Enzyme Nomenclature

Continued from EC 2.8.1 and EC 2.8.2

EC 2.8.3 to EC 2.10.1

Sections

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


EC 2.8.3 CoA-transferases

Contents

EC 2.8.3.1 propionate CoA-transferase
EC 2.8.3.2 oxalate CoA-transferase
EC 2.8.3.3 malonate CoA-transferase
EC 2.8.3.4 deleted
EC 2.8.3.5 3-oxoacid CoA-transferase
EC 2.8.3.6 3-oxoadipate CoA-transferase
EC 2.8.3.7 deleted now EC 2.8.3.20 and EC 2.8.3.22
EC 2.8.3.8 acetate CoA-transferase
EC 2.8.3.9 butyrate—acetoacetate CoA-transferase
EC 2.8.3.10 citrate CoA-transferase
EC 2.8.3.11 citramalate CoA-transferase
EC 2.8.3.12 glutaconate CoA-transferase
EC 2.8.3.13 succinate—hydroxymethylglutarate CoA-transferase
EC 2.8.3.14 5-hydroxypentanoate CoA-transferase
EC 2.8.3.15 succinyl-CoA:(R)-benzylsuccinate CoA-transferase
EC 2.8.3.16 formyl-CoA transferase
EC 2.8.3.17 cinnamoyl-CoA:phenyllactate CoA-transferase
EC 2.8.3.18 succinyl-CoA:acetate CoA-transferase
EC 2.8.3.19 CoA:oxalate CoA-transferase
EC 2.8.3.20 succinyl-CoA—D-citramalate CoA-transferase
EC 2.8.3.21 L-carnitine CoA-transferase
EC 2.8.3.22 succinyl-CoA—L-malate CoA-transferase
EC 2.8.3.23 caffeate CoA-transferase
EC 2.8.3.24 (R)-2-hydroxy-4-methylpentanoate CoA-transferase
EC 2.8.3.25 bile acid CoA-transferase


Entries

EC 2.8.3.1

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, EXPASY, KEGG, Metacyc, UM-BBD, 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.

[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.

[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 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 2.8.3.3 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 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, EXPASY, GTD, KEGG, Metacyc, PDB, UM-BBD, 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.

[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 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

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, UM-BBD, 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.

[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 2013)]

EC 2.8.3.7

Accepted name: succinate—citramalate CoA-transferase

Reaction: succinyl-CoA + citramalate = succinate + citramalyl-CoA

Other name(s): itaconate CoA-transferase; citramalate CoA-transferase; citramalate coenzyme A-transferase; succinyl coenzyme A-citramalyl coenzyme A transferase

Systematic name: succinyl-CoA:citramalate CoA-transferase

Comments: Itaconate can also act as acceptor.

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 9033-60-7

References:

1. Cooper, R.A. and Kornberg, H.L. The utilization of itaconate by Pseudomonas sp. Biochem. J. 91 (1964) 82-91. [PMID: 4284209]

[EC 2.8.3.7 created 1972]

EC 2.8.3.8

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; succinyl-CoA:acetate CoA transferase

Systematic name: acyl-CoA:acetate CoA-transferase

Comments: Acts on 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. [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]

[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 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]

[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, KEGG, Metacyc, 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]

[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. [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 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, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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]

[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

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]

[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 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, EXPASY, KEGG, Metacyc, UM-BBD, 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]

[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, 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]

[EC 2.8.3.16 created 2003]

EC 2.8.3.17

Accepted name: cinnamoyl-CoA:phenyllactate CoA-transferase

Reaction: (E)-cinnamoyl-CoA + (R)-phenyllactate = (E)-cinnamate + (R)-phenyllactyl-CoA

Other name(s): FldA

Systematic name: (E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase

Comments: 3-Phenylproprionate is a better CoA acceptor than (R)-phenyllactate in vitro. The enzyme from Clostridium sporogenes is specific for derivatives of 3-phenylpropionate and 4-phenylbutyrate.

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]

[EC 2.8.3.17 created 2003]

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 acetic acid bacteria the enzyme, which is highly specific, catalyses the conversion of toxic acetate to acetyl-CoA [2,3]. In the hydrogenosomes of some trichomonads the enzyme catalyses the production of acetate [1].

Links to other databases: BRENDA, EXPASY, GTD, KEGG, 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. 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]

3. 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]

[EC 2.8.3.18 created 2013]

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, KEGG, Metacyc, 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]

[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, 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]

[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, KEGG, MetaCyc, 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]

[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 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]

[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, 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]

[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: (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]

[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. 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]

[EC 2.8.3.25 created 2005 as EC 3.1.2.26, transferred 2016 to EC 2.8.3.25]


EC 2.8.4 Transferring alkylthio groups

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 S12] (aspartate89-C3)-methylthiotransferase
EC 2.8.4.5 tRNA (N6-L-threonylcarbamoyladenosine37-C2)-methylthiotransferase


EC 2.8.4.1

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-mercaptoethanesulfonate
2-(methylthio)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, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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]

[EC 2.8.4.1 created 2001, modified 2011]

EC 2.8.4.2

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]

[EC 2.8.4.2 created 2010]

EC 2.8.4.3

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-methylthio-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-methylthio-N6-dimethylallyladenine37 in tRNA

For diagram of reaction click here.

Other name(s): MiaB; 2-methylthio-N-6-isopentenyl adenosine synthase; tRNA-i6A37 methylthiotransferase

Systematic name: tRNA (N6-dimethylallyladenosine37):sulfur-(sulfur carrier),S-adenosyl-L-methionine C2-methylthiotransferase

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, 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]

[EC 2.8.4.3 created 2014, modified 2015]

EC 2.8.4.4

Accepted name: [ribosomal protein S12] (aspartate89-C3)-methylthiotransferase

Reaction: L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced acceptor = 3-methylthio-L-aspartate89-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + oxidized acceptor (overall reaction)
(1a) S-adenosyl-L-methionine + L-aspartate89-[ribosomal protein S12] + sulfur-(sulfur carrier) = S-adenosyl-L-homocysteine + L-aspartate89-[ribosomal protein S12]-methanethiol + (sulfur carrier)
(1b) L-aspartate89-[ribosomal protein S12]-methanethiol + S-adenosyl-L-methionine + reduced acceptor = 3-methylthio-L-aspartate89-[ribosomal protein S12] + L-methionine + 5'-deoxyadenosine + oxidized receptor

Other name(s): RimO; [ribosomal protein S12]-Asp89:sulfur-(sulfur carrier),S-adenosyl-L-methionine C3-methylthiotransferase

Systematic name: [ribosomal protein S12]-L-aspartate89:sulfur-(sulfur carrier),S-adenosyl-L-methionine C3-methylthiotransferase

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 methylthiol 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, 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]

[EC 2.8.4.4 created 2014, modified 2014]

EC 2.8.4.5

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-methylthio-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-methylthio-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)

Systematic name: tRNA (N6-L-threonylcarbamoyladenosine37):sulfur-(sulfur carrier),S-adenosyl-L-methionine C2-methylthiotransferase

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]

[EC 2.8.4.5 created 2014, modified 2015]


EC 2.9 Transferring Selenium-Containing Groups

EC 2.9.1 Selenotransferases

Contents

EC 2.9.1.1 L-seryl-tRNASec selenium transferase
EC 2.9.1.2 O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase


Entries

EC 2.9.1.1

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, 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]

[EC 2.9.1.1 created 1999]

EC 2.9.1.2

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, 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]

[EC 2.9.1.2 created 2009, modified 2014]


EC 2.10 Transferring molybdenum- or tungsten-containing groups

EC 2.10.1 Molybdenumtransferases or tungstentransferases with sulfide groups as acceptors

EC 2.10.1.1

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-6,7-dimercapto-4-oxo-4,5,5a,8,9a,10-hexahydro-1H-pyrano[3,2-g]pteridin-8-yl)methyl dihydrogen phosphate = [(5aR,8R,9aR)-2-amino-4-oxo-6,7-disulfanyl-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-di(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]

[EC 2.10.1.1 created 2011]


Continued with EC 3
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