The Enzyme Database

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EC 2.8.3.1     
Accepted name: propionate CoA-transferase
Reaction: acetyl-CoA + propanoate = acetate + propanoyl-CoA
Other name(s): propionate coenzyme A-transferase; propionate-CoA:lactoyl-CoA transferase; propionyl CoA:acetate CoA transferase; propionyl-CoA transferase
Systematic name: acetyl-CoA:propanoate CoA-transferase
Comments: Butanoate and lactate can also act as acceptors.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 9026-15-7
References:
1.  Stadtman, E.R. Acyl-coenzyme A synthesis by phosphotransacetylase and coenzyme A transphorase. Fed. Proc. 11 (1952) 291.
[EC 2.8.3.1 created 1961]
 
 
EC 2.8.3.2     
Accepted name: oxalate CoA-transferase
Reaction: succinyl-CoA + oxalate = succinate + oxalyl-CoA
Other name(s): succinyl—β-ketoacyl-CoA transferase; oxalate coenzyme A-transferase
Systematic name: succinyl-CoA:oxalate CoA-transferase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-17-9
References:
1.  Quayle, J.R., Keech, D.B. and Taylor, G.A. Carbon assimilation by Pseudomonas oxalaticus (OXI). 4. Metabolism of oxalate in cell-free extracts of the organism grown on oxalate. Biochem. J. 78 (1961) 225–236. [PMID: 16748872]
[EC 2.8.3.2 created 1961]
 
 
EC 2.8.3.3     
Accepted name: malonate CoA-transferase
Reaction: acetyl-CoA + malonate = acetate + malonyl-CoA
Other name(s): malonate coenzyme A-transferase
Systematic name: acetyl-CoA:malonate CoA-transferase
Comments: The enzyme from Pseudomonas ovalis also catalyses the reaction of EC 4.1.1.9 malonyl-CoA decarboxylase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-18-0
References:
1.  Hayaishi, O. Enzymatic decarboxylation of malonic acid. J. Biol. Chem. 215 (1955) 125–136. [PMID: 14392148]
2.  Takamura, Y. and Kitayama, Y. Purification and some properties of malonate decarboxylase from Pseudomonas ovalis: an oligomeric enzyme with bifunctional properties. Biochem. Int. 3 (1981) 483–491.
[EC 2.8.3.3 created 1961]
 
 
EC 2.8.3.4      
Deleted entry:  butyrate CoA-transferase
[EC 2.8.3.4 created 1961, deleted 1964]
 
 
EC 2.8.3.5     
Accepted name: 3-oxoacid CoA-transferase
Reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA
Other name(s): 3-oxoacid coenzyme A-transferase; 3-ketoacid CoA-transferase; 3-ketoacid coenzyme A transferase; 3-oxo-CoA transferase; 3-oxoacid CoA dehydrogenase; acetoacetate succinyl-CoA transferase; acetoacetyl coenzyme A-succinic thiophorase; succinyl coenzyme A-acetoacetyl coenzyme A-transferase; succinyl-CoA transferase
Systematic name: succinyl-CoA:3-oxo-acid CoA-transferase
Comments: Acetoacetate and, more slowly, 3-oxopropanoate, 3-oxopentanoate, 3-oxo-4-methylpentanoate or 3-oxohexanoate can act as acceptors; malonyl-CoA can act instead of succinyl-CoA.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9027-43-4
References:
1.  Hersh, L.B. and Jencks, W.P. Coenzyme A transferase. Kinetics and exchange reactions. J. Biol. Chem. 242 (1967) 3468–3480.
2.  Lynen, F. and Ochoa, S. Enzymes of fatty acid metabolism. Biochim. Biophys. Acta 12 (1953) 299–314. [DOI] [PMID: 13115439]
3.  Menon, G.K.K. and Stern, J.R. Enzymic synthesis and metabolism of malonyl coenzyme A and glutaryl coenzyme A. J. Biol. Chem. 235 (1960) 3393–3398. [PMID: 13769479]
4.  Stern, J.R., Coon, M.J., del Campillo, A. and Schneider, M.C. Enzymes of fatty acid metabolism. IV. Preparation and properties of coenzyme A transferase. J. Biol. Chem. 221 (1956) 15–31. [PMID: 13345795]
[EC 2.8.3.5 created 1961, modified 1980]
 
 
EC 2.8.3.6     
Accepted name: 3-oxoadipate CoA-transferase
Reaction: succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA
For diagram of benzoate metabolism, click here and for diagram of 4-nitrophenol metabolism, click here
Other name(s): 3-oxoadipate coenzyme A-transferase; 3-oxoadipate succinyl-CoA transferase
Systematic name: succinyl-CoA:3-oxoadipate CoA-transferase
Comments: The enzyme, often found in soil bacteria and fungi, is involved in the catabolism of a variety of aromatic compounds, including catechol and protocatechuate, which are degraded via 3-oxoadipate.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9026-16-8
References:
1.  Katagiri, M. and Hayaishi, O. Enzymatic degradation of β-ketoadipic acid. J. Biol. Chem. 226 (1957) 439–448. [PMID: 13428776]
2.  Kaschabek, S.R., Kuhn, B., Müller, D., Schmidt, E. and Reineke, W. Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: purification and characterization of 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase. J. Bacteriol. 184 (2002) 207–215. [DOI] [PMID: 11741862]
3.  Gobel, M., Kassel-Cati, K., Schmidt, E. and Reineke, W. Degradation of aromatics and chloroaromatics by Pseudomonas sp. strain B13: cloning, characterization, and analysis of sequences encoding 3-oxoadipate:succinyl-coenzyme A (CoA) transferase and 3-oxoadipyl-CoA thiolase. J. Bacteriol. 184 (2002) 216–223. [DOI] [PMID: 11741863]
[EC 2.8.3.6 created 1961]
 
 
EC 2.8.3.7      
Deleted entry: succinate—citramalate CoA-transferase. The activity has now been shown to be due to two separate enzymes described by EC 2.8.3.22, succinyl-CoA—L-malate CoA-transferase, and EC 2.8.3.20, succinyl-CoA—D-citramalate CoA-transferase
[EC 2.8.3.7 created 1972, deleted 2014]
 
 
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, EAWAG-BBD, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, 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, Gene, KEGG, MetaCyc, PDB, 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 2.8.3.10     
Accepted name: citrate CoA-transferase
Reaction: acetyl-CoA + citrate = acetate + (3S)-citryl-CoA
Systematic name: acetyl-CoA:citrate CoA-transferase
Comments: The enzyme is a component of EC 4.1.3.6 [citrate (pro-3S)-lyase]. Also catalyses the transfer of thioacyl carrier protein from its acetyl thioester to citrate.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 65187-14-6
References:
1.  Dimroth, P., Loyal, R. and Eggerer, H. Characterization of the isolated transferase subunit of citrate lyase as a CoA-transferase. Evidence against a covalent enzyme-substrate intermediate. Eur. J. Biochem. 80 (1977) 479–488. [DOI] [PMID: 336371]
[EC 2.8.3.10 created 1984]
 
 
EC 2.8.3.11     
Accepted name: citramalate CoA-transferase
Reaction: acetyl-CoA + citramalate = acetate + (3S)-citramalyl-CoA
Systematic name: acetyl-CoA:citramalate CoA-transferase
Comments: The enzyme is a component of EC 4.1.3.22 citramalate lyase. Also catalyses the transfer of thioacyl carrier protein from its acetyl thioester to citramalate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9033-60-7
References:
1.  Dimroth, P., Buckel, W., Loyal, R. and Eggerer, H. Isolation and function of the subunits of citramalate lyase and formation of hybrids with the subunits of citrate lyase. Eur. J. Biochem. 80 (1977) 469–477. [DOI] [PMID: 923590]
[EC 2.8.3.11 created 1984]
 
 
EC 2.8.3.12     
Accepted name: glutaconate CoA-transferase
Reaction: acetyl-CoA + (E)-glutaconate = acetate + glutaconyl-1-CoA
For diagram of reaction, click here
Systematic name: acetyl-CoA:(E)-glutaconate CoA-transferase
Comments: Glutarate, (R)-2-hydroxyglutarate, propenoate and propanoate, but not (Z)-glutaconate, can also act as acceptors.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 79078-99-2
References:
1.  Buckel, W.S., Dorn, U. and Semmler, R. Glutaconate CoA-transferase from Acidaminococcus fermentans. Eur. J. Biochem. 118 (1981) 315–321. [DOI] [PMID: 6945182]
[EC 2.8.3.12 created 1984, modified 2002]
 
 
EC 2.8.3.13     
Accepted name: succinate—hydroxymethylglutarate CoA-transferase
Reaction: succinyl-CoA + 3-hydroxy-3-methylglutarate = succinate + (S)-3-hydroxy-3-methylglutaryl-CoA
For diagram of mevalonate biosynthesis, click here
Other name(s): hydroxymethylglutarate coenzyme A-transferase; dicarboxyl-CoA:dicarboxylic acid coenzyme A transferase
Systematic name: succinyl-CoA:3-hydroxy-3-methylglutarate CoA-transferase
Comments: Malonyl-CoA can also act as donor, but more slowly.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 80237-90-7
References:
1.  Deana, R., Rigoni, F., Deana, A.D. and Galzigna, L. Submitochondrial localization and partial purification of the succinyl CoA: 3-hydroxy-3-methylglutarate coenzyme A transferase from rat liver. Biochim. Biophys. Acta 662 (1981) 119–124. [DOI] [PMID: 6946836]
[EC 2.8.3.13 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 2.8.3.15     
Accepted name: succinyl-CoA:(R)-benzylsuccinate CoA-transferase
Reaction: succinyl-CoA + (R)-2-benzylsuccinate = succinate + (R)-2-benzylsuccinyl-CoA
For diagram of anaerobic toluene catabolism, click here
Other name(s): benzylsuccinate CoA-transferase
Systematic name: succinyl-CoA:(R)-2-benzylsuccinate CoA-transferase
Comments: Involved in anaerobic catabolism of toluene and is a strictly toluene-induced enzyme that catalyses the reversible regio- and enantio-selective synthesis of (R)-2-benzylsuccinyl-CoA. The enzyme from Thauera aromatica is inactive when (R)-benzylsuccinate is replaced by (S)-benzylsuccinate.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, CAS registry number: 260966-56-1
References:
1.  Leutwein, C. and Heider, J. Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: an enzyme of the anaerobic toluene catabolic pathway in denitrifying bacteria. J. Bacteriol. 183 (2001) 4288–4295. [DOI] [PMID: 11418570]
2.  Leutwein, C. and Heider, J. Anaerobic toluene-catabolic pathway in denitrifying Thauera aromatica: activation and β-oxidation of the first intermediate, (R)-(+)-benzylsuccinate. Microbiology 145 (1999) 3265–3271. [DOI] [PMID: 10589736]
3.  Leuthner, B. and Heider, J. Anaerobic toluene catabolism of Thauera aromatica: the bbs operon codes for enzymes of β oxidation of the intermediate benzylsuccinate. J. Bacteriol. 182 (2000) 272–277. [DOI] [PMID: 10629170]
4.  Heider, J. A new familiy of CoA-transferases. FEBS Lett. 509 (2001) 345–349. [DOI] [PMID: 11749953]
[EC 2.8.3.15 created 2003]
 
 
EC 2.8.3.16     
Accepted name: formyl-CoA transferase
Reaction: formyl-CoA + oxalate = formate + oxalyl-CoA
Other name(s): formyl-coenzyme A transferase; formyl-CoA oxalate CoA-transferase
Systematic name: formyl-CoA:oxalate CoA-transferase
Comments: The enzyme from Oxalobacter formigenes can also catalyse the transfer of CoA from formyl-CoA to succinate.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 128826-27-7
References:
1.  Baetz, A.L. and Allison, M.J. Purification and characterization of formyl-coenzyme A transferase from Oxalobacter formigenes. J. Bacteriol. 172 (1990) 3537–3540. [DOI] [PMID: 2361939]
2.  Sidhu, H., Ogden, S.D., Lung, H.Y., Luttge, B.G., Baetz, A.L. and Peck, A.B. DNA sequencing and expression of the formyl coenzyme A transferase gene, frc, from Oxalobacter formigenes. J. Bacteriol. 179 (1997) 3378–3381. [DOI] [PMID: 9150242]
[EC 2.8.3.16 created 2003]
 
 
EC 2.8.3.17     
Accepted name: 3-(aryl)acryloyl-CoA:(R)-3-(aryl)lactate CoA-transferase
Reaction: (1) (E)-cinnamoyl-CoA + (R)-(phenyl)lactate = (E)-cinnamate + (R)-(phenyl)lactoyl-CoA
(2) (E)-4-coumaroyl-CoA + (R)-3-(4-hydroxyphenyl)lactate = 4-coumarate + (R)-3-(4-hydroxyphenyl)lactoyl-CoA
(3) 3-(indol-3-yl)acryloyl-CoA + (R)-3-(indol-3-yl)lactate = 3-(indol-3-yl)acrylate + (R)-3-(indol-3-yl)lactoyl-CoA
Other name(s): FldA; cinnamoyl-CoA:phenyllactate CoA-transferase
Systematic name: 3-(aryl)acryloyl-CoA:(R)-3-(aryl)lactate CoA-transferase
Comments: The enzyme, found in some amino acid-fermenting anaerobic bacteria, participates in the fermentation pathways of L-phenylalanine, L-tyrosine, and L-tryptophan. It forms a complex with EC 4.2.1.175, (R)-3-(aryl)lactoyl-CoA dehydratase.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, CAS registry number: 289682-21-9
References:
1.  Dickert, S., Pierik, A.J., Linder, D. and Buckel, W. The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes. Eur. J. Biochem. 267 (2000) 3874–3884. [DOI] [PMID: 10849007]
2.  Dodd, D., Spitzer, M.H., Van Treuren, W., Merrill, B.D., Hryckowian, A.J., Higginbottom, S.K., Le, A., Cowan, T.M., Nolan, G.P., Fischbach, M.A. and Sonnenburg, J.L. A gut bacterial pathway metabolizes aromatic amino acids into nine circulating metabolites. Nature 551 (2017) 648–652. [PMID: 29168502]
[EC 2.8.3.17 created 2003, modified 2019]
 
 
EC 2.8.3.18     
Accepted name: succinyl-CoA:acetate CoA-transferase
Reaction: succinyl-CoA + acetate = acetyl-CoA + succinate
Other name(s): aarC (gene name); SCACT
Systematic name: succinyl-CoA:acetate CoA-transferase
Comments: In some bacteria the enzyme catalyses the conversion of acetate to acetyl-CoA as part of a modified tricarboxylic acid (TCA) cycle [3,5,6]. In other organisms it converts acetyl-CoA to acetate during fermentation [1,2,4,7]. In some organisms the enzyme also catalyses the activity of EC 2.8.3.27, propanoyl-CoA:succinate CoA transferase.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
References:
1.  Steinbuchel, A. and Muller, M. Anaerobic pyruvate metabolism of Tritrichomonas foetus and Trichomonas vaginalis hydrogenosomes. Mol. Biochem. Parasitol. 20 (1986) 57–65. [DOI] [PMID: 3090435]
2.  Sohling, B. and Gottschalk, G. Molecular analysis of the anaerobic succinate degradation pathway in Clostridium kluyveri. J. Bacteriol. 178 (1996) 871–880. [DOI] [PMID: 8550525]
3.  Mullins, E.A., Francois, J.A. and Kappock, T.J. A specialized citric acid cycle requiring succinyl-coenzyme A (CoA):acetate CoA-transferase (AarC) confers acetic acid resistance on the acidophile Acetobacter aceti. J. Bacteriol. 190 (2008) 4933–4940. [DOI] [PMID: 18502856]
4.  van Grinsven, K.W., van Hellemond, J.J. and Tielens, A.G. Acetate:succinate CoA-transferase in the anaerobic mitochondria of Fasciola hepatica. Mol. Biochem. Parasitol. 164 (2009) 74–79. [DOI] [PMID: 19103231]
5.  Mullins, E.A. and Kappock, T.J. Crystal structures of Acetobacter aceti succinyl-coenzyme A (CoA):acetate CoA-transferase reveal specificity determinants and illustrate the mechanism used by class I CoA-transferases. Biochemistry 51 (2012) 8422–8434. [DOI] [PMID: 23030530]
6.  Kwong, W.K., Zheng, H. and Moran, N.A. Convergent evolution of a modified, acetate-driven TCA cycle in bacteria. Nat Microbiol 2:17067 (2017). [DOI] [PMID: 28452983]
7.  Zhang, B., Lingga, C., Bowman, C. and Hackmann, T.J. A new pathway for forming acetate and synthesizing ATP during fermentation in bacteria. Appl. Environ. Microbiol. 87 (2021) e0295920. [DOI] [PMID: 33931420]
[EC 2.8.3.18 created 2013, modified 2022]
 
 
EC 2.8.3.19     
Accepted name: CoA:oxalate CoA-transferase
Reaction: acetyl-CoA + oxalate = acetate + oxalyl-CoA
Other name(s): acetyl-coenzyme A transferase; acetyl-CoA oxalate CoA-transferase; ACOCT; YfdE; UctC
Systematic name: acetyl-CoA:oxalate CoA-transferase
Comments: The enzymes characterized from the bacteria Escherichia coli and Acetobacter aceti can also use formyl-CoA and oxalate (EC 2.8.3.16, formyl-CoA transferase) or formyl-CoA and acetate, with significantly reduced specific activities.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB
References:
1.  Mullins, E.A., Sullivan, K.L. and Kappock, T.J. Function and X-Ray crystal structure of Escherichia coli YfdE. PLoS One 8 (2013) e67901. [DOI] [PMID: 23935849]
[EC 2.8.3.19 created 2013]
 
 
EC 2.8.3.20     
Accepted name: succinyl-CoA—D-citramalate CoA-transferase
Reaction: (1) succinyl-CoA + (R)-citramalate = succinate + (R)-citramalyl-CoA
(2) succinyl-CoA + (R)-malate = succinate + (R)-malyl-CoA
Glossary: (R)-citramalate = (2R)-2-hydroxy-2-methylbutanedioate
(R)-malate = (2R)-2-hydroxybutanedioate
(R)-malyl-CoA = (3R)-3-carboxy-3-hydroxypropanoyl-CoA
Other name(s): Sct
Systematic name: succinyl-CoA:(R)-citramalate CoA-transferase
Comments: The enzyme, purified from the bacterium Clostridium tetanomorphum, can also accept itaconate as acceptor, with lower efficiency.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Friedmann, S., Alber, B.E. and Fuchs, G. Properties of succinyl-coenzyme A:D-citramalate coenzyme A transferase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. J. Bacteriol. 188 (2006) 6460–6468. [DOI] [PMID: 16952935]
[EC 2.8.3.20 created 2014]
 
 
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, Gene, KEGG, MetaCyc, PDB
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 2.8.3.22     
Accepted name: succinyl-CoA—L-malate CoA-transferase
Reaction: (1) succinyl-CoA + (S)-malate = succinate + (S)-malyl-CoA
(2) succinyl-CoA + (S)-citramalate = succinate + (S)-citramalyl-CoA
For diagram of the 3-hydroxypropanoate cycle, click here
Glossary: (S)-citramalate = (2S)-2-hydroxy-2-methylbutanedioate
(S)-malate = (2S)-2-hydroxybutanedioate
(S)-malyl-CoA = (3S)-3-carboxy-3-hydroxypropanoyl-CoA
Other name(s): SmtAB
Systematic name: succinyl-CoA:(S)-malate CoA-transferase
Comments: The enzyme, purified from the bacterium Chloroflexus aurantiacus, can also accept itaconate as acceptor, with lower efficiency. It is part of the 3-hydroxypropanoate cycle for carbon assimilation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Friedmann, S., Steindorf, A., Alber, B.E. and Fuchs, G. Properties of succinyl-coenzyme A:L-malate coenzyme A transferase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus. J. Bacteriol. 188 (2006) 2646–2655. [DOI] [PMID: 16547052]
[EC 2.8.3.22 created 2014]
 
 
EC 2.8.3.23     
Accepted name: caffeate CoA-transferase
Reaction: 3-(3,4-dihydroxyphenyl)propanoyl-CoA + (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate = 3-(3,4-dihydroxyphenyl)propanoate + (2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl-CoA
Glossary: 3-(3,4-dihydroxyphenyl)propanoate = hydrocaffeate
(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate = (2E)-3-(3,4-dihydroxyphenyl)acrylate = trans-caffeate
Other name(s): CarA
Systematic name: 3-(3,4-dihydroxyphenyl)propanoyl-CoA:(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoate CoA-transferase
Comments: The enzyme, isolated from the bacterium Acetobacterium woodii, catalyses an energy-saving CoA loop for caffeate activation. In addition to caffeate, the enzyme can utilize 4-coumarate or ferulate as CoA acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Hess, V., Gonzalez, J.M., Parthasarathy, A., Buckel, W. and Muller, V. Caffeate respiration in the acetogenic bacterium Acetobacterium woodii: a coenzyme A loop saves energy for caffeate activation. Appl. Environ. Microbiol. 79 (2013) 1942–1947. [DOI] [PMID: 23315745]
[EC 2.8.3.23 created 2015]
 
 
EC 2.8.3.24     
Accepted name: (R)-2-hydroxy-4-methylpentanoate CoA-transferase
Reaction: 4-methylpentanoyl-CoA + (R)-2-hydroxy-4-methylpentanoate = 4-methylpentanoate + (R)-2-hydroxy-4-methylpentanoyl-CoA
Glossary: 4-methylpentanoate = isocaproate
Other name(s): hadA (gene name)
Systematic name: 4-methylpentanoyl-CoA:(R)-2-hydroxy-4-methylpentanoate CoA-transferase
Comments: The enzyme, characterized from the bacterium Peptoclostridium difficile, participates in an L-leucine fermentation pathway. The reaction proceeds via formation of a covalent anhydride intermediate between a conserved aspartate residue and the acyl group of the CoA thioester substrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Kim, J., Darley, D., Selmer, T. and Buckel, W. Characterization of (R)-2-hydroxyisocaproate dehydrogenase and a family III coenzyme A transferase involved in reduction of L-leucine to isocaproate by Clostridium difficile. Appl. Environ. Microbiol. 72 (2006) 6062–6069. [DOI] [PMID: 16957230]
[EC 2.8.3.24 created 2016]
 
 
EC 2.8.3.25     
Accepted name: bile acid CoA-transferase
Reaction: (1) lithocholoyl-CoA + cholate = lithocholate + choloyl-CoA
(2) deoxycholoyl-CoA + cholate = deoxycholate + choloyl-CoA
Other name(s): baiF (gene name); baiK (gene name); bile acid coenzyme A transferase
Systematic name: lithocholoyl-CoA:cholate CoA-transferase
Comments: The enzyme, characterized from the gut bacterium Clostridium scindens, catalyses the last step in bile acid 7α-dehydroxylation, the removal of the CoA moiety from the products. By using a transferase rather than hydrolase, the bacteria conserve the thioester bond energy, saving ATP molecules. Clostridium scindens possesses two forms of the enzyme, encoded by the baiF and baiK genes. While the enzymes have a broad acceptor specificity and can use allocholate, ursodeoxycholate, and β-muricholate, the donor specificity is more strict. BaiF acts on lithocholoyl-CoA and deoxycholoyl-CoA, and BaiK acts only on the latter.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc
References:
1.  Ridlon, J.M. and Hylemon, P.B. Identification and characterization of two bile acid coenzyme A transferases from Clostridium scindens, a bile acid 7α-dehydroxylating intestinal bacterium. J. Lipid Res. 53 (2012) 66–76. [DOI] [PMID: 22021638]
[EC 2.8.3.25 created 2005 as EC 3.1.2.26, transferred 2016 to EC 2.8.3.25]
 
 
EC 2.8.3.26     
Accepted name: succinyl-CoA:mesaconate CoA transferase
Reaction: succinyl-CoA + mesaconate = 2-methylfumaryl-CoA + succinate
Glossary: 2-methylfumaryl-CoA = (E)-3-carboxy-2-methylprop-2-enoyl-CoA
mesaconate = 2-methylbut-2-enedioic acid
Other name(s): mct (gene name)
Systematic name: succinyl-CoA:mesaconate CoA transferase
Comments: The enzyme participates in the methylaspartate cycle, an anaplerotic pathway that operates in some members of the haloarchaea and forms malate from acetyl-CoA.
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc
References:
1.  Khomyakova, M., Bukmez, O., Thomas, L.K., Erb, T.J. and Berg, I.A. A methylaspartate cycle in haloarchaea. Science 331 (2011) 334–337. [PMID: 21252347]
2.  Borjian, F., Johnsen, U., Schonheit, P. and Berg, I.A. Succinyl-CoA:mesaconate CoA-transferase and mesaconyl-CoA hydratase, enzymes of the methylaspartate cycle in Haloarcula hispanica. Front. Microbiol. 8:1683 (2017). [PMID: 28932214]
[EC 2.8.3.26 created 2020]
 
 
EC 2.8.3.27     
Accepted name: propanoyl-CoA:succinate CoA transferase
Reaction: propanoyl-CoA + succinate = propanoate + succinyl-CoA
Other name(s): succinyl-CoA:propionate CoA-transferase; propionyl-CoA:succinyl-CoA transferase; ASCT; scpC (gene name)
Systematic name: propanoyl-CoA:succinate CoA transferase
Comments: The enzyme is most specific in Escherichia coli, where the preferred substrates are propanoyl-CoA and succinate. In other organisms, the enzyme uses acetyl-CoA at the same rate as propanoyl-CoA (cf. EC 2.8.3.18, succinyl-CoA:acetate CoA-transferase).
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc
References:
1.  Allen, S. H., Kellermeyer, R. W., Stjernholm, R. L., and Wood, H. G. Purification and properties of enzymes involved in the propionic acid fermentation. J. Bacteriol. 87 (1964) 171–187. [DOI] [PMID: 14102852]
2.  Schulz, T.KF. and Kluytmans, J.H. Pathway of propionate synthesis in the sea mussel Mytilus edulis L. Comp. Biochem. Physiol. B. Comp. Biochem. 75 (1983) 365–372. [DOI]
3.  Haller, T., Buckel, T., Retey, J. and Gerlt, J.A. Discovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli. Biochemistry 39 (2000) 4622–4629. [DOI] [PMID: 10769117]
4.  van Grinsven, K.W., van Hellemond, J.J. and Tielens, A.G. Acetate:succinate CoA-transferase in the anaerobic mitochondria of Fasciola hepatica. Mol. Biochem. Parasitol. 164 (2009) 74–79. [DOI] [PMID: 19103231]
5.  Zhang, B., Lingga, C., Bowman, C. and Hackmann, T.J. A new pathway for forming acetate and synthesizing ATP during fermentation in bacteria. Appl. Environ. Microbiol. 87 (2021) e0295920. [DOI] [PMID: 33931420]
[EC 2.8.3.27 created 2022]
 
 
EC 2.8.3.28     
Accepted name: phenylsuccinyl-CoA transferase
Reaction: (1) phenylsuccinate + succinyl-CoA = 2-phenylsuccinyl-CoA + succinate
(2) phenylsuccinate + succinyl-CoA = 3-phenylsuccinyl-CoA + succinate
Other name(s): iaaL (gene name)
Systematic name: succinyl-CoA:2/3-phenylsuccinate CoA-transferase
Comments: The enzyme, characterized from the bacterium Aromatoleum aromaticum, is involved in degradation of (indol-3-yl)acetate, where it is believed to function on (2-aminophenyl)succinate. It has a broad substrate specificity towards other C4-dicarboxylic acids, phenylacetate, and the non-physiological compound 2-naphthylacetate. The enzyme produces 2- and 3-phenylsuccinyl-CoA in equimolar amounts. It can also perform an intramolecular transfer of the CoA moiety to convert 2-phenylsuccinyl-CoA to 3-phenylsuccinyl-CoA.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Schuhle, K., Nies, J. and Heider, J. An indoleacetate-CoA ligase and a phenylsuccinyl-CoA transferase involved in anaerobic metabolism of auxin. Environ. Microbiol. 18 (2016) 3120–3132. [DOI] [PMID: 27102732]
[EC 2.8.3.28 created 2022]
 
 


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