg, J.R., Price, N.P., Oliver, R.P., Sherman, F. and Rustchenko, E. Erratum report: Candida albicans SOU1 encodes a sorbose reductase required for L-sorbose utilization. Yeast 22 (2005) 1171 only. 3. Sugisawa, T., Hoshino, T. and Fujiwara, A. Purification and properties of NADPH-linked L- sorbose reductase from Gluconobacter melanogenus N44-1. Agric. Biol. Chem. 55 (1991) 2043– 2049. 4. Shinjoh, M., Tazoe, M. and Hoshino, T. NADPH-dependent L-sorbose reductase is responsible for L-sorbose assimilation in Gluconobacter suboxydans IFO 3291. J. Bacteriol. 184 (2002) 861– 863. [PMID: 11790761] [EC 1.1.1.289 created 2006] EC 1.1.1.290 Common name: 4-phosphoerythronate dehydogenase Reaction: 4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH + H+ For diagram of pyridoxal biosynthesis, click here Other name(s): PdxB; PdxB 4PE dehydrogenase; 4-O-phosphoerythronate dehydrogenase Systematic name: 4-phospho-D-erythronate:NAD+ 2-oxidoreductase Comments: This enzyme catalyses the second step in the biosynthesis of the coenzyme pyridoxal 5′-phosphate in Escherichia coli.
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