Continued from EC 2.8.1 and EC 2.8.2
EC 2.8.3 CoA-transferases
EC 2.8.4 Transferring alkylthio groups
EC 2.9.1 Selenotransferases
EC 2.10.1 Molybdenumtransferases or tungstentransferases with sulfide groups as acceptors
Accepted name: propionate CoA-transferase
Reaction: acetyl-CoA + propanoate = acetate + propanoyl-CoA
Other names: 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, 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 only.
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.
Accepted name: malonate CoA-transferase
Reaction: acetyl-CoA + malonate = acetate + malonyl-CoA
Other names: 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.
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 2.8.3.4 Deleted entry: butyrate CoA-transferase (EC 2.8.3.4 created 1961, deleted 1964)]
Accepted name: 3-oxoacid CoA-transferase
Reaction: succinyl-CoA + a 3-oxo acid = succinate + a 3-oxoacyl-CoA
Other names: 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, 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.
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.
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.
Accepted name: 3-oxoadipate CoA-transferase
Reaction: succinyl-CoA + 3-oxoadipate = succinate + 3-oxoadipyl-CoA
For diagram click here or click here.
Other names: 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, 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.
2. Kaschabek, S.R., Kuhn, B., MŸller, 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) 207Ð215. [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) 216Ð223. [PMID: 11741863]
[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 2013)]
Accepted name: acetate CoA-transferase
Reaction: acyl-CoA + acetate = a fatty acid anion + acetyl-CoA
Other names: acetate coenzyme A-transferase; butyryl CoA:acetate CoA transferase; butyryl coenzyme A transferase
Systematic name: acyl-CoA:acetate CoA-transferase
Comments: Acts on butanoyl-CoA and pentanoyl-CoA.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, 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. [PMID: 4884054]
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. [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. [PMID: 11741863]
Accepted name: butyrate—acetoacetate CoA-transferase
Reaction: butanoyl-CoA + acetoacetate = butanoate + acetoacetyl-CoA
Other names: 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]
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, 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. [PMID: 336371]
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. [PMID: 923590]
Accepted name: glutaconate CoA-transferase
Reaction: acetyl-CoA + (E)-glutaconate = acetate + glutaconyl-1-CoA
For reaction pathway 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, 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. [PMID: 6945182]
Accepted name: succinate—hydroxymethylglutarate CoA-transferase
Reaction: succinyl-CoA + 3-hydroxy-3-methylglutarate = succinate + (S)-3-hydroxy-3-methylglutaryl-CoA
Systematic name: succinyl-CoA:3-hydroxy-3-methylglutarate CoA-transferase
Other names: hydroxymethylglutarate coenzyme A-transferase; dicarboxyl-CoA:dicarboxylic acid coenzyme A transferase
Comments: Malonyl-CoA can also act as donor, but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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. [PMID: 6946836]
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]
Accepted name: succinyl-CoA:(R)-benzylsuccinate CoA-transferase
Reaction: succinyl-CoA + (R)-2-benzylsuccinate = succinate + (R)-2-benzylsuccinyl-CoA
For diagram 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. [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. [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. [PMID: 10629170]
4. Heider, J. A new familiy of CoA-transferases. FEBS Lett. 509 (2001) 345-349. [PMID: 11749953]
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, KEGG, Metacyc, 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. [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. [PMID: 9150242]
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, 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. [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]
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, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Steinbuchel, A. and Muller, M. Anaerobic pyruvate metabolism of Tritrichomonas foetus and Trichomonas vaginalis hydrogenosomes. Mol. Biochem. Parasitol. 20 (1986) 57-65. [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. [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. [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. [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. [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 (2017) 17067. [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. [PMID: 33931420]
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, KEGG, Metacyc, PDB, CAS registry number:
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. [PMID: 23935849]
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, CAS registry number:
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. [PMID: 16952935]
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, PDB, CAS registry number:
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. [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. [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. [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. [PMID: 15823031]
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 reaction 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, CAS registry number:
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. [PMID: 16547052]
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, CAS registry number:
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. [PMID: 23315745]
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: (R)-2-hydroxy-4-methylpentanoate = D-leucate
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, CAS registry number:
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. [PMID: 16957230]
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. The enzyme has a broad substrate specificity and can use multiple acceptors, including allocholate, ursodeoxycholate, and β-muricholate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
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. [PMID: 22021638]
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, KEGG, MetaCyc, CAS registry number:
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 (2017) 1683. [PMID: 28932214]
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, KEGG, MetaCyc, CAS registry number:
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. [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.
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. [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. [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. [PMID: 33931420]
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, CAS registry number:
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. [PMID: 27102732]
Contents
EC 2.8.4.1 coenzyme-B sulfoethylthiotransferase
EC 2.8.4.2 arsenate-mycothiol transferase
EC 2.8.4.3 tRNA-2-methylthio-N6-dimethylallyladenosine synthase
EC 2.8.4.4 [ribosomal protein uS12] (aspartate89-C3)-methylthiotransferase
EC 2.8.4.5 tRNA (N6-L-threonylcarbamoyladenosine37-C2)-methylthiotransferase
EC 2.8.4.6 S-methyl-1-thioxylulose 5-phosphate methylthiotransferase
Accepted name: coenzyme-B sulfoethylthiotransferase
Reaction: methyl-CoM + CoB = CoM-S-S-CoB + methane
For diagram of reaction click here
Glossary: coenzyme B = CoB = N-(7-mercaptoheptanoyl)threonine 3-O-phosphate = N-(7-thioheptanoyl)-3-O-phosphothreonine
coenzyme M = CoM = 2-sulfanylethane-1-sulfonate = 2-mercaptoethanesulfonate (deprecated)
2-(methylsulfanyl)ethanesulfonate = methyl-CoM
Other name(s): methyl-CoM reductase; methyl coenzyme M reductase
Systematic name: methyl-CoM:CoB S-(2-sulfoethyl)thiotransferase
Comments: This enzyme catalyses the final step in methanogenesis, the biological production of methane. This important anaerobic process is carried out only by methanogenic archaea. The enzyme can also function in reverse, for anaerobic oxidation of methane. The enzyme requires the hydroporphinoid nickel complex coenzyme F430. Highly specific for coenzyme B with a heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor substrates. The sulfide sulfur can be replaced by selenium but not by oxygen.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Bobik, T.A., Olson, K.D., Noll, K.M. and Wolfe, R.S. Evidence that the heterodisulfide of coenzyme-M and 7-mercaptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium. Biochem. Biophys. Res. Commun. 149 (1987) 455-460. [PMID: 3122735]
2. Ellermann, J., Hedderich, R., Boecher, R. and Thauer, R.K. The final step in methane formation: investigations with highly purified methyl coenzyme M reductase component C from Methanobacterium thermoautotrophicum (strain Marburg). Eur. J. Biochem. 184 (1988) 63-68.
3. Ermler, U., Grabarse, W., Shima, S., Goubeaud, M. and Thauer, R.K. Crystal structure of methyl coenzyme M reductase: The key enzyme of biological methane formation. Science 278 (1997) 1457-1462. [PMID: 9367957]
4. Signor, L., Knuppe, C., Hug, R., Schweizer, B., Pfaltz, A. and Jaun, B. Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate — a process mimicking methanogenesis in Archaea. Chemistry 6 (2000) 3508-3516. [PMID: 11072815]
5. Scheller, S., Goenrich, M., Boecher, R., Thauer, R.K. and Jaun, B. The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane. Nature 465 (2010) 606-608. [PMID: 20520712]
Accepted name: arsenate-mycothiol transferase
Reaction: arsenate + mycothiol = arseno-mycothiol + H2O
Glossary: mycothiol = 1-O-[2-(N2-acetyl-L-cysteinamido)-2-deoxy--D-glucopyranosyl]-1D-myo-inositol
Other name(s): ArsC1; ArsC2; mycothiol:arsenate transferase
Systematic name: mycothiol:arsenate S-arsenotransferase
Comments: Reduction of arsenate is part of a defence mechanism of the cell against toxic arsenate. The product arseno-mycothiol is reduced by EC 1.20.4.3 (mycoredoxin) to arsenite and mycothiol-mycoredoxin disulfide. Finally, a second mycothiol recycles mycoredoxin and forms mycothione.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Ordonez, E., Van Belle, K., Roos, G., De Galan, S., Letek, M., Gil, J.A., Wyns, L., Mateos, L.M. and Messens, J. Arsenate reductase, mycothiol, and mycoredoxin concert thiol/disulfide exchange. J. Biol. Chem. 284 (2009) 15107-15116. [PMID: 19286650]
Accepted name: tRNA-2-methylthio-N6-dimethylallyladenosine synthase
Reaction: N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-(methylsulfanyl)-N6-dimethylallyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor (overall reaction)
(1a) N6-dimethylallyladenine37 in tRNA + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced electron acceptor = 2-thio-N6-dimethylallyladenine37 in tRNA + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor
(1b) S-adenosyl-L-methionine + 2-thio-N6-dimethylallyladenine37 in tRNA = S-adenosyl-L-homocysteine + 2-(methylsulfanyl)-N6-dimethylallyladenine37 in tRNA
For diagram of reaction click here.
Other name(s): MiaB; 2-methylthio-N-6-isopentenyl adenosine synthase; tRNA-i6A37 methylthiotransferase; tRNA (N6-dimethylallyladenosine37):sulfur-(sulfur carrier),S-adenosyl-L-methionine C2-methylthiotransferase
Systematic name: tRNA (N6-dimethylallyladenosine37):sulfur-(sulfur carrier),S-adenosyl-L-methionine C2-(methylsulfanyl)transferase
Comments: This bacterial enzyme binds two [4Fe-4S] clusters as well as the transferred sulfur [3]. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover. The identity of the electron donor is not known.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Pierrel, F., Bjork, G.R., Fontecave, M. and Atta, M. Enzymatic modification of tRNAs: MiaB is an iron-sulfur protein. J. Biol. Chem. 277 (2002) 13367-13370. [PMID: 11882645]
2. Pierrel, F., Hernandez, H.L., Johnson, M.K., Fontecave, M. and Atta, M. MiaB protein from Thermotoga maritima. Characterization of an extremely thermophilic tRNA-methylthiotransferase. J. Biol. Chem. 278 (2003) 29515-29524. [PMID: 12766153]
3. Pierrel, F., Douki, T., Fontecave, M. and Atta, M. MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA. J. Biol. Chem. 279 (2004) 47555-47563. [PMID: 15339930]
4. Hernandez, H.L., Pierrel, F., Elleingand, E., Garcia-Serres, R., Huynh, B.H., Johnson, M.K., Fontecave, M. and Atta, M. MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters. Biochemistry 46 (2007) 5140-5147. [PMID: 17407324]
5. Landgraf, B.J., Arcinas, A.J., Lee, K.H. and Booker, S.J. Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB. J. Am. Chem. Soc. 135 (2013) 15404-15416. [PMID: 23991893]
Accepted name: [ribosomal protein uS12] (aspartate89-C3)-methylthiotransferase
Reaction: L-aspartate89-[ribosomal protein uS12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced acceptor = 3-(methylsulfanyl)-L-aspartate89-[ribosomal protein uS12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor (overall reaction)
(1a) S-adenosyl-L-methionine + L-aspartate89-[ribosomal protein uS12] + sulfur-(sulfur carrier) = S-adenosyl-L-homocysteine + L-aspartate89-[ribosomal protein uS12]-methanethiol + (sulfur carrier)
(1b) L-aspartate89-[ribosomal protein uS12]-methanethiol + S-adenosyl-L-methionine + reduced acceptor = 3-(methylsulfanyl)-L-aspartate89-[ribosomal protein uS12] + L-methionine + 5'-deoxyadenosine + oxidized acceptor
Other name(s): RimO; [ribosomal protein S12]-Asp89:sulfur-(sulfur carrier),S-adenosyl-L-methionine C3-methylthiotransferase; [ribosomal protein S12]-L-aspartate89:sulfur-(sulfur carrier),S-adenosyl-L-methionine C3-methylthiotransferase
Systematic name: [ribosomal protein uS12]-L-aspartate89:sulfur-(sulfur carrier),S-adenosyl-L-methionine C3-(methylsulfanyl)transferase
Comments: This bacterial enzyme binds two [4Fe-4S] clusters [2,3]. A bridge of five sulfur atoms is formed between the free Fe atoms of the two [4Fe-4S] clusters [6]. In the first reaction the enzyme transfers a methyl group from AdoMet to the external sulfur ion of the sulfur bridge. In the second reaction the enzyme catalyses the reductive fragmentation of a second molecule of AdoMet, yielding a 5'-deoxyadenosine radical, which then attacks the methylated sulfur atom of the polysulfide bridge, resulting in the transfer of a methylsulfanyl group to aspartate89 [5,6]. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Anton, B.P., Saleh, L., Benner, J.S., Raleigh, E.A., Kasif, S. and Roberts, R.J. RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli. Proc. Natl. Acad. Sci. USA 105 (2008) 1826-1831. [PMID: 18252828]
2. Lee, K.H., Saleh, L., Anton, B.P., Madinger, C.L., Benner, J.S., Iwig, D.F., Roberts, R.J., Krebs, C. and Booker, S.J. Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily. Biochemistry 48 (2009) 10162-10174. [PMID: 19736993]
3. Arragain, S., Garcia-Serres, R., Blondin, G., Douki, T., Clemancey, M., Latour, J.M., Forouhar, F., Neely, H., Montelione, G.T., Hunt, J.F., Mulliez, E., Fontecave, M. and Atta, M. Post-translational modification of ribosomal proteins: structural and functional characterization of RimO from Thermotoga maritima, a radical S-adenosylmethionine methylthiotransferase. J. Biol. Chem. 285 (2010) 5792-5801. [PMID: 20007320]
4. Strader, M.B., Costantino, N., Elkins, C.A., Chen, C.Y., Patel, I., Makusky, A.J., Choy, J.S., Court, D.L., Markey, S.P. and Kowalak, J.A. A proteomic and transcriptomic approach reveals new insight into β-methylthiolation of Escherichia coli ribosomal protein S12. Mol. Cell. Proteomics 10 (2011) M110.005199. [PMID: 21169565]
5. Landgraf, B.J., Arcinas, A.J., Lee, K.H. and Booker, S.J. Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB. J. Am. Chem. Soc. 135 (2013) 15404-15416. [PMID: 23991893]
6. Forouhar, F., Arragain, S., Atta, M., Gambarelli, S., Mouesca, J.M., Hussain, M., Xiao, R., Kieffer-Jaquinod, S., Seetharaman, J., Acton, T.B., Montelione, G.T., Mulliez, E., Hunt, J.F. and Fontecave, M. Two Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferases. Nat. Chem. Biol. 9 (2013) 333-338. [PMID: 23542644]
Accepted name: tRNA (N6-L-threonylcarbamoyladenosine37-C2)-methylthiotransferase
Reaction: N6-L-threonylcarbamoyladenine37 in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-(methylsulfanyl)-N6-L-threonylcarbamoyladenine37 in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor (overall reaction)
(1a) N6-L-threonylcarbamoyladenine37 in tRNA + sulfur-(sulfur carrier) + S-adenosyl-L-methionine + reduced electron acceptor = 2-thio-N6-L-threonylcarbamoyladenine37 in tRNA + (sulfur carrier) + L-methionine + 5-deoxyadenosine + electron acceptor
(1b) S-adenosyl-L-methionine + 2-thio-N6-L-threonylcarbamoyladenine37 in tRNA = S-adenosyl-L-homocysteine + 2-(methylsulfanyl)-N6-L-threonylcarbamoyladenine37 in tRNA
For diagram of reaction click here.
Glossary: N6-L-threonylcarbamoyladenine37 = t6A37
2-thio-N6-L-threonylcarbamoyladenine37 = ms2t6A37
Other name(s): MtaB; methylthio-threonylcarbamoyl-adenosine transferase B; CDKAL1 (gene name); tRNA (N6-L-threonylcarbamoyladenosine37):sulfur-(sulfur carrier),S-adenosyl-L-methionine C2-methylthiotransferase
Systematic name: tRNA (N6-L-threonylcarbamoyladenosine37):sulfur-(sulfur carrier),S-adenosyl-L-methionine C2-(methylsulfanyl)transferase
Comments: The enzyme, which is a member of the S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes superfamily, binds two [4Fe-4S] clusters as well as the transferred sulfur. The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover. The identity of the electron donor is not known.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Arragain, S., Handelman, S.K., Forouhar, F., Wei, F.Y., Tomizawa, K., Hunt, J.F., Douki, T., Fontecave, M., Mulliez, E. and Atta, M. Identification of eukaryotic and prokaryotic methylthiotransferase for biosynthesis of 2-methylthio-N6-threonylcarbamoyladenosine in tRNA. J. Biol. Chem. 285 (2010) 28425-28433. [PMID: 20584901]
Accepted name: S-methyl-1-thioxylulose 5-phosphate methylthiotransferase
Reaction: S-methyl-1-thio-D-xylulose 5-phosphate + glutathione = 1-deoxy-D-xylulose 5-phosphate + S-(methylsulfanyl)glutathione
Other name(s): 1-methylthioxylulose 5-phosphate sulfurylase (incorrect)
Systematic name: S-methyl-1-thio-D-xylulose 5-phosphate:glutathione methylthiotransferase
Comments: The enzyme, characterized from the bacterium Rhodospirillum rubrum, belongs to the cupin superfamily and contains a manganese ion. It participates in an anaerobic salvage pathway that restores methionine from S-methyl-5'-thioadenosine. The enzyme was assayed in vitro using L-dithiothreitol instead of glutathione.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Erb, T.J., Evans, B.S., Cho, K., Warlick, B.P., Sriram, J., Wood, B.M., Imker, H.J., Sweedler, J.V., Tabita, F.R. and Gerlt, J.A. A RubisCO-like protein links SAM metabolism with isoprenoid biosynthesis. Nat. Chem. Biol. 8 (2012) 926-932. [PMID: 23042035]
2. Warlick, B.P., Evans, B.S., Erb, T.J., Ramagopal, U.A., Sriram, J., Imker, H.J., Sauder, J.M., Bonanno, J.B., Burley, S.K., Tabita, F.R., Almo, S.C., Sweedler, J.S. and Gerlt, J.A. 1-methylthio-D-xylulose 5-phosphate methylsulfurylase: a novel route to 1-deoxy-D-xylulose 5-phosphate in Rhodospirillum rubrum, Biochemistry 51 (2012) 8324-8326. [PMID: 23035785]
3. Cho, K., Evans, B.S., Wood, B.M., Kumar, R., Erb, T.J., Warlick, B.P., Gerlt, J.A. and Sweedler, J.V. Integration of untargeted metabolomics with transcriptomics reveals active metabolic pathways. Metabolomics 2014 (2014) . [PMID: 25705145]
Contents
EC 2.8.5.1 S-sulfo-L-cysteine synthase (3-phospho-L-serine-dependent)
EC 2.8.5.2 L-cysteine S-thiosulfotransferase
Accepted name: S-sulfo-L-cysteine synthase (3-phospho-L-serine-dependent)
Reaction: O-phospho-L-serine + thiosulfate = S-sulfo-L-cysteine + phosphate
Other name(s): cysK2 (gene name); thiosulfate:3-phospho-L-serine thiosulfotransferase
Systematic name: thiosulfate:3-phospho-L-serine thiosulfonotransferase
Comments: The enzyme, which has been characterized from the bacterium Mycobacterium tuberculosis, has no activity with O-acetyl-L-serine. Requires pyridoxal 5'-phosphate. cf. EC 2.5.1.144, S-sulfo-L-cysteine synthase (O-acetyl-L-serine-dependent).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Steiner, E.M., Both, D., Lossl, P., Vilaplana, F., Schnell, R. and Schneider, G. CysK2 from Mycobacterium tuberculosis is an O-phospho-L-serine-dependent S-sulfocysteine synthase. J. Bacteriol. 196 (2014) 3410-3420. [PMID: 25022854]
Accepted name: L-cysteine S-thiosulfotransferase
Reaction: (1) [SoxY protein]-L-cysteine + thiosulfate + 2 ferricytochrome c = [SoxY protein]-S-sulfosulfanyl-L-cysteine + 2 ferrocytochrome c + 2H+
(2) [SoxY protein]-S-sulfanyl-L-cysteine + thiosulfate + 2 ferricytochrome c = [SoxY protein]-S-(2-sulfodisulfanyl)-L-cysteine + 2 ferrocytochrome c + 2H+
Other name(s): SoxXA
Systematic name: thiosulfate:[SoxY protein]-L-cysteine thiosufotransferase
Comments: The enzyme is part of the Sox enzyme system, which participates in a bacterial thiosulfate oxidation pathway that produces sulfate. It catalyses two reactions in the pathway - early in the pathway it attaches a thiosulfate molecule to the sulfur atom of an L-cysteine of a SoxY protein; later it transfers a second thiosulfate molecule to a sulfane group that is already attached to the same cysteine residue.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Friedrich, C.G., Quentmeier, A., Bardischewsky, F., Rother, D., Kraft, R., Kostka, S. and Prinz, H. Novel genes coding for lithotrophic sulfur oxidation of Paracoccus pantotrophus GB17. J. Bacteriol. 182 (2000) 4677-4687. [PMID: 10940005]
2. Cheesman, M.R., Little, P.J. and Berks, B.C. Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum. Biochemistry 40 (2001) 10562-10569. [PMID: 11523998]
3. Rother, D. and Friedrich, C.G. The cytochrome complex SoxXA of Paracoccus pantotrophus is produced in Escherichia coli and functional in the reconstituted sulfur-oxidizing enzyme system. Biochim. Biophys. Acta 1598 (2002) 65-73. [PMID: 12147345]
4. Bamford, V.A., Bruno, S., Rasmussen, T., Appia-Ayme, C., Cheesman, M.R., Berks, B.C. and Hemmings, A.M. Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme. EMBO J. 21 (2002) 5599-5610. [PMID: 12411478]
5. Dambe, T., Quentmeier, A., Rother, D., Friedrich, C. and Scheidig, A.J. Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a heme enzyme initiating chemotrophic sulfur oxidation. J. Struct. Biol. 152 (2005) 229-234. [PMID: 16297640]
6. Hensen, D., Sperling, D., Truper, H.G., Brune, D.C. and Dahl, C. Thiosulphate oxidation in the phototrophic sulphur bacterium Allochromatium vinosum. Mol. Microbiol. 62 (2006) 794-810. [PMID: 16995898]
7. Grabarczyk, D.B. and Berks, B.C. Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ. PLoS One 12 (2017) e0173395. [PMID: 28257465]
Accepted name: L-seryl-tRNASec selenium transferase
Reaction: L-seryl-tRNASec + selenophosphate = L-selenocysteinyl-tRNASec + phosphate
Other name(s): L-selenocysteinyl-tRNASel synthase; L-selenocysteinyl-tRNASec synthase selenocysteine synthase; cysteinyl-tRNASec-selenium transferase; cysteinyl-tRNASec-selenium transferase
Systematic name: selenophosphate:L-seryl-tRNASec selenium transferase
Comments: a pyridoxal 5'-phosphate enzyme identified in Escherichia coli. Recognises specifically tRNASec-species. Binding of tRNASec also occurs in the absence of the seryl group. 2-Aminoacryloyl-tRNA, bound to the enzyme as an imine with the pyridoxal phosphate, is an intermediate in the reaction. Since the selenium atom replaces oxygen in serine, the product may also be referred to as L-selenoseryl-tRNASec. The symbol Sel has also been used for selenocysteine but Sec is preferred.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number: 183869-06-9
References:
1. Forchhammer, K., Böck, A. Selenocysteine from Escherichia coli. Analysis of the reaction sequence. J. Biol. Chem. 266 (1991) 6324-6328. [PMID: 2007585]
Accepted name: O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase
Reaction: O-phospho-L-seryl-tRNASec + selenophosphate + H2O = L-selenocysteinyl-tRNASec + 2 phosphate
Other name(s): MMPSepSecS; SepSecS; SLA/LP; O-phosphoseryl-tRNA:selenocysteinyl-tRNA synthase; O-phospho-L-seryl-tRNA:L-selenocysteinyl-tRNA synthase
Systematic name: selenophosphate:O-phospho-L-seryl-tRNASec selenium transferase
Comments: A pyridoxal-phosphate protein [4]. In archaea and eukarya selenocysteine formation is achieved by a two-step process: EC 2.7.1.164 (O-phosphoseryl-tRNASec kinase) phosphorylates the endogenous L-seryl-tRNASec to O-phospho-L-seryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number:
References:
1. Palioura, S., Sherrer, R.L., Steitz, T.A., Soll, D. and Simonovic, M. The human SepSecS-tRNASec complex reveals the mechanism of selenocysteine formation. Science 325 (2009) 321-325. [PMID: 19608919]
2. Araiso, Y., Palioura, S., Ishitani, R., Sherrer, R.L., O'Donoghue, P., Yuan, J., Oshikane, H., Domae, N., Defranco, J., Soll, D. and Nureki, O. Structural insights into RNA-dependent eukaryal and archaeal selenocysteine formation. Nucleic Acids Res. 36 (2008) 1187-1199. [PMID: 18158303]
3. Aeby, E., Palioura, S., Pusnik, M., Marazzi, J., Lieberman, A., Ullu, E., Soll, D. and Schneider, A. The canonical pathway for selenocysteine insertion is dispensable in Trypanosomes. Proc. Natl. Acad. Sci. USA 106 (2009) 5088-5092. [PMID: 19279205]
4. Yuan, J., Palioura, S., Salazar, J.C., Su, D., O'Donoghue, P., Hohn, M.J., Cardoso, A.M., Whitman, W.B. and Soll, D. RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea. Proc. Natl. Acad. Sci. USA 103 (2006) 18923-18927. [PMID: 17142313]
Accepted name: tRNA 2-selenouridine synthase
Reaction: selenophosphate + geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA + H2O = 5-methylaminomethyl-2-selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol + diphosphate + phosphate (overall reaction)
(1a) geranyl diphosphate + 5-methylaminomethyl-2-thiouridine34 in tRNA = 5-methylaminomethyl-2-(S-geranyl)thiouridine34 in tRNA + diphosphate
(1b) selenophosphate + 5-methylaminomethyl-2-(S-geranyl)thiouridine34 in tRNA = 5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA + (2E)-3,7-dimethylocta-2,6-diene-1-thiol
(1c) 5-methylaminomethyl-2-(Se-phospho)selenouridine34 in tRNA + H2O = 5-methylaminomethyl-2-selenouridine34 in tRNA + phosphate
Other name(s): selU (gene name); mnmH (gene name); ybbB (gene name); sufY (gene name)
Systematic name: geranyl diphosphate/selenophosphate:tRNA 5-methylaminomethyl-2-thiouridine34 geranyl/selenophosphatetransferase
Comments: This bacterial enzyme converts 5-methylaminomethyl-2-uridine and 5-carboxymethylaminomethyl-2-uridine to the respective selenouridine forms in a two-step process that involves geranylation and subsequent phosphoselenation of the resulting geranylated intermediates. The resultant seleno-phosphorylated uridine intermediates further react with a water molecule to release a phosphate anion and 2-selenouridine tRNA. The enzyme contains a rhodanese domain.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Bartos, P., Maciaszek, A., Rosinska, A., Sochacka, E. and Nawrot, B. Transformation of a wobble 2-thiouridine to 2-selenouridine via S-geranyl-2-thiouridine as a possible cellular pathway. Bioorg. Chem. 56 (2014) 49-53. [PMID: 24971911]
2. Jager, G., Chen, P. and Bjork, G.R. Transfer RNA bound to mnmh protein is enriched with geranylated tRNA—a possible intermediate in its selenation. PLoS One 11 (2016) e0153488. [PMID: 27073879]
3. Sierant, M., Leszczynska, G., Sadowska, K., Komar, P., Radzikowska-Cieciura, E., Sochacka, E. and Nawrot, B. Escherichia coli tRNA 2-selenouridine synthase (SelU) converts S2U-RNA to Se2U-RNA via S-geranylated-intermediate. FEBS Lett. 592 (2018) 2248-2258. [PMID: 29862510]
EC 2.10.1 Molybdenumtransferases or tungstentransferases with sulfide groups as acceptors
Accepted name: molybdopterin molybdotransferase
Reaction: adenylyl-molybdopterin + molybdate = molybdenum cofactor + AMP
For diagram of reaction click here.
Glossary: molybdopterin = H2Dtpp-mP = [(5aR,8R,9aR)-2-amino-4-oxo-6,7-bis(sulfanyl)-1,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogen phosphate
molybdate = tetraoxidomolybdate(2-) = MoO42-
molybdenum cofactor = MoCo = MoO2(OH)Dtpp-mP = {[(5aR,8R,9aR)-2-amino-4-oxo-6,7-bis(sulfanyl-κS)-1,5,5a,8,9a,10-hexahydro-4H-pyrano[3,2-g]pteridin-8-yl]methyl dihydrogenato(2–) phosphate}(dioxo)molybdate
Other name(s): MoeA; Cnx1 (ambiguous)
Systematic name: adenylyl-molybdopterin:molybdate molybdate transferase (AMP-forming)
Comments: Catalyses the insertion of molybdenum into the ene-dithiol group of molybdopterin. In eukaryotes this reaction is catalysed by the N-terminal domain of a fusion protein whose C-terminal domain catalyses EC 2.7.7.75, molybdopterin adenylyltransferase. Requires divalent cations such as Mg2+ or Zn2+ for activity.
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
References:
1. Nichols, J.D. and Rajagopalan, K.V. In vitro molybdenum ligation to molybdopterin using purified components. J. Biol. Chem. 280 (2005) 7817-7822. [PMID: 15632135]
2. Nichols, J.D., Xiang, S., Schindelin, H. and Rajagopalan, K.V. Mutational analysis of Escherichia coli MoeA: two functional activities map to the active site cleft. Biochemistry 46 (2007) 78-86. [PMID: 17198377]
3. Llamas, A., Otte, T., Multhaup, G., Mendel, R.R. and Schwarz, G. The Mechanism of nucleotide-assisted molybdenum insertion into molybdopterin. A novel route toward metal cofactor assembly. J. Biol. Chem. 281 (2006) 18343-18350. [PMID: 16636046]