Recommended name: sulcatone reductase
Reaction: sulcatone + NADH2 = sulcatol + NAD
Glossary entries:
sulcatone: 6-methylhept-5-en-2-one
sulcatol: 6-methylhept-5-en-2-ol
Systematic name: sulcatol:NAD oxidoreductase
Comments: Studies on the effects of growth-stage and nutrient supply on the stereochemistry of sulcatone reduction in Clostridia pasteurianum, C. tyrobutyricum and Lactobacillus brevis suggest that there may be at least two sulcatone reductases with different stereospecificities.
References:
1. Belan, A., Botle, J., Fauve, A., Gourcy, J.G. and Veschambre, H. Use of biological systems for the preparation of chiral molecules. 3. An application in pheromone synthesis: Preparation of sulcatol enantiomers. J. Org. Chem. 52 (1987) 256-260.
2. Tidswell, E.C., Salter, G.J., Kell, D.B. and Morris, J.G. Enantioselectivity of sulcatone reduction by some anaerobic bacteria. Enzyme Microb. Technol. 21 (1997) 143-147.
3.Tidswell, E.C., Thompson, A.N. and Morris, J.G. Selection in chemostat culture of a mutant strain of Clostridium tryobutyricum improved in its reduction of ketones. J. Appl. Microbiol. Biotechnol. 35 (1991) 317-322.
Recommended name: vanillin dehydrogenase
Reaction: vanillin + NAD + H2O = vanillate + NADH2
Glossary entries:
Vanillate: 4-hydroxy-3-methoxybenzoate
Vanillin: 4-hydroxy-3-methoxybenzaldehyde
Systematic name: vanillin:NAD oxidoreductase
References:
1. Pometto, A.L. and Crawford, D.L. Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus. Appl. Environ. Microbiol. 45 (1983) 1582-1585. [Medline UI: 83254833]
Recommended name: δ12-fatty acid dehydrogenase
Reaction: linoleate + AH2 + O2 = crepenynate + A + H2O
Glossary entries:
crepenynate: (9Z)-octadec-9-en-12-ynoate
linoleate: (9Z,12Z)-octadeca-9,12-dienoate
Other name(s): crepenynate synthase; linoleate δ12-fatty acid acetylenase (desaturase)
Systematic name: linoleate, hydrogen-donor:oxygen oxidoreductase (δ12-unsaturating)
Comments: Contains non-heme iron.
References:
1. Banas, A., Bafor, M., Wiberg, E., Lenman, M., Staahl, U. and Stymne, S. Biosynthesis of an acetylenic fatty acid in microsomal preparations from developing seeds Crepis alpina. Physiol. Biochem. Mol. Biol. Plant Lipids [Proc. Int. Symp. Plant Lipids] 12th (1997) 57-59.
2. Lee, M., Lenman, M., Banas, A., Bafor, M., Singh, S., Schweizer, M., Nilsson, R., Liljenberg, C., Dahlqvist, A., Gummeson, P.O., Sjodahl, S., Green, A. and Stymne, S. Identification of non-heme di-iron proteins that catalyze triple bond and epoxy group formation. Science 280 (1998) 915-918. [Medline UI: 98239771]
Recommended name: monoprenyl isoflavone epoxidase
Reaction: 7-O -methylluteone + NADPH2 + O2 = dihydrofurano derivatives + NADP + H2O
Glossary entries:
luteone: 3-(2,4-dihydroxyphenyl)-5,7-dihydroxy-6-(3-methyl-2-butenyl)-4H-1-benzopyran-4-one
naringenin: (S)-2,3-dihydo-5,7-dihydroxy-2-(4-hydroxyphenyl)-4H-1-benzopyran-4-one
Other name(s): monoprenyl isoflavone monooxygenase
Systematic name: 7-O -methylluteone:O2 oxidoreductase
Comments: A flavoprotein (FAD) with high specificity for monoprenyl isoflavone. The product of the prenyl epoxidation reaction contains an oxygen atom derived from O2, but not from H2O. It is slowly and nonenzymically converted into the corresponding dihydrofurano derivative. The enzyme in the fungus Botrytis cinerea is induced by the substrate analogue, 6-prenylnaringenin.
References:
1. Tanaka, M. and Tahara, S. FAD-dependent epoxidase as a key enzyme in fungal metabolism of prenylated flavonoids. Phytochemistry 46 (1997) 433-439.
Recommended name: arsenate reductase (glutaredoxin)
Reaction: arsenate + reduced glutaredoxin = arsenite + oxidized glutaredoxin
Systematic name: gluthathione:arsenate oxidoreductase
Comments: A molybdoenzyme. The glutaredoxins catalyse glutathione-disulfide oxidoreductions and have a redox-active disulfide/dithiol in the active site (-Cys-Pro-Tyr-Cys-) that forms a disulfide bond in the oxidized form [2, 10]. Glutaredoxins have a binding site for glutathione, which is required to reduce them to the dithiol form [3, 6]. Thioredoxins reduced by NADPH2 and thioredoxin reductase can act as alternative substrates. The enzyme [1, 4, 7, 9] is a part of a system for detoxifying arsenate. Although the arsenite formed is more toxic than arsenate, it can be extruded from some bacteria by EC 3.6.3.16, arsenite-transporting ATPase; in other organisms, arsenite can be methylated by EC 2.1.1.137, arsenite methyltransferase, in a pathway to non-toxic organoarsenical compounds.
References:
1. Gladysheva, T., Liu, J.Y. and Rosen, B.P. His-8 lowers the pKa of the essential Cys-12 residue of the ArsC arsenate reductase of plasmid R773. J. Biol. Chem. 271 (1996) 33256-33260. [Medline UI: 97125961]
2. Gladysheva, T.B., Oden, K.L. and Rosen, B.P. Properties of the arsenate reductase of plasmid R773. Biochemistry 33 (1994) 7288-7293.
3. Holmgren, A. and Aslund, F. Glutaredoxins. Methods Enzymol. 252 (1995) 283-292.
4. Ji, G.Y., Garber, E.A.E., Armes, L.G., Chen, C.M., Fuchs, J.A. and Silver, S. Arsenate reductase of Staphylococcus aureus plasmid PI258. Biochemistry 33 (1994) 7294-7299. [Medline UI: 94271784]
5. Krafft, T. and Macy, J.M. Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis. Eur. J. Biochem. 255 (1998) 647-653. [Medline UI: 98409284]
6. Martin, J.L. Thioredoxin - a fold for all reasons. Structure 3 (1995) 245-250.
7. Messens, J., Hayburn, G., Desmyter, A., Laus, G. and Wyns, L. The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus. Biochemistry 38 (1999) 16857-16865. [Medline UI: 20074536]
8. Radabaugh, T.R. and Aposhian, H.V. Enzymatic reduction of arsenic compounds in mammalian systems: reduction of arsenate to arsenite by human liver arsenate reductase. Chem. Res. Toxicol. 13 (2000) 26-30. [Medline UI: 20115133]
9. Sato, T. and Kobayashi, Y. The ars operon in the skin element of Bacillus subtilis confers resistance to arsenate and arsenite. J. Bacteriol. 180 (1998) 1655-1661. [Medline UI: 98196706]
10. Shi, J., Vlamis-Gardikas, V., Aslund, F., Holmgren, A. and Rosen, B.P. Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction. J. Biol. Chem. 274 (1999) 36039-36042. [Medline UI: 20062807]
Recommended name: arsenate reductase (donor)
Reaction: arsenate + donor = arsenite + oxidized donor
Systematic name: arsenate:(acceptor) oxidoreductase
Comments: Benzyl viologen can act as an acceptor. Unlike EC 1.97.1.5, arsenate reductase (glutaredoxin), reduced glutaredoxin cannot serve as a reductant.
References:
1. Krafft, T. and Macy, J.M. Purification and characterization of the respiratory arsenate reductase of Chrysiogenes arsenatis. Eur. J. Biochem. 255 (1998) 647-653. [Medline UI: 98409284]
2. Radabaugh, T.R. and Aposhian, H.V. Enzymatic reduction of arsenic compounds in mammalian systems: reduction of arsenate to arsenite by human liver arsenate reductase. Chem. Res. Toxicol. 13 (2000) 26-30. [Medline UI: 20115133]
Recommended name: methylarsonate reductase
Reaction: methylarsonate + 2 glutathione = methylarsonite + oxidized glutathione
Systematic name: gluthathione:methylarsonate oxidoreductase
Comments: The product, Me-As(OH)2 (methylarsonous acid), is biologically methylated by EC 2.1.1.138, methylarsonite methyltransferase, to form cacodylic acid (dimethylarsinic acid).
References:
1. Zakharyan, R.A. and Aposhian, H.V. Enzymatic reduction of arsenic compounds in mammalian systems: the rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase. Chem. Res. Toxicol. 12 (1999) 1278-1283. [Medline UI: 20072591]
Recommended name: chlorophenol O-methyltransferase
Other name(s): halogenated phenol O-methyltransferase, trichlorophenol O-methyltransferase
Reaction: S-adenosyl-L-methionine + trichlorophenol = S-adenosyl-L-homocysteine + trichloroanisole
Systematic name: S-adenosyl-L-methionine:trichlorophenol O-methyltransferase
Comments: The enzyme from Trichoderma virgatum, when cultured in the presence of halogenated phenol, also acts on a range of mono-, di- and trichlorophenols.
References:
1. Kikuchi, T. and Oe, T. Halogenated phenol O-methyltransferase, its preparation from Trichoderma, and methods for wood products deodorization. Patent document (Rengo Co., Ltd., Japan), Jpn. Kokai Tokyo Koho, 8 pp. JP 09234062 A2 970909 Heisei, JP 96-44897 960301, 1996.
Recommended name: arsenite methyltransferase
Reaction: S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + methylarsonate
Systematic name: S-adenosyl-L-methionine:arsenite As-methyltransferase
Comments: An enzyme of the biotransformation pathway that forms methylarsonate from inorganic arsenite. The enzyme has been purified from rabbit liver.
References:
1. Zakharyan, R.A. and Aposhian, H.V. Enzymatic reduction of arsenic compounds in mammalian systems: The rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase. Chem. Res. Toxicol. 121 (1999) 1278-1283. [Medline UI: 20072591]
2. Zakharyan, R.A., Ayala-Fierro, F., Cullen, W.R., Carter, D.M. and Aposhian, H.V. Enzymatic methylation of arsenic compounds. VII. Monomethylarsonous acid (MMAIII) is the substrate for MMA methyltransferase of rabbit liver and human hepatocytes. Toxicol. Appl. Pharmacol. 158 (1999) 9-15. [Medline UI: 99317121]
3. Zakharyan, R.A., Wildfang, E. and Aposhian, H.V. Enzymatic methylation of arsenic compounds. III. The marmoset and tamarin, but not the rhesus, monkeys are deficient in methyltransferases that methylate inorganic arsenic. Toxicol. Appl. Pharmacol. 140 (1996) 77-84. [Medline UI: 96400496]
4. Zakharyan, R.A., Wu, Y., Bogdan, G.M. and Aposhian, H.V. Enzymatic methylation of arsenic compounds: assay, partial purification, and properties of arsenite methyltransferase and monomethylarsonic acid methyltransferase of rabbit liver. Chem.Res. Toxicol. 8 (1995) 1029-1038. [Medline UI: 96189424]
Recommended name: methylarsonite methyltransferase
Reaction: S-adenosyl-L-methionine + methylarsonite = S-adenosyl-L-homocysteine + dimethylarsinate
Systematic name: S-adenosyl-L-methionine:methylarsonite As-methyltransferase
Comments: The dimethylarsinic acid formed is a less toxic product in the pathway that starts with and biotransforms toxic arsenate. The enzyme has been partially purified from rabbit liver and Chang human hepatocytes.
References:
1. Zakharyan, R.A. and Aposhian, H.V. Enzymatic reduction of arsenic compounds in mammalian systems: The rate-limiting enzyme of rabbit liver arsenic biotransformation is MMA(V) reductase. Chem. Res. Toxicol. 121 (1999) 1278-1283. [Medline UI: 20072591]
2. Zakharyan, R.A., Ayala-Fierro, F., Cullen, W.R., Carter, D.M. and Aposhian, H.V. Enzymatic methylation of arsenic compounds. VII. Monomethylarsonous acid (MMAIII) is the substrate for MMA methyltransferase of rabbit liver and human hepatocytes. Toxicol. Appl. Pharmacol. 158 (1999) 9-15. [Medline UI: 99317121]
Recommended name: propionyl-CoA C2-trimethyltridecanoyltransferase
Reaction: 4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = 3-oxopristanoyl-CoA + CoA
For reaction pathway click here.
Other name(s): 3-oxopristanoyl-CoA hydrolase; 3-oxopristanoyl-CoA thiolase; peroxisome sterol carrier protein thiolase; sterol carrier protein; oxopristanoyl-CoA thiolase; peroxisomal 3-oxoacyl coenzyme A thiolase; SCPx
Systematic name: 4,8,12-trimethyltridecanoyl-CoA:propanoyl-CoA C2-4,8,12-trimethyltridecanoyltransferase
Comments: The peroxisomal protein sterol carrier protein X (SCPx) combines this thiolase activity with its carrier function, and is involved in branched chain fatty acid β-oxidation in peroxisomes. It also acts on 3-oxopalmitoyl-CoA as a substrate but differs from EC 2.3.1.16 (acetyl-CoA C-acyltransferase), which has little activity towards the 3-oxoacyl-CoA esters of 2-methyl-branched chain fatty acids such as 3-oxopristanoyl-CoA.
References:
1. Seedorf, U., Brysch, P., Engel, T., Schrage, K. and Assmann, G. Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity. J. Biol. Chem. 269 (1994) 21277-21283. [Medline UI: 94342300]
2. Wanders, R.J.A., Denis, S., Wouters, F., Wirtz, K.W.A. and Seedorf, U. Sterol carrier protein X (SCPx) is a peroxisomal branched-chain β-ketothiolase specifically reacting with 3-oxo-pristanoyl-CoA: a new, unique role for SCPx in branched-chain fatty acid metabolism in peroxisomes. Biochem. Biophys. Res. Commun. 236 (1997) 565-569. [Medline UI: 97396135]
Recommended name: acetyl-CoA C-myristoyltransferase
Reaction: myristoyl-CoA + acetyl-CoA = 3-oxopalmitoyl-CoA + CoA
Other name: 3-oxopalmitoyl-CoA hydrolase; 3-oxopalmitoyl-CoA-CoA acetyltransferase
Systematic name: myristoyl-CoA:acetylCoA C-myristoyltransferase
Comments: A peroxisomal enzyme involved in branched chain fatty acid β-oxidation in peroxisomes. It differs from EC 2.3.1.154 (propionyl-CoA C2-trimethyldecanoyltransferase) in not being active towards 3-oxopristanoyl-CoA.
References:
1. Miyazawa, S., Furuta, S., Osumi, T., Hashimoto, T. and Ui, N. Properties of peroxisomal 3-ketoacyl-coA thiolase from rat liver. J Biochem (Tokyo) 90 (1981) 511-519. [Medline UI: 82052935]
Recommended name: cutinase
Reaction: cutin + H2O = cutin monomers
Systematic name: cutin hydrolase
Comments: Cutin, a polymeric structural component of plant cuticles, is an hydroxy fatty acid polymer, usually C16 or C18 and that contains one to three hydroxyl groups. The enzyme from several fungal sources also hydrolyses the p-nitrophenyl esters of hexadecanoic acid. It is however inactive towards several esters that are substrates for non-specific esterases.
References:
1. Garcia-Lepe, R., Nuero, O.M., Reyes, F. and Santamaria, F. Lipases in autolysed cultures of filamentous fungi. Lett. Appl. Microbiol. 25 (1997) 127-130. [Medline UI: 97426685]
2. Purdy, R.E. and Kolattukudy, P.E. Hydrolysis of plant cuticle by plant pathogens. Purification, amino acid composition, and molecular weight of two isoenzymes of cutinase and a nonspecific esterase from Fusarium solani f. pisi. Biochemistry 14 (1975) 2824-2831. [Medline UI: 76000309]
3. Purdy, R.E. and Kolattukudy, P.E. Hydrolysis of plant cuticle by plant pathogens. Properties of cutinase I, cutinase II, and a nonspecific esterase isolated from Fusarium solani pisi. Biochemistry 14 (1975) 2832-2840. [Medline UI: 76000310]
Recommended name: mandelamide amidase
Reaction: (R)-mandelamide + H2O = (R)-mandelate + NH3
Other name(s): Pseudomonas mandelamide hydrolase
Systematic name: mandelamide hydrolase
References:
1. Yamamoto, K., Oishi, K., Fujimatsu, I. and Komatsu, K. Production of R-(–)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750. Appl. Environ. Microbiol. 57 (1991) 3028-3032. [Medline UI: 92082254]
Recommended name: vanillin synthase
Reaction: 3-hydroxy-3-(3-hydroxy-4-methoxyphenyl)propionyl-CoA = vanillin + acetyl-CoA
Glossary entries:
Vanillin: 4-hydroxy-3-methoxybenzaldehyde
Systematic name: 3-hydroxy-3-(3-hydroxy-4-methoxyphenyl)propionyl-CoA:vanillin lyase (acetyl-CoA-forming)
Comments: Involved, together with EC 4.2.1.101, trans-feruloyl-CoA hydratase, in the production of vanillin from trans-ferulic acid. Vanillin is converted to vanillate by EC 1.2.1.67, vanillin dehydrogenase.
References:
1. Narbad, A. and Gasson, M.J. Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens. Microbiology 144 (1998) 1397-1405. [Medline UI: 98274748]
2. Pometto, A.L. and Crawford, D.L.Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus. Appl. Environ. Microbiol. 45 (1983) 1582-1585. [Medline UI: 83254833]
Recommended name: pinene synthase
Reaction: geranyl diphosphate = pinene + diphosphate
For reaction pathway click here.
Glossary entries:
α-pinene: a monoterpenoid
β-pinene: a monoterpenoid
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. 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]
3. 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]
Recommended name: myrcene synthase
Reaction: geranyl diphosphate = myrcene + diphosphate
For reaction pathway click here.
Glossary entries:
myrcene: a monoterpenoid
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:
limonene: a monoterpenoid
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.
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]
Recommended name: trans-feruloyl-CoA hydratase
Reaction: trans-feruloyl-CoA + H2O = 4-hydroxy-3-methoxyphenyl-β-hydroxypropionyl-CoA
Systematic name: trans-feruloyl-CoA hydro-lyase
References:
1. Narbad, A. and Gasson, M.J. Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens. Microbiology 144 (1998) 1397-1405. [Medline UI: 98274748]
2. Pometto, A.L. and Crawford, D.L. Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus. Appl. Environ. Microbiol. 45 (1983) 1582-1585. [Medline UI: 83254833]
Recommended name: deacetylisoipecoside synthase
Reaction: dopamine + secologanin = deacetylisoipecoside + H2O
Systematic name: deacetylisoipecoside dopamine-lyase
Comments: The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 4.3.3.4, deacetylipecoside synthase. The product is rapidly converted to demethylisoalangiside.
References:
1. DeEknamkul, W., Ounaroon, A., Tanahashi, T., Kutchan, T. and Zenk, M.H. Enzymatic condensation of dopamine and secologanin by cell-free extracts of Alangium lamarckii. Phytochemistry 45 (1997) 477-484.
Recommended name: deacetylipecoside synthase
Reaction: dopamine + secologanin = deacetylipecoside + H2O
Systematic name: deacetylipecoside dopamine-lyase
Comments: The enzyme from the leaves of Alangium lamarckii differs in enantiomeric specificity from EC 4.3.3.3, deacetylisoipecoside synthase. The product is rapidly converted to demethylalangiside.
References:
1. DeEknamkul, W., Ounaroon, A., Tanahashi, T., Kutchan, T. and Zenk, M.H. Enzymatic condensation of dopamine and secologanin by cell-free extracts of Alangium lamarckii. Phytochemistry 45 (1997) 477-484.
Recommended name: trans-feruloyl-CoA synthase
Reaction: ferulic acid + CoASH + ATP = trans-feruloyl-CoA + products of ATP breakdown
Other name(s): trans-feruloyl-CoA synthetase
Systematic name: trans-ferulate:CoASH ligase (ATP-hydrolysing)
Comments: Requires Mg2+. It has not yet been established whether AMP + diphosphate or ADP + phosphate are formed in this reaction.
References:
1. Narbad, A. and Gasson, M.J. Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens. Microbiology 144 (1998) 1397-1405. [Medline UI: 98274748]
2. Pometto, A.L. and Crawford, D.L. Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus. Appl. Environ. Microbiol. 45 (1983) 1582-1585. [Medline UI: 83254833]
Glossary
crepenynic acid: octadec-9-en-12-ynoic acid
sulcatone: 6-methylhept-5-en-2-one
sulcatol: 6-methylhept-5-en-2-ol
vanillin: 3-hydroxy-4-methoxybenzaldehyde