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, 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.
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, 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.
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.
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]
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]
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, 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, 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]
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, 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]
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: 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]
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]
Contents
EC 2.8.4.1 coenzyme-B sulfoethylthiotransferase
EC 2.8.4.2 arsenate-mycothiol transferase
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]
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: 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]
Accepted name: O-phospho-L-seryl-tRNASec:L-selenocysteinyl-tRNA synthase
Reaction: O-phospho-L-seryl-tRNASec + selenophosphate = L-selenocysteinyl-tRNASec + 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 [17142313]. 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]
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-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
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]