The Enzyme Database

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EC 1.1.1.157     
Accepted name: 3-hydroxybutyryl-CoA dehydrogenase
Reaction: (S)-3-hydroxybutanoyl-CoA + NADP+ = 3-acetoacetyl-CoA + NADPH + H+
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): β-hydroxybutyryl coenzyme A dehydrogenase; L(+)-3-hydroxybutyryl-CoA dehydrogenase; BHBD; dehydrogenase, L-3-hydroxybutyryl coenzyme A (nicotinamide adenine dinucleotide phosphate); L-(+)-3-hydroxybutyryl-CoA dehydrogenase; β-hydroxybutyryl-CoA dehydrogenase
Systematic name: (S)-3-hydroxybutanoyl-CoA:NADP+ oxidoreductase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39319-78-3
References:
1.  Madan, V.K., Hillmer, P. and Gottschalk, G. Purification and properties of NADP-dependent L(+)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium kluyveri. Eur. J. Biochem. 32 (1973) 51–56. [DOI] [PMID: 4405720]
[EC 1.1.1.157 created 1976]
 
 
EC 1.1.1.178     
Accepted name: 3-hydroxy-2-methylbutyryl-CoA dehydrogenase
Reaction: (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA + NAD+ = 2-methylacetoacetyl-CoA + NADH + H+
Other name(s): 2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase; 2-methyl-3-hydroxybutyryl coenzyme A dehydrogenase; 2-methyl-3-hydroxy-butyryl CoA dehydrogenase
Systematic name: (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA:NAD+ oxidoreductase
Comments: Also acts, more slowly, on (2S,3S)-2-hydroxy-3-methylpentanoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 52227-66-4
References:
1.  Conrad, R.S., Massey, L.K. and Sokatch, J.R. D- and L-isoleucine metabolism and regulation of their pathways in Pseudomonas putida. J. Bacteriol. 118 (1974) 103–111. [PMID: 4150713]
[EC 1.1.1.178 created 1981]
 
 
EC 1.2.1.57     
Accepted name: butanal dehydrogenase
Reaction: butanal + CoA + NAD(P)+ = butanoyl-CoA + NAD(P)H + H+
Systematic name: butanal:NAD(P)+ oxidoreductase (CoA-acylating)
Comments: Also acts on acetaldehyde, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 116412-25-0
References:
1.  Palosaari, N.R. and Rogers, P. Purification and properties of the inducible coenzyme A-linked butyraldehyde dehydrogenase from Clostridium acetobutylicum. J. Bacteriol. 170 (1988) 2971–2976. [DOI] [PMID: 3384801]
[EC 1.2.1.57 created 1992]
 
 
EC 1.3.1.52      
Transferred entry: 2-methyl-branched-chain-enoyl-CoA reductase. Now EC 1.3.8.5, 2-methyl-branched-chain-enoyl-CoA reductase
[EC 1.3.1.52 created 1992, deleted 2012]
 
 
EC 1.3.1.85     
Accepted name: crotonyl-CoA carboxylase/reductase
Reaction: (2S)-ethylmalonyl-CoA + NADP+ = (E)-but-2-enoyl-CoA + CO2 + NADPH + H+
Glossary: (E)-but-2-enoyl-CoA = crotonyl-CoA
Other name(s): CCR; crotonyl-CoA reductase (carboxylating)
Systematic name: (2S)-ethylmalonyl-CoA:NADP+ oxidoreductase (decarboxylating)
Comments: The reaction is catalysed in the reverse direction. This enzyme, isolated from the bacterium Rhodobacter sphaeroides, catalyses (E)-but-2-enoyl-CoA-dependent oxidation of NADPH in the presence of CO2. When CO2 is absent, the enzyme catalyses the reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA, but with only 10% of maximal activity (relative to (E)-but-2-enoyl-CoA carboxylation).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Erb, T.J., Berg, I.A., Brecht, V., Muller, M., Fuchs, G. and Alber, B.E. Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway. Proc. Natl. Acad. Sci. USA 104 (2007) 10631–10636. [DOI] [PMID: 17548827]
2.  Erb, T.J., Brecht, V., Fuchs, G., Muller, M. and Alber, B.E. Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase. Proc. Natl. Acad. Sci. USA 106 (2009) 8871–8876. [DOI] [PMID: 19458256]
[EC 1.3.1.85 created 2011]
 
 
EC 1.3.1.86     
Accepted name: crotonyl-CoA reductase
Reaction: butanoyl-CoA + NADP+ = (E)-but-2-enoyl-CoA + NADPH + H+
For diagram of lysine catabolism, click here
Glossary: (E)-but-2-enoyl-CoA = crotonyl-CoA
butanoyl-CoA = butyryl-CoA
Other name(s): butyryl-CoA dehydrogenase; butyryl dehydrogenase; unsaturated acyl-CoA reductase; ethylene reductase; enoyl-coenzyme A reductase; unsaturated acyl coenzyme A reductase; butyryl coenzyme A dehydrogenase; short-chain acyl CoA dehydrogenase; short-chain acyl-coenzyme A dehydrogenase; 3-hydroxyacyl CoA reductase; butanoyl-CoA:(acceptor) 2,3-oxidoreductase; CCR
Systematic name: butanoyl-CoA:NADP+ 2,3-oxidoreductase
Comments: Catalyses the reaction in the reverse direction. This enzyme from Streptomyces collinus is specific for (E)-but-2-enoyl-CoA, and is proposed to provide butanoyl-CoA as a starter unit for straight-chain fatty acid biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wallace, K.K., Bao, Z.Y., Dai, H., Digate, R., Schuler, G., Speedie, M.K. and Reynolds, K.A. Purification of crotonyl-CoA reductase from Streptomyces collinus and cloning, sequencing and expression of the corresponding gene in Escherichia coli. Eur. J. Biochem. 233 (1995) 954–962. [DOI] [PMID: 8521864]
[EC 1.3.1.86 created 2011]
 
 
EC 1.3.1.109     
Accepted name: butanoyl-CoA dehydrogenase (NAD+, ferredoxin)
Reaction: butanoyl-CoA + 2 NAD+ + 2 reduced ferredoxin [iron-sulfur] cluster = (E)-but-2-enoyl-CoA + 2 NADH + 2 oxidized ferredoxin [iron-sulfur] cluster
Glossary: (E)-but-2-enoyl-CoA = crotonyl-CoA
Other name(s): bifurcating butyryl-CoA dehydrogenase; butyryl-CoA dehydrogenase/Etf complex; Etf-Bcd complex; bifurcating butanoyl-CoA dehydrogenase; butanoyl-CoA dehydrogenase/Etf complex
Systematic name: butanoyl-CoA:NAD+, ferredoxin oxidoreductase
Comments: This flavin containg enzyme, isolated from the bacteria Acidaminococcus fermentans and butanoate-producing Clostridia species, couples the exergonic reduction of (E)-but-2-enoyl-CoA to butanoyl-CoA with NADH to the endergonic reduction of ferredoxin by NADH, using electron bifurcation to overcome the steep energy barrier in ferredoxin reduction.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Li, F., Hinderberger, J., Seedorf, H., Zhang, J., Buckel, W. and Thauer, R.K. Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri. J. Bacteriol. 190 (2008) 843–850. [DOI] [PMID: 17993531]
2.  Aboulnaga el,-H., Pinkenburg, O., Schiffels, J., El-Refai, A., Buckel, W. and Selmer, T. Effect of an oxygen-tolerant bifurcating butyryl coenzyme A dehydrogenase/electron-transferring flavoprotein complex from Clostridium difficile on butyrate production in Escherichia coli. J. Bacteriol. 195 (2013) 3704–3713. [DOI] [PMID: 23772070]
3.  Chowdhury, N.P., Mowafy, A.M., Demmer, J.K., Upadhyay, V., Koelzer, S., Jayamani, E., Kahnt, J., Hornung, M., Demmer, U., Ermler, U. and Buckel, W. Studies on the mechanism of electron bifurcation catalyzed by electron transferring flavoprotein (Etf) and butyryl-CoA dehydrogenase (Bcd) of Acidaminococcus fermentans. J. Biol. Chem. 289 (2014) 5145–5157. [DOI] [PMID: 24379410]
[EC 1.3.1.109 created 2015]
 
 
EC 1.3.8.1     
Accepted name: short-chain acyl-CoA dehydrogenase
Reaction: a short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
Glossary: a short-chain acyl-CoA = an acyl-CoA thioester where the acyl chain contains less than 6 carbon atoms.
Other name(s): butyryl-CoA dehydrogenase; butanoyl-CoA dehydrogenase; butyryl dehydrogenase; unsaturated acyl-CoA reductase; ethylene reductase; enoyl-coenzyme A reductase; unsaturated acyl coenzyme A reductase; butyryl coenzyme A dehydrogenase; short-chain acyl CoA dehydrogenase; short-chain acyl-coenzyme A dehydrogenase; 3-hydroxyacyl CoA reductase; butanoyl-CoA:(acceptor) 2,3-oxidoreductase; ACADS (gene name).
Systematic name: short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
Comments: Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme catalyses the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms. The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. The highest activity was reported with either butanoyl-CoA [2] or pentanoyl-CoA [4]. The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA [6]. cf. EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9027-88-7
References:
1.  Mahler, H.R. Studies on the fatty acid oxidizing system of animal tissue. IV. The prosthetic group of butyryl coenzyme A dehydrogenase. J. Biol. Chem. 206 (1954) 13–26. [PMID: 13130522]
2.  Green, D.E., Mii, S., Mahler, H.R. and Bock, R.M. Studies on the fatty acid oxidizing system of animal tissue. III. Butyryl coenzyme A dehydrogenase. J. Biol. Chem. 206 (1954) 1–12. [PMID: 13130521]
3.  Beinert, H. Acyl coenzyme A dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 447–466.
4.  Shaw, L. and Engel, P.C. The purification and properties of ox liver short-chain acyl-CoA dehydrogenase. Biochem. J. 218 (1984) 511–520. [PMID: 6712627]
5.  Thorpe, C. and Kim, J.J. Structure and mechanism of action of the acyl-CoA dehydrogenases. FASEB J. 9 (1995) 718–725. [PMID: 7601336]
6.  Ikeda, Y., Ikeda, K.O. and Tanaka, K. Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme. J. Biol. Chem. 260 (1985) 1311–1325. [PMID: 3968063]
7.  McMahon, B., Gallagher, M.E. and Mayhew, S.G. The protein coded by the PP2216 gene of Pseudomonas putida KT2440 is an acyl-CoA dehydrogenase that oxidises only short-chain aliphatic substrates. FEMS Microbiol. Lett. 250 (2005) 121–127. [DOI] [PMID: 16024185]
[EC 1.3.8.1 created 1961 as EC 1.3.2.1, transferred 1964 to EC 1.3.99.2, transferred 2011 to EC 1.3.8.1, modified 2012]
 
 
EC 1.3.8.4     
Accepted name: isovaleryl-CoA dehydrogenase
Reaction: isovaleryl-CoA + electron-transfer flavoprotein = 3-methylcrotonyl-CoA + reduced electron-transfer flavoprotein
Other name(s): isovaleryl-coenzyme A dehydrogenase; isovaleroyl-coenzyme A dehydrogenase; 3-methylbutanoyl-CoA:(acceptor) oxidoreductase
Systematic name: 3-methylbutanoyl-CoA:electron-transfer flavoprotein oxidoreductase
Comments: Contains FAD as prosthetic group. Pentanoate can act as donor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37274-61-6
References:
1.  Bachhawat, B.K., Robinson, W.G. and Coon, M.J. Enzymatic carboxylation of β-hydroxyisovaleryl coenzyme A. J. Biol. Chem. 219 (1956) 539–550. [PMID: 13319276]
2.  Ikeda, Y. and Tanaka, K. Purification and characterization of isovaleryl coenzyme A dehydrogenase from rat liver mitochondria. J. Biol. Chem. 258 (1983) 1077–1085. [PMID: 6401713]
3.  Tanaka, K., Budd, M.A., Efron, M.L. and Isselbacher, K.J. Isovaleric acidemia: a new genetic defect of leucine metabolism. Proc. Natl. Acad. Sci. USA 56 (1966) 236–242. [DOI] [PMID: 5229850]
[EC 1.3.8.4 created 1978 as EC 1.3.99.10, modified 1986, transferred 2012 to EC 1.3.8.4]
 
 
EC 1.3.8.5     
Accepted name: 2-methyl-branched-chain-enoyl-CoA reductase
Reaction: 2-methylbutanoyl-CoA + electron-transfer flavoprotein = (E)-2-methylbut-2-enoyl-CoA + reduced electron-transfer flavoprotein + H+
Systematic name: 2-methyl-branched-chain-acyl-CoA:electron-transfer flavoprotein 2-oxidoreductase
Comments: A flavoprotein (FAD) from Ascaris suum. The enzyme functions in shuttling reducing power from the electron-transport chain to 2-methyl branched-chain enoyl CoA
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Komuniecki, R., Fekete, S. and Thissen-Parra, J. Purification and characterization of the 2-methyl branched-chain acyl-CoA dehydrogenase, an enzyme involved in NADH-dependent enoyl-CoA reduction in anaerobic mitochondria of the nematode, Ascaris suum. J. Biol. Chem. 260 (1985) 4770–4777. [PMID: 3988734]
2.  Komuniecki, R., McCrury, J., Thissen, J. and Rubin, N. Electron-transfer flavoprotein from anaerobic Ascaris suum mitochondria and its role in NADH-dependent 2-methyl branched-chain enoyl-CoA reduction. Biochim. Biophys. Acta 975 (1989) 127–131. [DOI] [PMID: 2736251]
[EC 1.3.8.5 created 1992 as EC 1.3.1.52, transferred 2012 to EC 1.3.8.5]
 
 
EC 1.3.8.13     
Accepted name: crotonobetainyl-CoA reductase
Reaction: γ-butyrobetainyl-CoA + electron-transfer flavoprotein = crotonobetainyl-CoA + reduced electron-transfer flavoprotein
Glossary: γ-butyrobetainyl-CoA = 4-(trimethylammonio)butanoyl-CoA
crotonobetainyl-CoA = (E)-4-(trimethylammonio)but-2-enoyl-CoA
Other name(s): caiA (gene name)
Systematic name: γ-butyrobetainyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
Comments: The enzyme has been purified from the bacterium Escherichia coli O44 K74, in which it forms a complex with EC 2.8.3.21, L-carnitine CoA-transferase. The electron donor is believed to be an electron-transfer flavoprotein (ETF) encoded by the fixA and fixB genes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Roth, S., Jung, K., Jung, H., Hommel, R.K. and Kleber, H.P. Crotonobetaine reductase from Escherichia coli - a new inducible enzyme of anaerobic metabolization of L(–)-carnitine. Antonie Van Leeuwenhoek 65 (1994) 63–69. [PMID: 8060125]
2.  Preusser, A., Wagner, U., Elssner, T. and Kleber, H.P. Crotonobetaine reductase from Escherichia coli consists of two proteins. Biochim. Biophys. Acta 1431 (1999) 166–178. [DOI] [PMID: 10209289]
3.  Elssner, T., Hennig, L., Frauendorf, H., Haferburg, D. and Kleber, H.P. Isolation, identification, and synthesis of γ-butyrobetainyl-CoA and crotonobetainyl-CoA, compounds involved in carnitine metabolism of E. coli. Biochemistry 39 (2000) 10761–10769. [DOI] [PMID: 10978161]
4.  Walt, A. and Kahn, M.L. The fixA and fixB genes are necessary for anaerobic carnitine reduction in Escherichia coli. J. Bacteriol. 184 (2002) 4044–4047. [DOI] [PMID: 12081978]
[EC 1.3.8.13 created 2017]
 
 
EC 1.3.99.2      
Transferred entry: butyryl-CoA dehydrogenase. Now EC 1.3.8.1, butyryl-CoA dehydrogenase.
[EC 1.3.99.2 created 1961 as EC 1.3.2.1, transferred 1964 to EC 1.3.99.2, deleted 2011]
 
 
EC 1.3.99.10      
Transferred entry: isovaleryl-CoA dehydrogenase. Now EC 1.3.8.4, isovaleryl-CoA dehydrogenase
[EC 1.3.99.10 created 1978, modified 1986, deleted 2012]
 
 
EC 1.3.99.12     
Accepted name: 2-methylacyl-CoA dehydrogenase
Reaction: 2-methylbutanoyl-CoA + acceptor = 2-methylbut-2-enoyl-CoA + reduced acceptor
Other name(s): branched-chain acyl-CoA dehydrogenase; 2-methyl branched chain acyl-CoA dehydrogenase; 2-methylbutanoyl-CoA:(acceptor) oxidoreductase
Systematic name: 2-methylbutanoyl-CoA:acceptor oxidoreductase
Comments: Also oxidizes 2-methylpropanoyl-CoA. Not identical with EC 1.3.8.1 (butyryl-CoA dehydrogenase), EC 1.3.8.7 (medium-chain acyl-CoA dehydrogenase), EC 1.3.8.8 (long-chain acyl-CoA dehydrogenase), EC 1.3.8.9 (very-long-chain acyl-CoA dehydrogenase) or EC 1.3.99.10 (isovaleryl-CoA dehydrogenase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85130-32-1
References:
1.  Ikeda, Y., Dabrowski, C. and Tanaka, K. Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase. J. Biol. Chem. 258 (1983) 1066–1076. [PMID: 6401712]
[EC 1.3.99.12 created 1986]
 
 
EC 2.1.3.15     
Accepted name: acetyl-CoA carboxytransferase
Reaction: [biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier protein]-N6-biotinyl-L-lysine + malonyl-CoA
Other name(s): accAD (gene names)
Systematic name: [biotin carboxyl-carrier protein]-N6-carboxybiotinyl-L-lysine:acetyl-CoA:carboxytransferase
Comments: The enzyme catalyses the transfer of a carboxyl group carried on a biotinylated biotin carboxyl carrier protein (BCCP) to acetyl-CoA, forming malonyl-CoA. In some organisms this activity is part of a multi-domain polypeptide that includes the carrier protein and EC 6.3.4.14, biotin carboxylase (see EC 6.4.1.2, acetyl-CoA carboxylase). Some enzymes can also carboxylate propanonyl-CoA and butanoyl-CoA (cf. EC 6.4.1.3, propionyl-CoA carboxylase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9023-93-2
References:
1.  Bilder, P., Lightle, S., Bainbridge, G., Ohren, J., Finzel, B., Sun, F., Holley, S., Al-Kassim, L., Spessard, C., Melnick, M., Newcomer, M. and Waldrop, G.L. The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme. Biochemistry 45 (2006) 1712–1722. [DOI] [PMID: 16460018]
2.  Chuakrut, S., Arai, H., Ishii, M. and Igarashi, Y. Characterization of a bifunctional archaeal acyl coenzyme A carboxylase. J. Bacteriol. 185 (2003) 938–947. [DOI] [PMID: 12533469]
[EC 2.1.3.15 created 2017]
 
 
EC 2.3.1.7     
Accepted name: carnitine O-acetyltransferase
Reaction: acetyl-CoA + carnitine = CoA + O-acetylcarnitine
Other name(s): acetyl-CoA-carnitine O-acetyltransferase; acetylcarnitine transferase; carnitine acetyl coenzyme A transferase; carnitine acetylase; carnitine acetyltransferase; carnitine-acetyl-CoA transferase; CATC
Systematic name: acetyl-CoA:carnitine O-acetyltransferase
Comments: Also acts on propanoyl-CoA and butanoyl-CoA (cf. EC 2.3.1.21 carnitine O-palmitoyltransferase and EC 2.3.1.137 carnitine O-octanoyltransferase).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9029-90-7
References:
1.  Chase, J.F.A., Pearson, D.J. and Tubbs, P.K. The preparation of crystalline carnitine acetyltransferase. Biochim. Biophys. Acta 96 (1965) 162–165. [DOI] [PMID: 14285260]
2.  Friedman, S. and Fraenkel, G. Reversible enzymatic acetylation of carnitine. Arch. Biochem. Biophys. 59 (1955) 491–501. [DOI] [PMID: 13275966]
3.  Miyazawa, S., Ozasa, H., Furuta, S., Osumi, T. and Hashimoto, T. Purification and properties of carnitine acetyl transferase from rat liver. J. Biochem. (Tokyo) 93 (1983) 439–451. [PMID: 6404901]
[EC 2.3.1.7 created 1961]
 
 
EC 2.3.1.19     
Accepted name: phosphate butyryltransferase
Reaction: butanoyl-CoA + phosphate = CoA + butanoyl phosphate
Other name(s): phosphotransbutyrylase
Systematic name: butanoyl-CoA:phosphate butanoyltransferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-01-7
References:
1.  Valentine, R.C. and Wolfe, R.S. Purification and role of phosphotransbutyrylase. J. Biol. Chem. 235 (1960) 1948–1952. [PMID: 13840823]
[EC 2.3.1.19 created 1965]
 
 
EC 2.3.1.93     
Accepted name: 13-hydroxylupanine O-tigloyltransferase
Reaction: (E)-2-methylcrotonoyl-CoA + 13-hydroxylupanine = CoA + 13-[(E)-2-methylcrotonoyl]oxylupanine
Glossary: (E)-2-methylcrotonoyl-CoA = tigloyl-CoA = (E)-2-methylbut-2-enoyl-CoA
Other name(s): tigloyl-CoA:13-hydroxylupanine O-tigloyltransferase; 13-hydroxylupanine acyltransferase
Systematic name: (E)-2-methylcrotonoyl-CoA:13-hydroxylupanine O-2-methylcrotonoyltransferase
Comments: Benzoyl-CoA and, more slowly, pentanoyl-CoA, 3-methylbutanoyl-CoA and butanoyl-CoA can act as acyl donors. Involved in the synthesis of lupanine alkaloids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 85341-00-0
References:
1.  Wink, M. and Hartmann, T. Enzymatic synthesis of quinolizidine alkaloid esters: a tigloyl-CoA:13-hydroxylupanine O-tigloyl transferase from Lupinus albus L. Planta 156 (1982) 560–565. [PMID: 24272737]
2.  Okada, T.. Hirai, M.Y., Suzuki, H., Yamazaki, M. and Saito, K. Molecular characterization of a novel quinolizidine alkaloid O-tigloyltransferase: cDNA cloning, catalytic activity of recombinant protein and expression analysis in Lupinus plants. Plant Cell Physiol. 46 (2005) 233–244. [PMID: 15659437]
3.  Suzuki, H., Murakoshi, I. and Saito, K. A novel O-tigloyltransferase for alkaloid biosynthesis in plants. Purification, characterization, and distribution in Lupinus plants. J. Biol. Chem. 269 (1994) 15853–15860. [PMID: 8195240]
[EC 2.3.1.93 created 1986, modified 2011]
 
 
EC 2.3.1.247     
Accepted name: 3-keto-5-aminohexanoate cleavage enzyme
Reaction: (5S)-5-amino-3-oxohexanoate + acetyl-CoA = L-3-aminobutanoyl-CoA + acetoacetate
For diagram of lysine catabolism, click here
Glossary: L-3-aminobutyryl-CoA = (3S)-3-aminobutanoyl-CoA
Other name(s): kce (gene name)
Systematic name: (5S)-5-amino-3-oxohexanoate:acetyl-CoA ethylamine transferase
Comments: Requires Zn2+. The enzyme, isolated from the bacteria Fusobacterium nucleatum and Cloacimonas acidaminovorans, is involved in the anaerobic fermentation of lysine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Barker, H.A., Kahn, J.M. and Hedrick, L. Pathway of lysine degradation in Fusobacterium nucleatum. J. Bacteriol. 152 (1982) 201–207. [PMID: 6811551]
2.  Kreimeyer, A., Perret, A., Lechaplais, C., Vallenet, D., Medigue, C., Salanoubat, M. and Weissenbach, J. Identification of the last unknown genes in the fermentation pathway of lysine. J. Biol. Chem. 282 (2007) 7191–7197. [DOI] [PMID: 17166837]
3.  Bellinzoni, M., Bastard, K., Perret, A., Zaparucha, A., Perchat, N., Vergne, C., Wagner, T., de Melo-Minardi, R.C., Artiguenave, F., Cohen, G.N., Weissenbach, J., Salanoubat, M. and Alzari, P.M. 3-Keto-5-aminohexanoate cleavage enzyme: a common fold for an uncommon Claisen-type condensation. J. Biol. Chem. 286 (2011) 27399–27405. [DOI] [PMID: 21632536]
[EC 2.3.1.247 created 2015]
 
 
EC 2.3.3.5     
Accepted name: 2-methylcitrate synthase
Reaction: propanoyl-CoA + H2O + oxaloacetate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate + CoA
For diagram of reaction, click here
Glossary: 2-methylcitrate = (2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate
Other name(s): 2-methylcitrate oxaloacetate-lyase; MCS; methylcitrate synthase; methylcitrate synthetase
Systematic name: propanoyl-CoA:oxaloacetate C-propanoyltransferase (thioester-hydrolysing, 1-carboxyethyl-forming)
Comments: The enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and pentanoyl-CoA. The relative rate of condensation of acetyl-CoA and oxaloacetate is 140% of that of propanoyl-CoA and oxaloacetate, but the enzyme is distinct from EC 2.3.3.1, citrate (Si)-synthase. Oxaloacetate cannot be replaced by glyoxylate, pyruvate or 2-oxoglutarate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 57827-78-8
References:
1.  Uchiyama, H. and Tabuchi, T. Properties of methylcitrate synthase from Candida lipolytica. Agric. Biol. Chem. 40 (1976) 1411–1418.
2.  Textor, S., Wendisch, V.F., De Graaf, A.A., Muller, U., Linder, M.I., Linder, D. and Buckel, W. Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria. Arch. Microbiol. 168 (1997) 428–436. [PMID: 9325432]
3.  Horswill, A.R. and Escalante-Semerena, J.C. Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle. J. Bacteriol. 181 (1999) 5615–5623. [PMID: 10482501]
4.  Brock, M., Maerker, C., Schütz, A., Völker, U. and Buckel, W. Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Eur. J. Biochem. 269 (2002) 6184–6194. [DOI] [PMID: 12473114]
5.  Domin, N., Wilson, D. and Brock, M. Methylcitrate cycle activation during adaptation of Fusarium solani and Fusarium verticillioides to propionyl-CoA-generating carbon sources. Microbiology 155 (2009) 3903–3912. [DOI] [PMID: 19661181]
[EC 2.3.3.5 created 1978 as EC 4.1.3.31, transferred 2002 to EC 2.3.3.5, modified 2015]
 
 
EC 2.3.3.7     
Accepted name: 3-ethylmalate synthase
Reaction: butanoyl-CoA + H2O + glyoxylate = 3-ethylmalate + CoA
For diagram of reaction, click here
Other name(s): 2-ethyl-3-hydroxybutanedioate synthase; 3-ethylmalate glyoxylate-lyase (CoA-butanoylating)
Systematic name: butanoyl-CoA:glyoxylate C-butanoyltransferase (thioester-hydrolysing, 1-carboxypropyl-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-01-5
References:
1.  Ramasarma, T. and Giri, K.V. Phosphoglucose isomerase of green gram (Phaseolus radiatus). Arch. Biochem. Biophys. 62 (1956) 91–96. [DOI] [PMID: 13314642]
[EC 2.3.3.7 created 1965 as EC 4.1.3.10, modified 1983, transferred 2002 to EC 2.3.3.10]
 
 
EC 2.6.1.111     
Accepted name: 3-aminobutanoyl-CoA transaminase
Reaction: 3-aminobutanoyl-CoA + 2-oxoglutarate = acetoacetyl-CoA + L-glutamate
Other name(s): kat (gene name); acyl-CoA β-transaminase
Systematic name: 3-aminobutanoyl-CoA:2-oxoglutarate aminotransferase
Comments: The enzyme, found in bacteria, is part of a L-lysine degradation pathway. The enzyme is also active with other β-amino compounds such as 3-amino-5-methylhexanoyl-CoA and 3-amino-3-phenylpropanoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Perret, A., Lechaplais, C., Tricot, S., Perchat, N., Vergne, C., Pelle, C., Bastard, K., Kreimeyer, A., Vallenet, D., Zaparucha, A., Weissenbach, J. and Salanoubat, M. A novel acyl-CoA β-transaminase characterized from a metagenome. PLoS One 6:e22918 (2011). [DOI] [PMID: 21826218]
[EC 2.6.1.111 created 2017]
 
 
EC 2.8.3.8     
Accepted name: acetate CoA-transferase
Reaction: acyl-CoA + acetate = a fatty acid anion + acetyl-CoA
Other name(s): acetate coenzyme A-transferase; butyryl CoA:acetate CoA transferase; butyryl coenzyme A transferase
Systematic name: acyl-CoA:acetate CoA-transferase
Comments: The enzyme belongs to family I of CoA-transferases, which operate with a ping-pong kinetic mechanism. The reaction takes place in two half-reactions and involves the formation of a CoA thioester intermediate with a glutamate residue. Unlike EC 2.8.3.9, butyrate—acetoacetate CoA-transferase, this enzyme exhibits maximal activity using acetate as the CoA acceptor. Substrate range depends on the specific enzyme. Typical substrates include butanoyl-CoA and pentanoyl-CoA.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 37278-35-6
References:
1.  Vanderwinkel, E., Furmanski, P., Reeves, H.C. and Ajl, S.J. Growth of Escherichia coli on fatty acids: requirement for coenzyme A transferase activity. Biochem. Biophys. Res. Commun. 33 (1968) 902–908. [DOI] [PMID: 4884054]
2.  Rangarajan, E.S., Li, Y., Ajamian, E., Iannuzzi, P., Kernaghan, S.D., Fraser, M.E., Cygler, M. and Matte, A. Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases. J. Biol. Chem. 280 (2005) 42919–42928. [DOI] [PMID: 16253988]
[EC 2.8.3.8 created 1972]
 
 
EC 2.8.3.9     
Accepted name: butyrate—acetoacetate CoA-transferase
Reaction: butanoyl-CoA + acetoacetate = butanoate + acetoacetyl-CoA
Other name(s): butyryl coenzyme A-acetoacetate coenzyme A-transferase; butyryl-CoA-acetoacetate CoA-transferase
Systematic name: butanoyl-CoA:acetoacetate CoA-transferase
Comments: Butanoate, acetoacetate and their CoA thioesters are the preferred substrates, but the enzyme also acts, more slowly, on the derivatives of a number of C2 to C6 monocarboxylic acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 66231-37-6
References:
1.  Barker, H.A., Jeng, I.-M., Neff, N., Robertson, J.M., Tam, F.K. and Hosaka, S. Butyryl-CoA:acetoacetate CoA-transferase from a lysine-fermenting Clostridium. J. Biol. Chem. 253 (1978) 1219–1225. [PMID: 624727]
[EC 2.8.3.9 created 1984]
 
 
EC 2.8.3.14     
Accepted name: 5-hydroxypentanoate CoA-transferase
Reaction: acetyl-CoA + 5-hydroxypentanoate = acetate + 5-hydroxypentanoyl-CoA
Other name(s): 5-hydroxyvalerate CoA-transferase; 5-hydroxyvalerate coenzyme A transferase
Systematic name: acetyl-CoA:5-hydroxypentanoate CoA-transferase
Comments: Propanoyl-CoA, acetyl-CoA, butanoyl-CoA and some other acyl-CoAs can act as substrates, but more slowly than 5-hydroxypentanoyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 111684-68-5
References:
1.  Eikmanns, U. and Buckel, W. Properties of 5-hydroxyvalerate CoA-transferase from Clostridium aminovalericum. Biol. Chem. Hoppe-Seyler 371 (1990) 1077–1082. [PMID: 2085413]
[EC 2.8.3.14 created 1992]
 
 
EC 2.8.3.21     
Accepted name: L-carnitine CoA-transferase
Reaction: (1) (E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA
(2) 4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA
Glossary: L-carnitine = (3R)-3-hydroxy-4-(trimethylammonio)butanoate
(E)-4-(trimethylammonio)but-2-enoate = crotonobetaine
4-trimethylammoniobutanoate = γ-butyrobetaine
Other name(s): CaiB; crotonobetainyl/γ-butyrobetainyl-CoA:carnitine CoA-transferase
Systematic name: (E)-4-(trimethylammonio)but-2-enoyl-CoA:L-carnitine CoA-transferase
Comments: The enzyme is found in gammaproteobacteria such as Proteus sp. and Escherichia coli. It has similar activity with both substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Engemann, C., Elssner, T. and Kleber, H.P. Biotransformation of crotonobetaine to L-(–)-carnitine in Proteus sp. Arch. Microbiol. 175 (2001) 353–359. [PMID: 11409545]
2.  Elssner, T., Engemann, C., Baumgart, K. and Kleber, H.P. Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli. Biochemistry 40 (2001) 11140–11148. [DOI] [PMID: 11551212]
3.  Stenmark, P., Gurmu, D. and Nordlund, P. Crystal structure of CaiB, a type-III CoA transferase in carnitine metabolism. Biochemistry 43 (2004) 13996–14003. [DOI] [PMID: 15518548]
4.  Engemann, C., Elssner, T., Pfeifer, S., Krumbholz, C., Maier, T. and Kleber, H.P. Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp. Arch. Microbiol. 183 (2005) 176–189. [DOI] [PMID: 15731894]
5.  Rangarajan, E.S., Li, Y., Iannuzzi, P., Cygler, M. and Matte, A. Crystal structure of Escherichia coli crotonobetainyl-CoA: carnitine CoA-transferase (CaiB) and its complexes with CoA and carnitinyl-CoA. Biochemistry 44 (2005) 5728–5738. [DOI] [PMID: 15823031]
[EC 2.8.3.21 created 2014]
 
 
EC 3.5.1.51     
Accepted name: 4-acetamidobutyryl-CoA deacetylase
Reaction: 4-acetamidobutanoyl-CoA + H2O = acetate + 4-aminobutanoyl-CoA
Other name(s): aminobutyryl-CoA thiolesterase; deacetylase-thiolesterase
Systematic name: 4-acetamidobutanoyl-CoA amidohydrolase
Comments: The enzyme also hydrolyses 4-aminobutanoyl-CoA to aminobutanoate and coenzyme A.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ohsugi, M., Khan, J., Hensley, C., Chew, S. and Barker, H.A. Metabolism of L-β-lysine by a Pseudomonas. Purification and properties of a deacetylase-thiolesterase utilizing 4-acetamidobutyryl CoA and related compounds. J. Biol. Chem. 256 (1981) 7642–7651. [PMID: 6788773]
[EC 3.5.1.51 created 1984]
 
 
EC 4.1.1.94     
Accepted name: ethylmalonyl-CoA decarboxylase
Reaction: (S)-ethylmalonyl-CoA = butanoyl-CoA + CO2
Systematic name: (S)-ethylmalonyl-CoA carboxy-lyase (butanoyl-CoA-forming)
Comments: The enzyme, which exists in all vertebrates, decarboxylates ethylmalonyl-CoA, a potentially toxic compound that is formed in low amounts by the activity of EC 6.4.1.2, acetyl-CoA carboxylase and EC 6.4.1.3, propanoyl-CoA carboxylase. It prefers the S isomer, and can decarboxylate (R)-ethylmalonyl-CoA with lower efficiency. cf. EC 7.2.4.1, (S)-methylmalonyl-CoA decarboxylase (sodium-transporting).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Linster, C.L., Noel, G., Stroobant, V., Vertommen, D., Vincent, M.F., Bommer, G.T., Veiga-da-Cunha, M. and Van Schaftingen, E. Ethylmalonyl-CoA decarboxylase, a new enzyme involved in metabolite proofreading. J. Biol. Chem. 286 (2011) 42992–43003. [DOI] [PMID: 22016388]
[EC 4.1.1.94 created 2012]
 
 
EC 4.1.3.36     
Accepted name: 1,4-dihydroxy-2-naphthoyl-CoA synthase
Reaction: 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA = 1,4-dihydroxy-2-naphthoyl-CoA + H2O
For diagram of vitamin-K biosynthesis, click here
Other name(s): naphthoate synthase; 1,4-dihydroxy-2-naphthoate synthase; dihydroxynaphthoate synthase; o-succinylbenzoyl-CoA 1,4-dihydroxy-2-naphthoate-lyase (cyclizing); MenB; o-succinylbenzoyl-CoA dehydratase (cyclizing)
Systematic name: 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA dehydratase (cyclizing)
Comments: This enzyme is involved in the synthesis of 1,4-dihydroxy-2-naphthoate, a branch point metabolite leading to the biosynthesis of menaquinone (vitamin K2, in bacteria), phylloquinone (vitamin K1 in plants), and many plant pigments. The coenzyme A group is subsequently removed from the product by EC 3.1.2.28, 1,4-dihydroxy-2-naphthoyl-CoA hydrolase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 61328-42-5
References:
1.  Meganathan, R. and Bentley, R. Menaquinone (vitamin K2) biosynthesis: conversion of o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid by Mycobacterium phlei enzymes. J. Bacteriol. 140 (1979) 92–98. [PMID: 500558]
2.  Kolkmann, R. and Leistner, E. 4-(2′-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis. Z. Naturforsch. C: Sci. 42 (1987) 1207–1214. [PMID: 2966501]
3.  Johnson, T.W., Shen, G., Zybailov, B., Kolling, D., Reategui, R., Beauparlant, S., Vassiliev, I.R., Bryant, D.A., Jones, A.D., Golbeck, J.H. and Chitnis, P.R. Recruitment of a foreign quinone into the A(1) site of photosystem I. I. Genetic and physiological characterization of phylloquinone biosynthetic pathway mutants in Synechocystis sp. PCC 6803. J. Biol. Chem. 275 (2000) 8523–8530. [DOI] [PMID: 10722690]
4.  Truglio, J.J., Theis, K., Feng, Y., Gajda, R., Machutta, C., Tonge, P.J. and Kisker, C. Crystal structure of Mycobacterium tuberculosis MenB, a key enzyme in vitamin K2 biosynthesis. J. Biol. Chem. 278 (2003) 42352–42360. [DOI] [PMID: 12909628]
[EC 4.1.3.36 created 1992, modified 2010]
 
 
EC 4.2.1.55     
Accepted name: 3-hydroxybutyryl-CoA dehydratase
Reaction: (3R)-3-hydroxybutanoyl-CoA = crotonoyl-CoA + H2O
For diagram of Benzoyl-CoA catabolism, click here
Other name(s): D-3-hydroxybutyryl coenzyme A dehydratase; D-3-hydroxybutyryl-CoA dehydratase; enoyl coenzyme A hydrase (D); (3R)-3-hydroxybutanoyl-CoA hydro-lyase
Systematic name: (3R)-3-hydroxybutanoyl-CoA hydro-lyase (crotonoyl-CoA-forming)
Comments: Also acts on crotonoyl thioesters of pantetheine and acyl-carrier protein.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-82-7
References:
1.  Moskowitz, G.J. and Merrick, J.M. Metabolism of poly-β-hydroxybutyrate. II. Enzymatic synthesis of D-(-)-β-hydroxybutyryl coenzyme A by an enoyl hydrase from Rhodospirillum rubrum. Biochemistry 8 (1969) 2748–2755. [PMID: 5808333]
[EC 4.2.1.55 created 1972]
 
 
EC 4.2.1.116     
Accepted name: 3-hydroxypropionyl-CoA dehydratase
Reaction: 3-hydroxypropanoyl-CoA = acryloyl-CoA + H2O
For diagram of the 3-hydroxypropanoate cycle, click here and for diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Glossary: acryloyl-CoA = acrylyl-CoA
3-hydroxypropanoyl-CoA = 3-hydroxypropionyl-CoA
Other name(s): 3-hydroxypropionyl-CoA hydro-lyase; 3-hydroxypropanoyl-CoA dehydratase
Systematic name: 3-hydroxypropanoyl-CoA hydro-lyase
Comments: Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [1]. The enzyme from Metallosphaera sedula acts nearly equally as well on (S)-3-hydroxybutanoyl-CoA but not (R)-3-hydroxybutanoyl-CoA [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782–1786. [DOI] [PMID: 18079405]
2.  Teufel, R., Kung, J.W., Kockelkorn, D., Alber, B.E. and Fuchs, G. 3-hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales. J. Bacteriol. 191 (2009) 4572–4581. [DOI] [PMID: 19429610]
[EC 4.2.1.116 created 2009]
 
 
EC 4.2.1.120     
Accepted name: 4-hydroxybutanoyl-CoA dehydratase
Reaction: 4-hydroxybutanoyl-CoA = (E)-but-2-enoyl-CoA + H2O
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Glossary: 4-hydroxybutanoyl-CoA = 4-hydroxybutyryl-CoA
(E)-but-2-enoyl-CoA = crotonyl-CoA
Systematic name: 4-hydroxybutanoyl-CoA hydro-lyase
Comments: Contains FAD and a [4Fe-4S] iron-sulfur cluster. The enzyme has been characterized from several microorganisms, including Clostridium kluyveri, where it participates in succinate fermentation [1,2], Clostridium aminobutyricum, where it participates in 4-aminobutyrate degradation [3,4], and Metallosphaera sedula, where it participates in the 3-hydroxypropionate/4-hydroxybutyrate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [5].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Bartsch, R.G. and Barker, H.A. A vinylacetyl isomerase from Clostridium kluyveri. Arch. Biochem. Biophys. 92 (1961) 122–132. [DOI] [PMID: 13687513]
2.  Scherf, U., Sohling, B., Gottschalk, G., Linder, D. and Buckel, W. Succinate-ethanol fermentation in Clostridium kluyveri: purification and characterisation of 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA Δ32-isomerase. Arch. Microbiol. 161 (1994) 239–245. [PMID: 8161284]
3.  Scherf, U. and Buckel, W. Purification and properties of an iron-sulfur and FAD-containing 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA Δ32-isomerase from Clostridium aminobutyricum. Eur. J. Biochem. 215 (1993) 421–429. [DOI] [PMID: 8344309]
4.  Muh, U., Cinkaya, I., Albracht, S.P. and Buckel, W. 4-Hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum: characterization of FAD and iron-sulfur clusters involved in an overall non-redox reaction. Biochemistry 35 (1996) 11710–11718. [DOI] [PMID: 8794752]
5.  Berg, I.A., Kockelkorn, D., Buckel, W. and Fuchs, G. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318 (2007) 1782–1786. [DOI] [PMID: 18079405]
[EC 4.2.1.120 created 2009]
 
 
EC 4.2.1.149     
Accepted name: crotonobetainyl-CoA hydratase
Reaction: L-carnitinyl-CoA = (E)-4-(trimethylammonio)but-2-enoyl-CoA + H2O
Glossary: L-carnitinyl-CoA = (3R)-3-hydroxy-4-(trimethylammonio)butanoyl-CoA
(E)-4-(trimethylammonio)but-2-enoyl-CoA = crotonobetainyl-CoA
Other name(s): CaiD; L-carnityl-CoA dehydratase
Systematic name: L-carnitinyl-CoA hydro-lyase [(E)-4-(trimethylammonio)but-2-enoyl-CoA-forming]
Comments: The enzyme is also able to use crotonyl-CoA as substrate, with low efficiency [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Engemann, C., Elssner, T. and Kleber, H.P. Biotransformation of crotonobetaine to L-(–)-carnitine in Proteus sp. Arch. Microbiol. 175 (2001) 353–359. [PMID: 11409545]
2.  Elssner, T., Engemann, C., Baumgart, K. and Kleber, H.P. Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli. Biochemistry 40 (2001) 11140–11148. [DOI] [PMID: 11551212]
3.  Engemann, C., Elssner, T., Pfeifer, S., Krumbholz, C., Maier, T. and Kleber, H.P. Identification and functional characterisation of genes and corresponding enzymes involved in carnitine metabolism of Proteus sp. Arch. Microbiol. 183 (2005) 176–189. [DOI] [PMID: 15731894]
[EC 4.2.1.149 created 2014]
 
 
EC 4.2.1.153     
Accepted name: 3-methylfumaryl-CoA hydratase
Reaction: (S)-citramalyl-CoA = 3-methylfumaryl-CoA + H2O
For diagram of the 3-hydroxypropanoate cycle, click here
Glossary: (S)-citramalyl-CoA = (3S)-3-carboxy-3-hydroxybutanoyl-CoA
3-methylfumaryl-CoA = (E)-3-carboxybut-2-enoyl-CoA
Other name(s): Meh; mesaconyl-C4-CoA hydratase; mesaconyl-coenzyme A hydratase (ambiguous)
Systematic name: (S)-citramalyl-CoA hydro-lyase (3-methylfumaryl-CoA-forming)
Comments: The enzyme from the bacterium Chloroflexus aurantiacus is part of the 3-hydroxypropanoate cycle for carbon assimilation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Zarzycki, J., Brecht, V., Muller, M. and Fuchs, G. Identifying the missing steps of the autotrophic 3-hydroxypropionate CO2 fixation cycle in Chloroflexus aurantiacus. Proc. Natl. Acad. Sci. USA 106 (2009) 21317–21322. [DOI] [PMID: 19955419]
[EC 4.2.1.153 created 2014]
 
 
EC 5.1.2.3     
Accepted name: 3-hydroxybutyryl-CoA epimerase
Reaction: (S)-3-hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA
Other name(s): 3-hydroxybutyryl coenzyme A epimerase; 3-hydroxyacyl-CoA epimerase
Systematic name: 3-hydroxybutanoyl-CoA 3-epimerase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-21-9
References:
1.  Stern, J.R., del Campillo, A. and Lehninger, A.L. Enzymatic racemization of β-hydroxybutyryl-S-CoA and the stereospecificity of enzymes of the fatty acid cycle. J. Am. Chem. Soc. 77 (1955) 1073–1074.
2.  Wakil, S.J. D(-)β-Hydroxybutyryl CoA dehydrogenase. Biochim. Biophys. Acta 18 (1955) 314–315. [PMID: 13276396]
[EC 5.1.2.3 created 1961]
 
 
EC 5.3.3.20      
Transferred entry: 2-hydroxyisobutanoyl-CoA mutase. Now EC 5.4.99.64, 2-hydroxyisobutanoyl-CoA mutase
[EC 5.3.3.20 created 2016, deleted 2017]
 
 
EC 5.4.99.13     
Accepted name: isobutyryl-CoA mutase
Reaction: 2-methylpropanoyl-CoA = butanoyl-CoA
Glossary: pivalate = 2,2-dimethylpropanoate
Other name(s): isobutyryl coenzyme A mutase; butyryl-CoA:isobutyryl-CoA mutase; icmA (gene name); icmB (gene name); icmF (gene name)
Systematic name: 2-methylpropanoyl-CoA CoA-carbonylmutase
Comments: This bacterial enzyme utilizes 5′-deoxyadenosylcobalamin as a cofactor. Following substrate binding, the enzyme catalyses the homolytic cleavage of the cobalt-carbon bond of AdoCbl, yielding cob(II)alamin and a 5′-deoxyadenosyl radical, which initiates the the carbon skeleton rearrangement reaction by hydrogen atom abstraction from the substrate. At the end of each catalytic cycle the 5′-deoxyadenosyl radical and cob(II)alamin recombine, regenerating the resting form of the cofactor. The enzyme is prone to inactivation resulting from occassional loss of the 5′-deoxyadenosyl molecule. Inactivated enzymes are repaired by the action of EC 2.5.1.17, cob(I)yrinic acid a,c-diamide adenosyltransferase, and a G-protein chaperone, which restore cob(II)alamin (which is first reduced to cob(I)alamin by an unidentified reductase) to 5′-deoxyadenosylcobalamin and load it back on the mutase. Some mutases are fused with their G-protein chaperone. These enzyme can also catalyse the interconversion of isovaleryl-CoA with pivalyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 116405-23-3
References:
1.  Brendelberger, G., Rétey, J., Ashworth, D.M., Reynolds, K., Willenbrock, F. and Robinson, J.A. The enzymic interconversion of isobutyryl and N-butyrylcarba(dethia)-coenzyme-A - a coenzyme-B12-dependent carbon skeleton rearrangement. Angew. Chem. Int. Ed. Engl. 27 (1988) 1089–1091.
2.  Ratnatilleke, A., Vrijbloed, J.W. and Robinson, J.A. Cloning and sequencing of the coenzyme B12-binding domain of isobutyryl-CoA mutase from Streptomyces cinnamonensis, reconstitution of mutase activity, and characterization of the recombinant enzyme produced in Escherichia coli. J. Biol. Chem. 274 (1999) 31679–31685. [DOI] [PMID: 10531377]
3.  Cracan, V., Padovani, D. and Banerjee, R. IcmF is a fusion between the radical B12 enzyme isobutyryl-CoA mutase and its G-protein chaperone. J. Biol. Chem. 285 (2010) 655–666. [DOI] [PMID: 19864421]
4.  Cracan, V. and Banerjee, R. Novel coenzyme B12-dependent interconversion of isovaleryl-CoA and pivalyl-CoA. J. Biol. Chem. 287 (2012) 3723–3732. [DOI] [PMID: 22167181]
5.  Jost, M., Born, D.A., Cracan, V., Banerjee, R. and Drennan, C.L. Structural basis for substrate specificity in adenosylcobalamin-dependent isobutyryl-CoA mutase and related acyl-CoA mutases. J. Biol. Chem. 290 (2015) 26882–26898. [DOI] [PMID: 26318610]
6.  Li, Z., Kitanishi, K., Twahir, U.T., Cracan, V., Chapman, D., Warncke, K. and Banerjee, R. Cofactor editing by the G-protein metallochaperone domain regulates the radical B12 enzyme IcmF. J. Biol. Chem. 292 (2017) 3977–3987. [DOI] [PMID: 28130442]
[EC 5.4.99.13 created 1992, revised 2017]
 
 
EC 5.4.99.64     
Accepted name: 2-hydroxyisobutanoyl-CoA mutase
Reaction: 2-hydroxy-2-methylpropanoyl-CoA = (S)-3-hydroxybutanoyl-CoA
Glossary: 2-hydroxy-2-methylpropanoyl-CoA = 2-hydroxyisobutanoyl-CoA
Other name(s): hcmAB (gene names)
Systematic name: 2-hydroxy-2-methylpropanoyl-CoA mutase
Comments: The enzyme, characterized from the bacterium Aquincola tertiaricarbonis, uses radical chemistry to rearrange the positions of both a methyl group and a hydroxyl group. It consists of two subunits, the smaller one containing a cobalamin cofactor. It plays a central role in the degradation of assorted substrates containing a tert-butyl moiety.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Yaneva, N., Schuster, J., Schafer, F., Lede, V., Przybylski, D., Paproth, T., Harms, H., Muller, R.H. and Rohwerder, T. Bacterial acyl-CoA mutase specifically catalyzes coenzyme B12-dependent isomerization of 2-hydroxyisobutyryl-CoA and (S)-3-hydroxybutyryl-CoA. J. Biol. Chem. 287 (2012) 15502–15511. [DOI] [PMID: 22433853]
2.  Kurteva-Yaneva, N., Zahn, M., Weichler, M.T., Starke, R., Harms, H., Muller, R.H., Strater, N. and Rohwerder, T. Structural basis of the stereospecificity of bacterial B12-dependent 2-hydroxyisobutyryl-CoA mutase. J. Biol. Chem. 290 (2015) 9727–9737. [DOI] [PMID: 25720495]
[EC 5.4.99.64 created 2016 as EC 5.3.3.20, transferred 2017 to EC 5.4.99.64]
 
 
EC 6.2.1.26     
Accepted name: o-succinylbenzoate—CoA ligase
Reaction: ATP + 2-succinylbenzoate + CoA = AMP + diphosphate + 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA
For diagram of vitamin K biosynthesis, click here
Glossary: 2-succinylbenzoate = o-succinylbenzoate = 4-(2-carboxyphenyl)-4-oxobutanoate
Other name(s): o-succinylbenzoyl-coenzyme A synthetase; o-succinylbenzoate:CoA ligase (AMP-forming)
Systematic name: 2-succinylbenzoate:CoA ligase (AMP-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 72506-70-8
References:
1.  Heide, L., Arendt, S. and Leistner, E. Enzymatic-synthesis, characterization, and metabolism of the coenzyme-A ester of o-succinylbenzoic acid, an intermediate in menaquinone (vitamin K2) biosynthesis. J. Biol. Chem. 257 (1982) 7396–7400. [PMID: 7045104]
2.  Kolkmann, R. and Leistner, E. 4-(2′-Carboxyphenyl)-4-oxobutyryl coenzyme A ester, an intermediate in vitamin K2 (menaquinone) biosynthesis. Z. Naturforsch. C: Sci. 42 (1987) 1207–1214. [PMID: 2966501]
3.  Meganathan, R. and Bentley, R. Menaquinone (vitamin K2) biosynthesis: conversion of o-succinylbenzoic acid to 1,4-dihydroxy-2-naphthoic acid by Mycobacterium phlei enzymes. J. Bacteriol. 140 (1979) 92–98. [PMID: 500558]
[EC 6.2.1.26 created 1992]
 
 
EC 6.2.1.40     
Accepted name: 4-hydroxybutyrate—CoA ligase (AMP-forming)
Reaction: ATP + 4-hydroxybutanoate + CoA = AMP + diphosphate + 4-hydroxybutanoyl-CoA
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): 4-hydroxybutyrate-CoA synthetase (ambiguous); 4-hydroxybutyrate:CoA ligase (ambiguous); hbs (gene name); 4-hydroxybutyrate—CoA ligase
Systematic name: 4-hydroxybutanoate:CoA ligase (AMP-forming)
Comments: Isolated from the archaeon Metallosphaera sedula. Involved in the 3-hydroxypropanoate/4-hydroxybutanoate cycle. cf. EC 6.2.1.56, 4-hydroxybutyrate—CoA ligase (ADP-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ramos-Vera, W.H., Weiss, M., Strittmatter, E., Kockelkorn, D. and Fuchs, G. Identification of missing genes and enzymes for autotrophic carbon fixation in crenarchaeota. J. Bacteriol. 193 (2011) 1201–1211. [DOI] [PMID: 21169482]
2.  Hawkins, A.S., Han, Y., Bennett, R.K., Adams, M.W. and Kelly, R.M. Role of 4-hydroxybutyrate-CoA synthetase in the CO2 fixation cycle in thermoacidophilic archaea. J. Biol. Chem. 288 (2013) 4012–4022. [DOI] [PMID: 23258541]
[EC 6.2.1.40 created 2014, modified 2019]
 
 
EC 6.2.1.56     
Accepted name: 4-hydroxybutyrate—CoA ligase (ADP-forming)
Reaction: ATP + 4-hydroxybutanoate + CoA = ADP + phosphate + 4-hydroxybutanoyl-CoA
For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here
Other name(s): Nmar_0206 (locus name)
Systematic name: 4-hydroxybutanoate:CoA ligase (ADP-forming)
Comments: The enzyme, characterized from the marine ammonia-oxidizing archaeon Nitrosopumilus maritimus, participates in a variant of the 3-hydroxypropanoate/4-hydroxybutanate CO2 fixation cycle. cf. EC 6.2.1.40, 4-hydroxybutyrate—CoA ligase (AMP-forming).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Konneke, M., Schubert, D.M., Brown, P.C., Hugler, M., Standfest, S., Schwander, T., Schada von Borzyskowski, L., Erb, T.J., Stahl, D.A. and Berg, I.A. Ammonia-oxidizing archaea use the most energy-efficient aerobic pathway for CO2 fixation. Proc. Natl. Acad. Sci. USA 111 (2014) 8239–8244. [PMID: 24843170]
[EC 6.2.1.56 created 2019]
 
 
EC 6.4.1.3     
Accepted name: propionyl-CoA carboxylase
Reaction: ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA
For diagram of the 3-hydroxypropanoate cycle, click here
Other name(s): propionyl coenzyme A carboxylase
Systematic name: propanoyl-CoA:carbon-dioxide ligase (ADP-forming)
Comments: A biotinyl-protein. Also carboxylates butanoyl-CoA and catalyses transcarboxylation.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9023-94-3
References:
1.  Kaziro, Y., Ochoa, S., Warner, R.C. and Chen, J.-Y. Metabolism of propionic acid in animal tissues. VIII. Crystalline propionyl carboxylase. J. Biol. Chem. 236 (1961) 1917–1923. [PMID: 13752080]
2.  Lane, M.D., Halenz, D.R., Kosow, D.P. and Hegre, C.S. Further studies on mitochondrial propionyl carboxylase. J. Biol. Chem. 235 (1960) 3082–3086. [PMID: 13758723]
3.  Meyer, H., Nevaldine, B. and Meyer, F. Acyl-coenzyme A carboxylase of the free-living nematode Turbatrix aceti. 1. Its isolation and molecular characteristics. Biochemistry 17 (1978) 1822–1827. [PMID: 656363]
4.  Moss, J. and Lane, M.D. The biotin-dependent enzymes. Adv. Enzymol. Relat. Areas Mol. Biol. 35 (1971) 321–442. [PMID: 4150153]
5.  Vagelos, P. Regulation of fatty acid biosynthesis. Curr. Top. Cell. Regul. 4 (1971) 119–166.
[EC 6.4.1.3 created 1961, modified 1983]
 
 


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