An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.
Recommended name: glycerol-1-phosphate dehydrogenase [NAD(P)]
Reaction: sn-glycerol-1-phosphate + NAD(P) = glycerone phosphate + NAD(P)H2
Systematic name: sn-glycerol-1-phosphate:NAD(P) 2-oxidoreductase
Comments: This enzyme is responsible for the formation of Archaea-specific glycerophosphate and is stereospecifically different from EC 1.1.1.94, sn-glycerol-3-phosphate dehydrogenase.
References:
1. Koga, Y., Kyuragi, T., Nishihara, M. and Sone, N. Did archaeal and bacterial cells arise independently from noncellular precursors? A hypothesis stating that the advent of membrane phospholipid with enantiomeric glycerophosphate backbones caused the separation of the two lines of descent. J. Mol. Evol. 46 (1998) 54-63. [Medline UI: 98080610]
Recommended name: 4-hydroxythreonine-4-phosphate dehydrogenase
Reaction: 4-(phosphonooxy)-threonine + NAD = 2-amino-3-oxo-4-phosphonooxybutyrate + NADH2
Other name(s): NAD-dependent threonine 4-phosphate dehydrogenase; L-threonine 4-phosphate dehydrogenase; 4-(phosphohydroxy)-L-threonine dehydrogenase;PdxA
Systematic name: 4-(phosphonooxy)threonine:NAD oxidoreductase
Comments: The product of the reaction undergoes decarboxylation to give 3-amino-2-oxopropyl phosphate.
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.
Recommended name: 1,5-anhydro-D-fructose reductase
Reaction: 1,5-anhydro-D-glucitol + NADP = 1,5-anhydro-D-fructose + NADPH2
Systematic name: 1,5-anhydro-D-glucitol:NADP oxidoreductase
Comments: Also reduces pyridine-3-aldehyde and 2,3-butanedione. Acetaldehyde, 2-dehydroglucose (glucosone) and glucuronate are poor substrates, but there is no detectable action on glucose, mannose and fructose.
References:
1. Sakuma, M., Kametani, S. and Akanuma, H. Purification and some properties of a hepatic NADPH-dependent reductase that specifically acts on 1,5-anhydro-D-fructose. J. Biochem. (Tokyo) 123 (1998) 198-193.
Recommended name: L-idonate 5-dehydrogenase
Reaction: L-idonate + NAD(P) = 5-dehydrogluconate + NAD(P)H2
Systematic name: L-idonate:NAD(P) oxidoreductase
Comments: The enzyme from Escherichia coli cannot oxidize D-gluconate to form 5-dehydrogluconate, a reaction that is catalysed by EC 1.1.1.69, gluconate 5-dehydrogenase.
References:
1. Bausch, C., Peekhaus, N., Utz, C., Blais, T., Murray, E., Lowary, T. and Conway, T. Sequence analysis of the GntII (subsidiary) system for gluconate metabolism reveals a novel pathway for L-idonic acid catabolism in Escherichia coli. J. Bacteriol. 180 (1998) 3704-3710. [Medline UI: 98324983]
Recommended name: 3-methylbutanal reductase
Reaction: 3-methylbutanol + NAD(P) = 3-methylbutanal + NAD(P)H2
Systematic name: 3-methylbutanol:NAD(P) oxidoreductase
Comments: The enzyme purified from Saccharomyces cerevisiae catalyses the reduction of a number of straight-chain and branched aldehydes, as well as some aromatic aldehydes.
References:
1. van Iersel, M.F.M., Eppink, M.H.M., van Berkel, W.J.H., Rombouts, F.M. and Abee, T. Purification and characterization of a novel NADP-dependent branched-chain alcohol dehydrogenase from Saccharomyces cerevisiae. Appl. Environ. Microbiol. 63 (1997) 4079-4082. [Medline UI: 97468485]
2. Ven Nedervelde, L., Verlinden, V., Philipp, D. and Debourg, A. Purification and characterization of yeast 3-methyl butanal reductases involved in the removal of wort carbonyls during fermentation. Proc. 26th Congr.-Eur. Brew. Conv. (1997) 447-454.
Recommended name: coniferyl-aldehyde dehydrogenase
Reaction: coniferyl aldehyde + H2O + NAD(P) = ferulate + NAD(P)H2
For reaction pathway click here.
Systematic name: coniferyl aldehyde:NAD(P) oxidoreductase
Comments: Also oxidizes other aromatic aldehydes, but not aliphatic aldehydes.
References:
1. Achterholt, S., Priefert, H. and Steinbuchel, A. Purification and characterization of the coniferyl 2-hydroxy-1,4-benzoquinonealdehyde dehydrogenase from Pseudomonas sp. Strain HR199 and molecular characterization of the gene. J. Bacteriol. 180 (1998) 4387-4391. [Medline UI: 98389649]
Deleted entry: Not approved as the enzyme was shown to be a dehydrogenase and not an oxidase (see EC 1.5.99.12, cytokinin dehydrogenase)
Recommended name: 2-hydroxy-1,4-benzoquinone reductase
Reaction: 1,2,4-trihydroxybenzene + NAD = hydroxybenzoquinone + NADH2
Other name(s): hydroxybenzoquinone reductase
Systematic name: 1,2,4-trihydroxybenzene:NAD oxidoreductase
Comments: A flavoprotein (FMN) that differs in substrate speificity from other quinone reductases. The enzyme in Burkholderia cepacia is inducible by 2,4,5-trichlorophenoxyacetate.
References:
1. Zaborina, O., Daubaras, D.L., Zago, A., Xun, L., Saido, K., Klem,T., Nikolic, D. and Chakrabarty, A.M. Novel pathway for conversion of chlorohydroxyquinol to maleylacetate in Burkholderia cepacia AC1100. J. Bacteriol. 180 (1998) 4667-4675. [Medline UI: 98389686]
Recommended name: phosphoadenylyl-sulfate reductase (thioredoxin)
Reaction: adenosine 3',5'-bisphosphate + sulfite + oxidized thioredoxin = 3'-phosphoadenylyl sulfate + reduced thioredoxin
Glossary and synonyms entries:
3'-phosphoadenylyl sulfate: nucleotide sulfate
Other name(s): PAPS reductase, thioredoxin-dependent; PAPS reductase; thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase; 3'-phosphoadenylylsulfate reductase; thioredoxin:3'-phospho-adenylylsulfate reductase; phosphoadenosine-phosphosulfate reductase
Systematic name: adenosine 3',5'-bisphosphate,sulfite:oxidized-thioredoxin oxidoreductase (3'-phosphoadenosine-5'-phosphosulfate -forming)
Comments: specific for PAPS. The enzyme from E. coli will use thioredoxins from other species.
References:
1. Berendt, U., Haverkamp, T., Prior, A., Schwenn, J.D. Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. Eur. J. Biochem. 233 (1995) 347-356. [Medline UI: 96061968]
Recommended name: adenylyl-sulfate reductase (glutathione)
Reation: AMP + sulfite + oxidized glutathione = adenylyl sulfate + glutathione
Other name(s): plant-type 5'-adenylylsulfate reductase; 5'-adenylylsulfate reductase (also used for EC 1.8.99.2)
Systematic name: AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5'-phosphosulfate-forming)
Comments: This enzyme differs from EC 1.8.99.2, adenylyl-sulfate reductase (acceptor), in using glutathione as the reductant. Glutathione can be replaced by γ-glutamylcysteine or dithiothreitol, but not by thioredoxin, glutaredoxin or mercaptoethanol. The enzyme from the mouseear cress, Arabidopsis thaliana, contains a glutaredoxin-like domain. The enzyme is also found in other photosynthetic eukaryotes, e.g., the Madagascar periwinkle, Catharanthus roseus and the hollow green seaweed, Enteromorpha intestinalis.
References:
1. Gutierrez-Marcos, J.F., Roberts, M.A., Campbell, E.I. and Wray, J.L. Three members of a novel small gene-family from Arabidopsis thaliana able to complement functionally an Escherichia coli mutant defective in PAPS reductase activity encode proteins with a thioredoxin-like domain and 'APS reductase' activity. Proc. Natl. Acad. Sci. USA 93 (1996) 13377-13382. [Medline UI: 97075173]
2. Setya, A., Murillo, M. and Leustek, T. Sulfate reduction in higher plants: Molecular evidence for a novel 5-adenylylphosphosulfate (APS) reductase. Proc. Natl. Acad. Sci. USA 93 (1996) 13383-13388. [Medline UI: 97075174]
3. Bick, J.A., Aslund, F., Cen, Y. and Leustek, T. Glutaredoxin function for the carboxyl-terminal domain of the plant-type 5'-adenylylsulfate reductase. Proc. Natl. Acad. Sci. USA 95 (1998) 8404-8409. [PMID: 9653199]
[EC 1.8.99.4 Transferred entry: Now EC 1.8.4.8, phosphoadenylyl-sulfate reductase (thioredoxin)]
Recommended name: linoleate diol synthase
Reaction: linoleate + O2 = (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate
Other name(s): linoleate (8R)-dioxygenase
Systematic name: linoleate:oxygen 7S,8S-oxidoreductase
Comments: Oleate and linolenate are also substrates, whereas stearate, elaidate, γ-linolenate, arachidonate and eicosapentaenate are not. This enzyme differs from lipoxygenase (EC 1.13.11.12) because it catalyses the formation of a hydroperoxide without affecting the double bonds of the substrate.
References:
1. Brodowsky, I.D., Hamberg, M. and Oliw, E.H. A linoleic acid 8(R)-dioxygenase and hydroperoxide isomerase of the fungus Gaeumannomyces graminis: Biosynthesis of 8(R)-hydroxylinoleic acid and 7(S),8(S)-dihydroxylinoleic acid from 8(R)-hydroperoxylinoleic acid. J. Biol. Chem. 267 (1992) 1473 8-14745. [Medline UI: 92340511]
2. Hamberg, M., Zhang, L.-Y., Brodowsky, I.D. and Oliw, E.H. Sequential oxygenation of linoleic acid in the fungus Gaeumannomyces graminis: stereochemistry of dioxygenase and hydroperoxide isomerase reactions. Arch. Biochem. Biophys. 309 (1994) 77-80. [Medline UI: 94161560]
3. Hornsten, L., Su, C., Osbourn, A.E., Garosi, P., Hellman, U., Wernstedt, C. and Oliw, E.H. Cloning of linoleate diol synthase reveals homology with prostaglandin H synthases. J. Biol. Chem. 274 (1999) 28219-28224. [Medline UI: 99428486]
4. Oliw, E.H., Su, C., Skogstrom, T. and Benthin, G. Analysis of novel hydroperoxides and other metabolites of oleic, linoleic and linolenic acids by liquid chromatography-mass spectrometry with ion trap MSn. Lipids 33 (1998) 843-852. [Medline UI: 98449580]
5. Su, C. and Oliw, E.H. Purification and characterization of linoleate 8-dioxygenase from the fungus Gaeumannomyces graminis as a novel hemoprotein. J. Biol. Chem. 271 (1996) 14112-14118. [Medline UI: 96278864]
6. Su, C., Sahlin, M. and Oliw, E.H. A protein radical and ferryl intermediates are generated by linoleate diol synthase, a ferric hemeprotein with dioxygenase and hydroperoxide isomerase activities. J. Biol. Chem. 273 (1998) 20744-20751. [Medline UI: 98361938]
Recommended name: linoleate 11-lipoxygenase
Reaction: linoleate + O2 = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate
Glossary:
Other name(s): linoleate dioxygenase, manganese lipoxygenase
Systematic name: linoleate:oxygen 11S-oxidoreductase
Comments: The product (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate, is converted, more slowly, into (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate. The enzyme from the fungus Gaeumannomyces graminis requires Mn2+. It also acts on α-linolenate, whereas γ-linolenate is a poor substrate. Oleate and arachidonate are not substrates.
References:
1. Hamberg, M., Su, C. and Oliw, E.H. Manganese lipoxygenase: Discovery of bis-allylic hydroperoxide as product and intermediate in a lipoxygenase reaction. J. Biol. Chem. 273 (1998) 13080-13088. [Medline UI: 98250760]
2. Oliw, E.H., Su, C., Skogstrom, T. and Benthin, G. Analysis of novel hydroperoxides and other metabolites of oleic, linoleic, and linolenic acids by liquid chromatography-mass spectrometry with ion trap MSn. Lipids 33 (1998) 843-852. [Medline UI: 98449580]
3. Su, C. and Oliw, E.H. Manganese lipoxygenase: Purification and characterization. J. Biol. Chem. 273 (1998) 13072-13079. [Medline UI: 98250759]
*EC 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
Recommended name: phytanoyl-CoA dioxygenase
Reaction: phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2
Glossary entries
Other name(s): phytanoyl-CoA hydroxylase
Systematic name: phytanoyl-CoA, 2-oxoglutarate:oxygen oxidoreductase (2-hydroxylating)
Comments: Part of the peroxisomal phytanic acid α-oxidation pathway. Requires Fe2+ and ascorbate.
References:
1. Jansen, G.A., Mihalik, S.J., Watkins, P.A., Jakobs, C., Moser, H.W. and Wanders, R.J.A. Characterization of phytanoyl-CoA hydroxylase in human liver and activity measurements in patients with peroxisomal disorders. Clin. Chim. Acta 271 (1998) 203-211. [Medline UI: 98225008]
2. Jansen, G.A., Mihalik, S.J., Watkins, P.A., Moser, H.W., Jakobs, C., Denis, S. and Wanders, R.J.A. Phytanoyl-CoA hydroxylase is present in human liver, located in peroxisomes, and deficient in Zellweger syndrome: direct, unequivocal evidence for the new, revised pathway of phytanic acid α-oxidation in humans. Biochem. Biophys. Res. Commun. 229 (1996) 205-210. [Medline UI: 97112427]
3. Jansen, G.A., Ofman, R., Ferdinandusse, S., Ijlst, L., Muijsers, A.O., Skjeldal, O.H., Stokke, O., Jakobs, C., Besley, G.T.N., Wraith, J.E. and Wanders, R.J.A. Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene. Nat. Genet. 17 (1997) 190-193. [Medline UI: 97467731]
4. Mihalik, S.J., Rainville, A.M. and Watkins, P.A. Phytanic acid α-oxidation in rat liver peroxisomes. Production of α-hydroxyphytanoyl-CoA and formate is enhanced by dioxygenase cofactors. Eur. J. Biochem. 232 (1995) 545-551.
5. Mihalik, S.J., Morrell, J.C., Kim, D., Sacksteder, K.A., Watkins, P.A. and Gould, S.J. Identification of PAHX, a Refsum disease gene. Nat. Genet. 17 (1997) 185-189. [Medline UI: 97467730]
Recommended name: nitric oxide dioxygenase
Reaction: 2 NO + 2 O2 + NAD(P)H2 = 2 NO3-+ NAD(P) + 2 H+
Systematic name: nitric oxide, NAD(P)H2:oxygen oxidoreductase
Comments: A flavohemoglobin (FAD). It has been proposed that FAD functions as the electron carrier from NADPH2 to the ferric heme prosthetic group.
References:
1. Gardner, P.R., Costantino, G. and Salzman, A.L. Constitutive and adaptive detoxification of nitric oxide in Escherichia coli. Role of nitric-oxide dioxygenase in the protection of aconitase. J. Biol. Chem. 273 (1998) 26528-26533. [Medline UI: 98434561]
2. Gardner, P.R., Gardner, A.M., Martin, L.A. and Salzman, A.L. Nitric oxide dioxygenase: an enzymic function for flavohemoglobin. Proc. Natl. Acad. Sci. USA 95 (1998) 10378-10383. [Medline UI: 98393652]
Recommended name: quinine 3-monooxygenase
Reaction: quinine + NADPH2 + O2 = 3-hydroxyquinine + NADP + H2O
Glossary entries:
Other name(s): quinine 3-hydroxylase
Systematic name: quinine, NADPH2:oxygen oxidoreductase
References:
1. Relling, M.V., Evans, R., Dass, C., Desiderio, D.M. and Nemec, J. Human cytochrome P450 metabolism of teniposide and etoposide. J. Pharmacol. Exp. Ther. 261 (1992) 491-496. [Medline UI: 92251624]
2. Zhang, H., Coville, P.F., Walker, R.J., Miners, J.O., Birkett, D.J. and Wanwimolruk, S. Evidence for involvement of human CYP3A in the 3-hydroxylation of quinine. Br. J. Clin. Pharmacol. 43 (1997) 245-252. [Medline UI: 97243737]
3. Zhao, X.-J., Kawashiro, T. and Ishizaki, T. Mutual inhibition between quinine and etoposide by human liver microsomes. Evidence for cytochrome P4503A4 involvement in their major metabolic pathways. Drug Metab. Dispos. 26 (1998) 188-191. [Medline UI: 98122830]
4. Zhao, X.-J., Yokoyama, H., Chiba, K., Wanwimolruk, S. and Ishizaki, T. Identification of human cytochrome P450 isoforms involved in the 3-hydroxylation of quinine by human liver microsomes and nine recombinant human cytochromes P450. J. Pharmacol. Exp. Ther. 279 (1996) 1327-1334. [Medline UI: 97123108]
Recommended name: 4-hydroxyphenylacetaldehyde oxime monooxygenase
Reaction: 4-hydroxyphenylacetaldehyde oxime + NADPH2 + O2 = 4-hydroxymandelonitrile + NADP + 2 H2O
Other name(s): 4-hydroxybenzeneacetaldehyde oxime monooxygenase; cytochrome P450II-dependent monooxygenase; NADPH-cytochrome P450 reductase (CYP71E1)
Systematic name: 4-hydroxyphenylacetaldehyde oxime, NADPH2:oxygen oxidoreductase
Comments: Part of the biosynthetic pathway for dhurrin in Sorghum bicolor.
References:
1. MacFarlane, I.J., Lees, E.M. and Conn, E.E. The in vitro biosynthesis of dhurrin, the cyanogenic glycoside of Sorghum bicolor. J. Biol. Chem. 250 (1975) 4708-4713. [Medline UI: 75189435]
2. Shimada, M. and Conn, E.E. The enzymatic conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile Arch. Biochem. Biophys. 180 (1977) 199-207 [Medline UI: 77180424]
Recommended name: choline monooxygenase
Reaction: choline + O2 + 2 reduced ferredoxin + 2 H+ = betaine aldehyde hydrate + H2O + 2 oxidized ferredoxin
Systematic name: choline, reduced ferredoxin: oxygen oxidoreductase
Comments: The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+.
References:
1. Brouquisse, R., Weigel, P., Rhodes, D., Yocum, C.F. and Hanson, A.D. Evidence for a ferredoxin-dependent choline monooxygenase from spinach chloroplast stroma. Plant Physiol. 90 (1989) 322-329.
2. Burnet, M., Lafontaine, P.J. and Hanson, A.D. Assay, purification, and partial characterization of choline monooxygenase from spinach. Plant Physiol. 108 (1995) 581-588.
3. Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. Glycine betaine synthesis in transgenic tobacco expressing choline monooxygenase is limited by the endogenous choline supply. Plant J. 16 (1998) 101-110.
4. Rathinasabapathi, B., Burnet, M., Russell, B.L., Gage, D.A., Liao, P., Nye, G.J., Scott, P., Golbeck, J.H. and Hanson, A.D. Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning. Proc. Natl. Acad. Sci. USA 94 (1997) 3454-3458. [Medline UI: 97250559]
5. Russell, B.L., Rathinasabapathi, B. and Hanson, A.D. Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth. Plant Physiol. 116 (1998) 859-865.
EC 1.14.19 With oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
This sub-subclass differs from others in subclass EC 1.14 in that hydrogen atoms removed from the two donors are combined with molecular oxygen to form two molecules of water
Recommended name: stearoyl-CoA 9-desaturase
Reaction: stearoyl-CoA + AH2 + O2 = oleoyl-CoA + A + 2 H2O
Other name(s): acyl-CoA desaturase; fatty acid desaturase; δ9-desaturase
Systematic name: stearoyl-CoA, hydrogen-donor:oxygen oxidoreductase
Comments: An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome-b5 reductase. Formerly EC 1.14.99.5.
References:
1. Fulco, A.J. and Bloch, K. Cofactor requirements for the formation of δ9-unsaturated fatty acids in Mycobacterium phlei. J. Biol. Chem. 239 (1964) 993-997.
2. Oshino, N., Imai, Y. and Sato, R. Electron-transfer mechanism associated with fatty acid desaturation catalyzed by liver microsomes. Biochim. Biophys. Acta 128 (1966) 13-27. [Medline UI: 67182592]
3. Oshino, N., Imai, Y. and Sato, R. A function of cytochrome b5 in fatty acid desaturation by rat liver microsomes. J. Biochem. (Tokyo) 69 (1971) 155-167. [Medline UI: 71111382]
4. Strittmatter, P., Sputz, L., Corcoran, D., Rogers, M.J., Setlow, B. and Redline, R. Purification and properties of rat liver microsomal stearyl coenzyme A desaturase. Proc. Natl. Acad. Sci. USA 71 (1974) 4565-4569. [Medline UI: 75065561]
Recommended name: acyl-[acyl-carrier-protein] desaturase
Reaction: stearoyl-[acyl-carrier protein] + reduced acceptor + O2 = oleoyl-[acyl-carrier protein] + acceptor + 2 H2O
Other name(s): stearyl acyl carrier protein desaturase; stearyl-ACP desaturase
Systematic name: acyl-[acyl-carrier-protein], hydrogen-donor:oxygen oxidoreductase
Comments: The enzyme from safflower is specific for stearoyl-CoA; that from Euglena acts on derivatives of a number of long-chain fatty acids. Requires ferredoxin. Formerly EC 1.14.99.6.
References:
1. Jaworski, J.G. and Stumpf, P.K. Fat metabolism in higher plants. Properties of a soluble stearyl-acyl carrier protein desaturase from maturing Carthamus tinctorius. Arch. Biochem. Biophys. 162 (1974) 158-165. [Medline UI: 74173330]
2. Nagai, J. and Bloch, K. Enzymatic desaturation of stearyl acyl carrier protein. J. Biol. Chem. 243 (1968) 4626-4633. [Medline UI: 69012765]
Recommended name: linoleoyl-CoA desaturase
Reaction: linoleoyl-CoA + AH2 + O2 = γ-linolenoyl-CoA + A + 2 H2O
Other name(s):δ6-desaturase; δ6-fatty acyl-CoA desaturase; δ6-acyl CoA desaturase; fatty acid δ6-desaturase; fatty acid 6-desaturase; linoleate desaturase; linoleic desaturase; linoleic acid desaturase; linoleoyl CoA desaturase; linoleoyl-coenzyme A desaturase; long-chain fatty acid δ6-desaturase
Systematic name: linoleoyl-CoA,hydrogen-donor:oxygen oxidoreductase
Comments: An iron protein. The rat liver enzyme is an enzyme system involving cytochrome b5 and EC 1.6.2.2, cytochrome- b5 reductase. Formerly EC 1.14.99.25.
References:
1. Okayasu, T., Nagao, M., Ishibashi, T. and Imai, Y. Purification and partial characterization of linoleoyl-CoA desaturase from rat liver microsomes. Arch. Biochem. Biophys. 206 (1981) 21-28. [Medline UI: 81158904]
[EC 1.14.99.5 Transferred entry: now EC 1.14.19.1, stearoyl-CoA 9-desaturase]
[EC 1.14.99.6 Transferred entry: now EC 1.14.19.2, acyl-[acyl-carrier-protein] desaturase]
[EC 1.14.99.25 Transferred entry: now EC 1.14.19.3, linoleoyl-CoA desaturase]
Recommended name: thiophene-2-carbonyl-CoA monooxygenase
Reaction: thiophene-2-carbonyl-CoA + AH2 + O2 = 5-hydroxythiophene-2-carbonyl-CoA + A + H2O
Other name(s): thiophene-2-carboxyl-CoA dehydrogenase; thiophene-2-carboxyl-CoA hydroxylase; thiophene-2-carboxyl-CoA monooxygenase
Systematic name: thiophene-2-carbonyl-CoA, hydrogen-donor:oxygen oxidoreductase
Comments: A molybdenum enzyme. Highly specific for thiophene-2-carbonyl-CoA. Tetrazolium salts can act as electron acceptors.
References:
1. Bambauer, A., Rainey, F.A., Stackebrandt, E. and Winter, J. Characterization of Aquamicrobium defluvii gen. nov. sp. nov., a thiophene-2-carboxylate-metabolizing bacterium from activated sludge. Arch. Microbiol. 169 (1998) 293-302. [Medline UI: 98200555]
Recommended name: 3'-demethylstaurosporine O-methyltransferase
Reaction: S-adenosyl-L-methionine + 3'-demethylstaurosporine = S-adenosyl-L-homocysteine + staurosporine
Other name(s): 3'-demethoxy-3'-hydroxystaurosporine O-methyltransferase; staurosporine synthase
Systematic name: S-adenosyl-L-methionine:3'-demethylstaurosporine O-methyltransferase
Comments: Catalyses the final step in the biosynthesis of staurosporine, an alkaloidal antibiotic that is a potent inhibitor of protein kinases, especially protein kinase C.
References:
1. Weidner, S., Kittelmann, M., Goeke, K., Ghisalba, O. and Zahner, H. 3'-Demethoxy-3'-hydroxystaurosporine-O-methyltransferase from Streptomyces longisporoflavus catalyzing the last step in the biosynthesis of staurosporine. J. Antibiot. (Tokyo) 51 (1998) 679-682. [Medline UI: 98394378]
Recommended name: phosphoribosylglycinamide formyltransferase
Reaction: 10-formyltetrahydrofolate + N1-(5-phospho-D-ribosyl)glycinamide = tetrahydrofolate + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide
For reaction pathway click here.
Other name(s): 2-amino-N-ribosylacetamide 5'-phosphate transformylase; GAR formyltransferase; GAR transformylase; glycinamide ribonucleotide transformylase; GAR TFase; 5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide ribonucleotide transformylase
Systematic name: 10-formyltetrahydrofolate:5'-phosphoribosylglycinamide N-formyltransferase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
WIT,
CAS registry number: 9032-02-4
References:
1. Hartman, S.C. and Buchanan, J.M. Biosynthesis of the purines. XXVI. The identification of the formyl donors of the transformylation reaction. J. Biol. Chem. 234 (1959) 1812-1816.
2. Smith, G.K., Benkovic, P.A. and Benkovic, S.J. L(–)-10-Formyltetrahydrofolate is the cofactor for glycinamide ribonucleotide transformylase from chicken liver. Biochemistry 20 (1981) 4034-4036. [Medline UI: 82023939]
3. Warren, L. and Buchanan, J.M. Biosynthesis of the purines. XIX. 2-Amino-N-ribosylacetamide 5'-phosphate (glycinamide ribotide) transformylase. J. Biol. Chem. 229 (1957) 613-626.
Recommended name: phosphoribosylaminoimidazolecarboxamide formyltransferase
Reaction: 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
For reaction pathway click here.
Other name(s): 5-amino-4-imidazolecarboxamide ribonucleotide transformylase; AICAR transformylase; 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase; 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase; 5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase; 5-amino-4-imidazolecarboxamide ribotide transformylase; AICAR formyltransferase; aminoimidazolecarboxamide ribonucleotide transformylase
Systematic name: 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazole-carboxamide N-formyltransferase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
WIT,
CAS registry number: 9032-03-5
References:
1. Hartman, S.C. and Buchanan, J.M. Biosynthesis of the purines. XXVI. The identification of the formyl donors of the transformylation reaction. J. Biol. Chem. 234 (1959) 1812-1816.
Recommended name: glycine formimidoyltransferase
Reaction: 5-formimidoyltetrahydrofolate + glycine = tetrahydrofolate + N-formimidoylglycine
Other name(s): formiminoglycine formiminotransferase; FIG formiminotransferase; glycine formiminotransferase
Systematic name: 5-formimidoyltetrahydrofolate:glycine N-formimidoyltransferase
References:
1. Rabinowitz, J.C. and Pricer, W.E. Formiminotetrahydrofolic acid and methenyltetrahydrofolic acid as intermediates in the formation of N10-formyltetrahydrofolic acid. J. Am. Chem. Soc. 78 (1956) 5702-5704.
2. Rabinowitz, J.C. and Pricer, W.E. Formation, isolation and properties of 5-formiminotetrahydrofolic acid. Fed. Proc. 16 (1957) 236 only.
3. Sagers, R.D., Beck, J.V., Gruber, W. and Gunsalus, I.C. A tetrahydrofolic acid linked formimino transfer enzyme. J. Am. Chem. Soc. 78 (1956) 694-695.
Recommended name: glutamate formimidoyltransferase
Reaction: 5-formimidoyltetrahydrofolate + L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate
Other name(s): glutamate formyltransferase; formiminoglutamic acid transferase; formiminoglutamic formiminotransferase; glutamate formiminotransferase
Systematic name: 5-formimidoyltetrahydrofolate:L-glutamate N-formimidoyltransferase
Comments: A pyridoxal-phosphate protein. Also catalyses formyl transfer from 5-formyltetrahydrofolate to L-glutamate (a reaction formerly listed as EC 2.1.2.6). In eukaryotes, it occurs as a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) activity.
References:
1. Miller, A. and Waelsch, H. Formimino transfer from formamidinoglutaric acid to tetrahydrofolic acid. J. Biol. Chem. 228 (1957) 397-417.
2. Silverman, M., Keresztesy, J.C., Koval, G.J. and Gardiner, R.C. Citrovorium factor and the synthesis of formylglutamic acid. J. Biol. Chem. 226 (1957) 83-94.
3. Tabor, H. and Wyngarden, L. The enzymatic formation of formiminotetrahydrofolic acid, 5,10-methenyltetrahydrofolic acid, and 10-formyltetrahydrofolic acid in the metabolism of formiminoglutamic acid. J. Biol. Chem. 234 (1959) 1830-1849.
Recommended name: phloroisovalerophenone synthase
Reaction: isovaleryl-CoA + 3 malonyl-CoA = 4 CoASH + 3 CO2+ 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one
Other name(s): valerophenone synthase; 3-methyl-1-(trihydroxyphenyl)butan-1-one synthase
Systematic name: isovaleryl-CoA:malonyl-CoA acyltransferase
Comments: Closely related to EC 2.3.1.74, chalcone synthase. The product, 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one, is phloroisovalerophenone. Also acts on isobutyryl-CoA as substrate to give phlorisobutyrophenone. The products are intermediates in the biosynthesis of the bitter (α) acids in hops (Humulus lupulus).
References:
1. Fung, S.Y., Zuurbier, K.W.M., Paniego, N.B., Scheffer, J.J.C. and Verpoorte, R. Enzymes from the biosynthesis of hop α and β acids. Proc. 26th Congr. Eur. Brew. Conv. (1997) 215-221.
2. Zuurbier, K.W.M., Leser, J., Berger, T., Hofte, A.J.P., Schroder, G., Verpoorte, R. and Schroder, J. 4-Hydroxy-2-pyrone formation by chalcone and stilbene synthase with nonphysiological substrates. Phytochemistry 49 (1998) 1945-1951.
*EC 3.1.14 Exoribonucleases Producing 3'-Phosphomonoesters
*EC 3.1.16 Exonucleases Active with either Ribo- or Deoxyribonucleic Acids
and Producing 3'-Phosphomonoesters
*EC 3.1.31 Endoribonucleases Active with either Ribo-
or Deoxyribonucleic Acids and Producing 3'-Phosphomonoesters
Recommended name: formimidoylaspartate deiminase
Reaction:N-formimidoyl-L-aspartate + H2O = N-formyl-L-aspartate + NH3
Other name(s): formiminoaspartate deiminase
Systematic name:N-formimidoyl-L-aspartate iminohydrolase
References:
1. Hayaishi, O., Tabor, H. and Hayaishi, T. N-Formimino-L-aspartic acid as an intermediate in the enzymic conversion of imidazoleacetic acid to formylaspartic acid. J. Biol. Chem. 227 (1957) 161-180.
Recommended name: formimidoylglutamase
Reaction:N-formimidoyl-L-glutamate + H2O = L-glutamate + formamide
Other name(s): formiminoglutamase
Systematic name:N-formimino-L-glutamate formiminohydrolase
References:
1. Kaminskas, E., Kimhi, Y. and Magasanik, B. Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus subtilis, two enzymes of the histidine degradation pathway. J. Biol. Chem. 245 (1970) 3536-3544. [Medline UI: 71007904]
2. Lund, P. and Magasanik, B. N-Formimino-L-glutamate formiminohydrolase of Aerobacter aerogenes. J. Biol. Chem. 240 (1965) 4316-4319. [Medline UI: 66045196]
Recommended name: formimidoylglutamate deiminase
Reaction:N-formimidoyl-L-glutamate + H2O = N-formyl-L-glutamate + NH3
Other name(s): formiminoglutamate deiminase
Systematic name:N-formimidoyl-L-glutamate iminohydrolase
References:
1. Wickner, R.B. and Tabor, H. N-Formimino-L-glutamate iminohydrolase (Pseudomonas sp.). Methods Enzymol. 17B (1971) 80-84.
Recommended name: IMP cyclohydrolase
Reaction: IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
For reaction pathway click here.
Systematic name: IMP 1,2-hydrolase (decyclizing)
Links to other databases:
BRENDA,
EXPASY,
KEGG,
WIT,
CAS registry number: 9013-81-4
References:
1. Flaks, J.G., Erwin, M.J. and Buchanan, J.M. Biosynthesis of the purines. XVIII. 5-Amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase and inosinicase. J. Biol. Chem. 229 (1957) 603-612.
Recommended name: phosphoribosyl-AMP cyclohydrolase
Reaction: 1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
For reaction pathway click here.
Systematic name: 1-(5-phospho-D-ribosyl)-AMP 1,6-hydrolase
Comments: The Neurospora crassa enzyme also catalyses the reactions of EC 1.1.1.23 (histidinol dehydrogenase) and EC 3.6.1.31 (phosphoribosyl-ATP diphosphatase).
References:
1. Minson, A.C. and Creaser, E.H. Purification of a trifunctional enzyme, catalysing three steps of the histidine pathway, from Neurospora crassa. Biochem. J. 114 (1969) 49-56. [Medline UI: 69287482]
Recommended name: thiocyanate hydrolase
Reaction: thiocyanate + 2 H2O = carbonyl sulfide + NH3 + HO-
Systematic name: thiocyanate aminohydrolase
Comments: The enzyme from Thiobacillus thioparus catalyses the first step in the degradation of thiocyanate.
References:
1. Katayama, Y., Matsushita, Y., Kaneko, M., Kondo, M., Mizuno, T. and Nyunoya, H. Cloning of genes coding for the three subunits of thiocyanate hydrolase of Thiobacillus thioparus THI 115 and their evolutionary relationships to nitrile hydratase. J. Bacteriol. 180 (1998) 2583-2589. [Medline UI: 98241517]
2. Katayama, Y., Narahara, Y., Inoue, Y., Amano, F., Kanagawa, T. and Kuraishi, H. A thiocyanate hydrolase of Thiobacillus thioparus. J. Biol. Chem. 267 (1992) 9170-9175. [Medline UI: 92250515]
Recommended name: phosphoribosylaminoimidazole carboxylase
Reaction: 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2
For reaction pathway click here.
Systematic name: 1-(5-phosphoribosyl)-5-amino-4-imidazolecarboxylate carboxy-lyase
Links to other databases:
BRENDA,
EXPASY,
KEGG,
WIT,
CAS registry number: 9032-04-6
References:
1. Lukens, L.N. and Buchanan, J.M. Biosynthesis of purines. XXIV. The enzymatic synthesis of 5-amino-1-ribosyl-4-imidazolecarboxylic acid 5'-phosphate from 5-amino-1-ribosylimidazole 5'-phosphate and carbon dioxide. J. Biol. Chem. 234 (1959) 1799-1805.
Recommended name: acetylenedicarboxylate decarboxylase
Reaction: acetylenedicarboxylate + H2O = pyruvate + CO2
Systematic name: acetylenedicarboxylate carboxy-lyase
Other name(s): acetylenedicarboxylate hydratase
Comments: The mechanism appears to involve hydration of the acetylene and decarboxylation of the oxaloacetic acid formed, although free oxaloacetate is not an intermediate. It is thus analogous to EC 4.2.1.71 (acetylenecarboxylate hydratase) in its mechanism. Formerly EC 4.2.1.72
Links to other databases:
CAS registry number: 72561-10-5
References:
1. Yamada, E.W. and Jakoby, W.B. Enzymatic utilization of acetylenic compounds. I. A enzyme converting acetylenedicarboxylic acid to pyruvate. J. Biol. Chem. 233 (1958) 706-711.
[EC 4.1.99.6 Transferred entry: now EC 4.2.3.6, trichodiene synthase]
[EC 4.1.99.7 Transferred entry: now EC 4.2.3.9, aristolochene synthase]
[EC 4.1.99.8 Transferred entry: now EC 4.2.3.14, pinene synthase]
[EC 4.1.99.9 Transferred entry: now EC 4.2.3.15, myrcene synthase]
[EC 4.1.99.10 Transferred entry: now EC 4.2.3.16, trichodiene synthase]
Recommended name: benzylsuccinate synthase
Reaction: toluene + fumarate = benzylsuccinate
Systematic name: benzylsuccinate fumarate-lyase
Comments: A glycyl radical enzyme that is inhibited by benzyl alcohol, benzaldehyde, phenylhydrazine and is inactivated by oxygen.
References:
1. Beller, H.R. and Spormann, A.M. Analysis of the novel benzylsuccinate synthase reaction for anaerobic toluene activation based on structural studies of the product. J. Bacteriol. 180 (1998) 5454-5457. [Medline UI: 98440440]
2. Leuthner, B., Leutwein, C., Schultz, H., Hörth, P., Haehnel, W., Schiltz, E., Schägger, H. and Heider, J. Biochemical and genetic characterisation of benzylsuccinate synthase from Thauera aromatica: a new glycyl radical enzyme catalysing the first step in anaerobic toluene metabolism. Mol. Microbiol. 28 (1998) 615-628. [Medline UI: 98294052]
Recommended name: acetylenecarboxylate hydratase
Reaction: 3-oxopropanoate = propynoate + H2O
Other name(s): acetylenemonocarboxylate hydratase; alkynoate hydratase
Systematic name: 3-oxopropanoate hydro-lyase
Comments: The reaction is effectively irreversible, favouring oxopropanoate (malonic semialdehyde) and its tautomers. Also acts on 3-butynoate forming acetoacetate. The mechanism appears to involve hydration of the acetylene to 3-hydroxypropenoate, which will spontaneously tautomerize to 3-oxopropanoate. It is thus analogous to EC 4.1.1.78, in its mechanism.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
WIT,
CAS registry number: 72561-09-2
References:
1. Van den Tweel, W.J.J. and De Bont, J.A.M. Metabolism of 3-butyn-1-ol by Pseudomonas BB1. J. Gen. Microbiol. 131 (1985) 3155-3162.
2. Yamada, E.W. and Jakoby, W.B. Enzymatic utilization of acetylenic compounds. II. Acetylenemonocarboxylic acid hydrase. J. Biol. Chem. 234 (1959) 941-945.
[EC 4.2.1.72 Transferred entry: acetylenedicarboxylate hydratase. Now EC 4.1.1.78, acetylenedicarboxylate decarboxylase]
EC 4.2.3 Acting on phosphates
Recommended name: threonine synthase
Reaction: O-phospho-L-homoserine + H2O = L-threonine + phosphate
Systematic name: O-phospho-L-homoserine phospho-lyase (adding water)
Comments: A pyridoxal-phosphate protein.
Links to other databases:
CAS registry number: 9023-97-6
References:
1. Flavin, M. and Slaughter, C. Purification and properties of threonine synthetase of Neurospora. J. Biol. Chem. 235 (1960) 1103-1108.
Recommended name: ethanolamine-phosphate phospho-lyase
Reaction: ethanolamine phosphate + H2O = acetaldehyde + NH3 + phosphate
Systematic name: ethanolamine-phosphate phospho-lyase (deaminating)
Comments: A pyridoxal-phosphate protein. Also acts on D(or L)-1-aminopropan-2-ol O-phosphate.
Links to other databases:
CAS registry number: 37290-88-3
References:
1. Fleshood, H.L. and Pitot, H.C. The metabolism of O-phosphorylethanolamine in animal tissues. I. O-Phosphorylethanolamine phospho-lyase: partial purification and characterization. J. Biol. Chem. 245 (1970) 4414-4420. [Medline UI: 71103817]
2. Jones, A., Faulkner, A. and Turner, J.M. Microbial metabolism of amino alcohols. Metabolism of ethanolamine and 1-aminopropan-2-ol in species of Erwinia and the roles of amino alcohol kinase and amino alcohol o-phosphate phospho-lyase in aldehyde formation. Biochem. J. 134 (1973) 959-968. [Medline UI: 74053829]
Recommended name: methylglyoxal synthase
Reaction: glycerone phosphate = methylglyoxal + phosphate
Systematic name: glycerone-phosphate phospho-lyase
Comments: Does not act on D-glyceraldehyde 3-phosphate.
Links to other databases:
CAS registry number: 37279-01-9
References:
1. Cooper, R.A. and Anderson, A. The formation and catabolism of methylglyoxal during glycolysis in Escherichia coli. FEBS Lett. 11 (1970) 273-276.
2. Hopper, D.J. and Cooper, R.A. The regulation of Escherichia coli methylglyoxal synthase; a new control site in glycolysis? FEBS Lett. 13 (1971) 213-216.
3. Ray, S. and Ray, M. Isolation of methylglyoxal synthase from goat liver. J. Biol. Chem. 256 (1981) 6230-6233. [Medline UI: 81215570]
Recommended name: 3-dehydroquinate synthase
Reaction: 3-deoxy-arabino-heptulosonate 7-phosphate = 3-dehydroquinate + phosphate
Systematic name: 3-deoxy-arabino-heptulosonate-7-phosphate phosphate-lyase (cyclizing)
Comments: Requires Co2+. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product.
Links to other databases:
CAS registry number: 37211-77-1
References:
1. Rotenberg, S.L. and Sprinson, D.B. Mechanism and stereochemistry of 5-dehydroquinate synthetase. Proc. Natl. Acad. Sci. USA 67 (1970) 1669-1672. [Medline UI: 71063609]
2. Srinivasan, P.R., Rothschild, J. and Sprinson, D.B. The enzymic conversion of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate. J. Biol. Chem. 238 (1963) 3176-3182.
Recommended name: chorismate synthase
Reaction: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Systematic name: 5-O-(1-carboxyvinyl)-3-phosphoshikimate phosphate-lyase
Comments: Shikimate is numbered so that the double-bond is between C-1 and C-2, but some earlier papers numbered the ring in the reverse direction.
Links to other databases:
CAS registry number: 9077-07-0
References:
1. Gaertner, F.H. and Cole, K.W. Properties of chorismate synthase in Neurospora crassa. J. Biol. Chem. 248 (1973) 4602-4609. [Medline UI: 73218478]
2. Morell, H., Clark, M.J., Knowles, P.F. and Sprinson, D.B. The enzymic synthesis of chorismic and prephenic acids from 3-enolpyruvylshikimic acid 5-phosphate. J. Biol. Chem. 242 (1967) 82-90. [Medline UI: 67082484]
3. Welch, G.R., Cole, K.W. and Gaertner, F.H. Chorismate synthase of Neurospora crassa: a flavoprotein. Arch. Biochem. Biophys. 165 (1974) 505-518. [Medline UI: 75071773]
Recommended name: trichodiene synthase
Reaction: trans,trans-farnesyl diphosphate = trichodiene + diphosphate
For reaction pathway click here.
Other name(s): sesquiterpene cyclase
Systematic name: trans,trans-farnesyl-diphosphate sesquiterpenoid-lyase
References:
1. Hohn, T.M. and Vanmiddlesworth, F. Purification and characterization of the sesquiterpene cyclase trichodiene synthetase from Fusarium sporotrichioides. Arch. Biochem. Biophys. 251 (1986) 756-761. [Medline UI: 87098811]
Recommended name: pentalenene synthase
Reaction: 2-trans,6-trans-farnesyl diphosphate = pentalenene + diphosphate
For reaction pathway click here.
Systematic name: 2-trans,6-trans-farnesyldiphosphate diphosphate-lyase (cyclizing, pentalenene-forming)
Comments: The initial step in the reaction is probably a cyclization of farnesyl diphosphate to form humulene. The enzyme is involved in the biosynthesis of pentalenolactone and related antibiotics.
References:
1. Cane, D.E. Cell-free studies of monoterpene and sesquiterpene biosynthesis. Biochem. Soc. Trans. 11 (1983) 510-515. [Medline UI: 84058684]
Recommended name: casbene synthase
Reaction: geranylgeranyl diphosphate = casbene + diphosphate
For reaction pathway click here.
Systematic name: geranylgeranyl-diphosphate diphosphate-lyase (cyclizing)
Comments: The enzyme from castor bean (Ricinus communis) produces the antifungal diterpene casbene.
References:
1. Moesta, P. and West, C.A. Casbene synthetase: regulation of phytoalexin biosynthesis in Ricinus communis L. seedlings. Purification of casbene synthetase and regulation of its biosynthesis during elicitation. Arch. Biochem. Biophys. 238 (1985) 325-333. [Medline UI: 85173341]
Recommended name: aristolochene synthase
Reaction: trans,trans-farnesyl diphosphate = aristolochene + diphosphate
For reaction pathway click here.
Other name(s): sesquiterpene cyclase
Systematic name: trans,trans-farnesyl diphosphate aristolochene-lyase
Comments: The initial internal cyclization produces the monocyclic intermediate germacrene A; further cyclization and methyl transfer converts the intermediate into aristolochene. The enzyme from Penicillium roqueforti requires magnesium and manganese ions. Aristolochene is the likely parent compound for a number of sesquiterpenes produced by filamentous fungi.
References:
1. Cane, D.E., Prabhakaran, P.C., Oliver, J.S., McIlwaine, D.B. Aristolochene biosynthesis. Stereochemistry of the deprotonation steps in the enzymatic cyclization of farnesyl pyrophosphate. J. Am. Chem. Soc. 112 (1990) 3209-3210.
2. Cane, D.E., Prabhakaran, P.C., Salaski, E.J., Harrison, P.M.H., Noguchi, H., Rawlings, B.J. Aristolochene biosynthesis and enzymatic cyclization of farnesyl pyrophosphate. J. Am. Chem. Soc. 111 (1989) 8914-8916.
3. Hohn, T.M., Plattner, R.D. Purification and characterization of the sesquiterpene cyclase aristolochene synthase from Penicillium roqueforti. Arch. Biochem. Biophys. 272 (1989) 137-143. [Medline UI: 89286114]
4. Proctor, R.H., Hohn, T.M. Aristolochene synthase. Isolation, characterization, and bacterial expression of a sesquiterpenoid biosynthetic gene (Ari1) from Penicillium roqueforti. J. Biol. Chem. 268 (1993) 4543-4548. [Medline UI: 93179472]
Recommended name: (–)-endo-fenchol synthase
Reaction: geranyl diphosphate = (–)-endo-fenchol + diphosphate
For reaction pathway click here.
Systematic name: geranyl-diphosphate diphosphate-lyase [cyclizing, (–)-endo-fenchol-forming]
Comments: (3R)-linalyl diphosphate is an intermediate in the reaction
References:
1. Croteau, R., Miyazaki, J.H. and Wheeler, C.J. Monoterpene biosynthesis: mechanistic evaluation of the geranyl pyrophosphate:(–)-endo-fenchol cyclase from fennel (Foeniculum vulgare). Arch. Biochem. Biophys. 269 (1989) 507-516. [Medline UI: 89149097]
2. Croteau, R., Satterwhite, D.M., Wheeler, C.J. and Felton, N.M. Biosynthesis of monoterpenes. Stereochemistry of the enzymatic cyclization of geranyl pyrophosphate to (–)-endo-fenchol. J. Biol. Chem. 263 (1988) 15449-15453. [Medline UI: 89008446]
Recommended name: sabinene-hydrate synthase
Reaction: geranyl diphosphate = sabinene hydrate + diphosphate
For reaction pathway click here.
Systematic name: geranyl-diphosphate diphosphate-lyase (cyclizing, sabinene-hydrate-forming)
Comments: Both cis- and trans- isomers of sabinene hydrate are formed. (3R)-Linalyl diphosphate is an intermediate in the reaction
References:
1. Hallahan, T.W. and Croteau, R. Monoterpene biosynthesis: demonstration of a geranyl pyrophosphate:sabinene hydrate cyclase in soluble enzyme preparations from sweet marjoram (Majorana hortensis). Arch. Biochem. Biophys. 264 (1988) 618-631. [Medline UI: 88292975]
2. Hallahan, T.W. and Croteau, R. Monoterpene biosynthesis: mechanism and stereochemistry of the enzymatic cyclization of geranyl pyrophosphate to (+)-cis- and (+)-trans-sabinene hydrate. Arch. Biochem. Biophys. 269 (1989) 313-326. [Medline UI: 89133548]
Recommended name: 6-pyruvoyltetrahydropterin synthase
Reaction: 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropteridin = 6-(1,2-dioxopropyl)-5,6,7,8-tetrahydropterin + triphosphate
Systematic name: 2-amino-4-oxo-6-(erythro-1',2',3'-trihydroxypropyl)-7,8-dihydroxypterdine triphosphate lyase
Comments: catalyses triphosphate elimination and an intramolecular redox reaction in the presence of Mg2+. It has been identified in human liver. The product is 6-pyruvoyltetrahydrobiopterin.
References:
1. Milstien, S., Kaufman, S. The biosynthesis of tetrahydrobiopterin in rat brain. Purification and characterization of 6-pyruvoyl-tetrahydrobiopterin(2'-oxo) reductase. J. Biol. Chem. 264 (1989) 8066-8073. [Medline UI: 89255238]
2. Thöny, B., Leimbacher, W., Bürgisser, D., Heinzmann, C.W. Human 6-pyruvoyl-tetrahydrobiopterin synthase: cDNA cloning and heterologous expression of the recombinant enzyme. Biochem. Biophys. Res. Commun. 189 (1992) 1437-1443. [Medline UI: 93129208]
Recommended name: (+)-δ-cadinene synthase
Reaction: 2-trans,6-trans-farnesyl diphosphate = (+)-δ-cadinene + diphosphate
For reaction pathway click here.
Systematic name: 2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, (+)-δ-cadinene-forming)
Comments: the sesquiterpenoid (+)-δ-cadinene is an intermediate in phytoalexin biosynthesis. Mg2+ is required for activity.
References:
1. Chen, X.-Y., Chen, Y., Heinstein, P., Davisson, V.J. Cloning, expression and characterization of (+)-δ-cadinene synthase: a catalyst for cotton phytoalexin biosynthesis. Arch. Biochem. Biophys. 324 (1995) 255-266. [Medline UI: 96132653]
2. Davis, E.M., Tsuji, J., Davis, G.D., Pierce, M.L., Essenberg, M. Purification of (+)-δ-cadinene synthase, a sesquiterpene cyclase from bacteria-inoculated cotton foliar tissue. Phytochemistry 41 (1996) 1047-1055.
3. Davis, G.D., Essenberg, M. (+)-δ-Cadinene is a product of sesquiterpene cyclase activity in cotton. Phytochemistry 39 (1995) 553-567.
Recommended name: pinene synthase
Reaction: geranyl diphosphate = pinene + diphosphate
For reaction pathway click here.
Glossary entries:
Other name(s): β-geraniolene synthase; (–)-(1S,5S)-pinene synthase
Systematic name: geranyldiphosphate diphosphate lyase (pinene forming)
Comments: A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) require Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor. A mixture of α and β-pinene is produced.
References:
1. Bohlmann, J., Steele, C.L. and Croteau, R. Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (–)-(4S)-limonene synthase, and (–)-(1S,5S)-pinene synthase. J. Biol. Chem. 272 (1997) 21784-21792. [Medline UI: 97413772]
2. Gijzen, M., Lewinsohn, E. and Croteau, R. Characterization of the constitutive and wound-inducible monoterpene cyclases of grand fir (Abies grandis). Arch. Biochem. Biophys. 289 (1991) 267-273. [Medline UI: 91378555]
3. Wagschal, K.C., Pyun, H.J., Coates, R.M. and Croteau, R. Monoterpene biosynthesis: isotope effects associated with bicyclic olefin formation catalyzed by pinene synthases from sage (Salvia officinalis). Arch. Biochem. Biophys. 308 (1994) 477-487. [Medline UI: 94153096]
Recommended name: myrcene synthase
Reaction: geranyl diphosphate = myrcene + diphosphate
For reaction pathway click here.
Glossary entries:
Systematic name: geranyldiphosphate diphosphate lyase (myrcene forming)
Comments: A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) require Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor.
References:
1. Bohlmann, J., Steele, C.L. and Croteau, R. Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (–)-(4S)-limonene synthase, and (–)-(1S,5S)-pinene synthase. J. Biol. Chem. 272 (1997) 21784-21792. [Medline UI: 97413772]
Recommended name: (–)-(4S)-limonene synthase
Reaction: geranyl diphosphate = limonene + diphosphate
For reaction pathway click here.
Glossary entries:
Systematic name: geranyldiphosphate diphosphate lyase (limonene forming)
Comments: A recombinant enzyme (also known as a monoterpene synthase or cyclase) from the grand fir (Abies grandis) require Mn2+ and K+ for activity. Mg2+ is essentially ineffective as the divalent metal ion cofactor.
b>References:
1. Bohlmann, J., Steele, C.L. and Croteau, R. Monoterpene synthases from grand fir (Abies grandis). cDNA isolation, characterization, and functional expression of myrcene synthase, (–)-(4S)-limonene synthase, and (–)-(1S,5S)-pinene synthase. J. Biol. Chem. 272 (1997) 21784-21792. [Medline UI: 97413772]
2. Collby, S.M., Alonso, W.R., Katahira, E.J., McGarvey, D.J. and Croteau, R. 4S-Limonene synthase from the oil glands of spearmint (Mentha spicata). cDNA isolation, characterization, and bacterial expression of the catalytically active monoterpene cyclase. J. Biol. Chem. 268(1993) 23016-23024. [Medline UI: 94043077]
3. Yuba, A., Yazaki, K., Tabata, M., Honda, G. and Croteau, R. cDNA cloning, characterization, and functional expression of 4S-(–)-limonene synthase from Perilla frutescens. Arch. Biochem. Biophys. 332 (1996) 280-287. [Medline UI: 96400360]
[EC 4.2.99.2 Transferred entry: now EC 4.2.3.1, threonine synthase]
[EC 4.2.99.7 Transferred entry: now EC 4.2.3.2, ethanolamine-phosphate phospho-lyase]
[EC 4.2.99.11 Transferred entry: now EC 4.2.3.3, methylglyoxal synthase]
Recommended name: formimidoyltetrahydrofolate cyclodeaminase
Reaction: 5-formimidoyltetrahydrofolate = 5,10-methenyltetrahydrofolate + NH3
Other name(s): formiminotetrahydrofolate cyclodeaminase
Systematic name: 5-formimidoyltetrahydrofolate ammonia-lyase (cyclizing)
Comments: In eukaroytes, occurs as a bifunctional enzyme that also has glutamate formimidoyltransferase (EC 2.1.2.5) activity.
References:
1. Rabinowitz, J.C. and Pricer, W.E. Formimino-tetrahydrofolic acid and methenyltetrahydrofolic acid as intermediates in the formation of N10-formyltetrahydrofolic acid. J. Am. Chem. Soc. 78 (1956) 5702-5704.
Recommended name: adenylosuccinate lyase
Reaction:
(1) N6-(1,2-dicarboxyethyl)AMP = fumarate + AMP
(2) (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
For reaction pathway click here.
Systematic name: N6-(1,2-dicarboxyethyl)AMP AMP-lyase
Comments: Also acts on 1-(5-phosphoribosyl)-4-(N-succinocarboxamide)-5-aminoimidazole.
Links to other databases:
BRENDA,
EXPASY,
GTD,
KEGG,
WIT,
CAS registry number: 9027-81-0
References:
1. Carter, C.E. and Cohen, L.H. The preparation and properties of adenylosuccinase and adenylosuccinic acid. J. Biol. Chem. 222 (1956) 17-30.
[EC 4.6.1.3 Transferred entry: now EC 4.2.3.4, 3-dehydroquinate synthase]
[EC 4.6.1.4 Transferred entry: now EC 4.2.3.5, chorismate synthase]
[EC 4.6.1.5 Transferred entry: now EC 4.2.3.7, pentalenene synthase]
[EC 4.6.1.7 Transferred entry: now EC 4.2.3.8, casbene synthase]
[EC 4.6.1.8 Transferred entry: now EC 4.2.3.10, (–)-endo-fenchol synthase]
[EC 4.6.1.9 Transferred entry: now EC 4.2.3.11, sabinene-hydrate synthase]
[EC 4.6.1.10 Transferred entry: now EC 4.2.3.12, 6-pyruvoyltetrahydropterin synthase]
[EC 4.6.1.11 Transferred entry: now EC 4.2.3.13, trichodiene synthase]
Recommended name: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase
Reaction: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide = 5-[(5-phospho-1-deoxyribulos-1-ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4-carboxamide
For reaction pathway click here.
Other name(s): N-(5'-phospho-D-ribosylformimino)-5-amino-1-(5"-phosphoribosyl)-4-imidazolecarboxamide isomerase
Systematic name: 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide ketol-isomerase
References:
1. Margolies, M.N. and Goldberger, R.F. Isolation of the fourth (isomerase) of histidine biosynthesis from Salmonella typhimurium. J. Biol. Chem. 241 (1966) 3262-3269. [Medline UI: 67004792]
Recommended name: phosphoribosylaminoimidazolesuccinocarboxamide synthase
Reaction: ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
For reaction pathway click here.
Systematic name: 1-(5-phosphoribosyl)-5-amino-4-carboxyimidazole:L-aspartate ligase (ADP-forming)
Links to other databases:
BRENDA,
EXPASY,
KEGG,
WIT,
CAS registry number: 9023-67-0
References:
1. Lukens, L.N. and Buchanan, J.M. Biosynthesis of purines. XXIV. The enzymatic synthesis of 5-amino-1-ribosyl-4-imidazolecarboxylic acid 5'-phosphate from 5-amino-1-ribosylimidazole 5'-phosphate and carbon dioxide. J. Biol. Chem. 234 (1959) 1799-1805.
Recommended name: phosphoribosylformylglycinamidine cyclo-ligase
Reaction: ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
For reaction pathway click here.
Other name(s): phosphoribosylaminoimidazole synthetase
Systematic name: 2-(formamido)-N1-(5-phosphoribosyl)acetamidine cyclo-ligase (ADP-forming)
Links to other databases:
BRENDA,
EXPASY,
KEGG,
WIT,
CAS registry number: 9023-53-4
References:
1. Levenberg, B. and Buchanan, J.M. Properties of the purines. XII. Structure, enzymatic synthesis, and metabolism of 5-aminoimidazole ribotide. J. Biol. Chem. 224 (1957) 1005-1018.
2. Levenberg, B. and Buchanan, J.M. Properties of the purines. XIII. Structure, enzymatic synthesis, and metabolism of (α-N-formyl)-glycinamidine ribotide. J. Biol. Chem. 224 (1957) 1018-1027.
Recommended name: phosphoribosylamine-glycine ligase
Reaction: ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide
For reaction pathway click here.
Other name(s): phosphoribosylglycinamide synthetase; glycinamide ribonucleotide synthetase
Systematic name: 5-phospho-D-ribosylamine:glycine ligase (ADP-forming)
Comments: Formerly EC 6.3.1.3.
Links to other databases:
BRENDA,
EXPASY,
KEGG,
WIT,
CAS registry number: 9032-01-3
References:
1. Goldthwait, D.A., Peabody, R.A. and Greenberg, G.R. On the mechanism of synthesis of glycinamide ribotide and its formyl derivative. J. Biol. Chem. 221 (1956) 569-577.
2. Hartman, S.C. and Buchanan, J.M. Biosynthesis of the purines. XXII. 2-Amino-N-ribosylacetamide-5'-phosphate kinosynthase. J. Biol. Chem. 233 (1958) 456-461.
Recommended name: phosphoribosylformylglycinamidine synthase
Reaction: ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate
For reaction pathway click here.
Other name(s): phosphoribosylformylglycinamidine synthetase
Systematic name: 5'-phosphoribosylformylglycinamide:L-glutamine amido-ligase (ADP-forming)
Links to other databases:
BRENDA,
EXPASY,
KEGG,
WIT,
CAS registry number: 9032-84-2
References:
1. Melnick, I. and Buchanan, J.M. Biosynthesis of the purines. I. Conversion of (α-N-formyl)glycinamide ribotide to (α-N-formyl)glycinamidine ribotide; purification and requirements of the enzyme system. J. Biol. Chem. 225 (1957) 157-162.
arachidonate: (all-Z)-icosa-5,8,11,14-tetraenoate
linoleate: (9Z,12Z)-octadeca-9,12-dienoate
α-linolenate: (9Z,12Z,15Z)-octadeca-9,12,15-trienoate
γ-linolenate: (6Z,9Z,12Z)-octadeca-6,9,12-trienoate
oleate: (Z)-octadec-9-enoate
phytanate: 3,7,11,15-tetramethylhexadecanoate
Quinine: a quinoline alkaloid
α-pinene: a monoterpenoid
β-pinene: a monoterpenoid
myrcene: a monoterpenoid
limonene: a monoterpenoid
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