The Enzyme Database

Your query returned 9 entries.    printer_iconPrintable version

EC 2.1.1.248     
Accepted name: methylamine—corrinoid protein Co-methyltransferase
Reaction: methylamine + a [Co(I) methylamine-specific corrinoid protein] = a [methyl-Co(III) methylamine-specific corrinoid protein] + NH3
Other name(s): mtmB (gene name); monomethylamine methyltransferase
Systematic name: monomethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of a methyl group from methylamine to a methylamine-specific corrinoid protein (MtmC), is involved in methanogenesis from methylamine. The enzyme contains the unusual amino acid pyrrolysine [3]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Burke, S.A. and Krzycki, J.A. Reconstitution of Monomethylamine:Coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 272 (1997) 16570–16577. [DOI] [PMID: 9195968]
2.  Burke, S.A., Lo, S.L. and Krzycki, J.A. Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine. J. Bacteriol. 180 (1998) 3432–3440. [PMID: 9642198]
3.  Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484–491. [DOI] [PMID: 15450490]
[EC 2.1.1.248 created 2012]
 
 
EC 2.1.1.249     
Accepted name: dimethylamine—corrinoid protein Co-methyltransferase
Reaction: dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein] = a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
Other name(s): mtbB (gene name); dimethylamine methyltransferase
Systematic name: dimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of a methyl group from dimethylamine to a dimethylamine-specific corrinoid protein (MtbC), is involved in methanogenesis from dimethylamine. The enzyme contains the unusual amino acid pyrrolysine [3]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wassenaar, R.W., Keltjens, J.T., van der Drift, C. and Vogels, G.D. Purification and characterization of dimethylamine:5-hydroxybenzimidazolyl-cobamide methyltransferase from Methanosarcina barkeri Fusaro. Eur. J. Biochem. 253 (1998) 692–697. [DOI] [PMID: 9654067]
2.  Ferguson, D.J., Jr., Gorlatova, N., Grahame, D.A. and Krzycki, J.A. Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri. J. Biol. Chem. 275 (2000) 29053–29060. [DOI] [PMID: 10852929]
3.  Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484–491. [DOI] [PMID: 15450490]
[EC 2.1.1.249 created 2012]
 
 
EC 2.1.1.250     
Accepted name: trimethylamine—corrinoid protein Co-methyltransferase
Reaction: trimethylamine + a [Co(I) trimethylamine-specific corrinoid protein] = a [methyl-Co(III) trimethylamine-specific corrinoid protein] + dimethylamine
Other name(s): mttB (gene name); trimethylamine methyltransferase
Systematic name: trimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of a methyl group from trimethylamine to a trimethylamine-specific corrinoid protein (MttC), is involved in methanogenesis from trimethylamine. The enzyme contains the unusual amino acid pyrrolysine [2]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Ferguson, D.J., Jr. and Krzycki, J.A. Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri. J. Bacteriol. 179 (1997) 846–852. [DOI] [PMID: 9006042]
2.  Krzycki, J.A. Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases. Curr. Opin. Chem. Biol. 8 (2004) 484–491. [DOI] [PMID: 15450490]
[EC 2.1.1.250 created 2012]
 
 
EC 2.1.1.376     
Accepted name: glycine betaine—corrinoid protein Co-methyltransferase
Reaction: glycine betaine + a [Co(I) glycine betaine-specific corrinoid protein] = N,N-dimethylglycine + a [methyl-Co(III) glycine betaine-specific corrinoid protein]
Other name(s): mtgB (gene name); glycine betaine methyltransferase
Systematic name: glycine betaine:[Co(I) glycine betaine-specific corrinoid protein] Co-methyltransferase
Comments: The enzyme, which catalyses the transfer of a methyl group from glycine betaine to a glycine betaine-specific corrinoid protein (MtgC), is involved in methanogenesis from glycine betaine in some methanogenic archaea, and in glycine betaine degradation in some bacteria. Unlike similar enzymes involved in methanogenesis from methylated C1 compounds, this enzyme does not contain the unusual amino acid L-pyrrolysine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ticak, T., Kountz, D.J., Girosky, K.E., Krzycki, J.A. and Ferguson, D.J., Jr. A nonpyrrolysine member of the widely distributed trimethylamine methyltransferase family is a glycine betaine methyltransferase. Proc. Natl. Acad. Sci. USA 111 (2014) E4668–E4676. [DOI] [PMID: 25313086]
2.  Creighbaum, A.J., Ticak, T., Shinde, S., Wang, X. and Ferguson, D.J., Jr. Examination of the glycine betaine-dependent methylotrophic methanogenesis pathway: insights into anaerobic quaternary amine methylotrophy. Front. Microbiol. 10:2572 (2019). [DOI] [PMID: 31787957]
[EC 2.1.1.376 created 2021]
 
 
EC 2.1.1.378     
Accepted name: [methyl-Co(III) glycine betaine-specific corrinoid protein]—tetrahydrofolate methyltransferase
Reaction: a [methyl-Co(III) glycine betaine-specific corrinoid protein] + tetrahydrofolate = a [Co(I) glycine betaine-specific corrinoid protein] + 5-methyltetrahydrofolate
Other name(s): mtgA (gene name); DSY3157 (locus name)
Systematic name: [methyl-Co(III) glycine betaine-specific corrinoid protein]:tetrahydrofolate N-methyltransferase
Comments: This enzyme, characterized from the anaerobic bacterium Desulfitobacterium hafniense Y51, catalyses a similar reaction to that of EC 2.1.1.258, 5-methyltetrahydrofolate—corrinoid/iron-sulfur protein Co-methyltransferase, but in the opposite direction, transferring a methyl group from a methylated corrinoid protein to tetrahydrofolate. The corrinoid protein is specifically methylated by EC 2.1.1.376, glycine betaine—corrinoid protein Co-methyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ticak, T., Kountz, D.J., Girosky, K.E., Krzycki, J.A. and Ferguson, D.J., Jr. A nonpyrrolysine member of the widely distributed trimethylamine methyltransferase family is a glycine betaine methyltransferase. Proc. Natl. Acad. Sci. USA 111 (2014) E4668–E4676. [DOI] [PMID: 25313086]
[EC 2.1.1.378 created 2021]
 
 
EC 5.4.99.58     
Accepted name: methylornithine synthase
Reaction: L-lysine = (3R)-3-methyl-D-ornithine
Glossary: (3R)-3-methyl-D-ornithine = (2R,3R)-2,5-diamino-3-methylpentanoate
Other name(s): PylB
Systematic name: L-lysine carboxy-aminomethylmutase
Comments: The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The reaction is part of the biosynthesis pathway of pyrrolysine, a naturally occurring amino acid found in some archaeal methyltransferases.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Gaston, M.A., Zhang, L., Green-Church, K.B. and Krzycki, J.A. The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine. Nature 471 (2011) 647–650. [DOI] [PMID: 21455182]
2.  Quitterer, F., List, A., Eisenreich, W., Bacher, A. and Groll, M. Crystal structure of methylornithine synthase (PylB): insights into the pyrrolysine biosynthesis. Angew. Chem. Int. Ed. Engl. 51 (2012) 1339–1342. [DOI] [PMID: 22095926]
[EC 5.4.99.58 created 2012]
 
 
EC 6.1.1.25      
Deleted entry: lysine—tRNAPyl ligase. The tRNAPyl is now known only to be charged with pyrrolysine (cf. EC 6.1.1.26).
[EC 6.1.1.25 created 2002, deleted 2012]
 
 
EC 6.1.1.26     
Accepted name: pyrrolysine—tRNAPyl ligase
Reaction: ATP + L-pyrrolysine + tRNAPyl = AMP + diphosphate + L-pyrrolysyl-tRNAPyl
Glossary: pyrrolysine = N6-[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-ylcarbonyl]-L-lysine
Other name(s): PylS; pyrrolysyl-tRNA synthetase
Systematic name: L-pyrrolysine:tRNAPyl ligase (AMP-forming)
Comments: In organisms such as Methanosarcina barkeri that incorporate the modified amino acid pyrrolysine (Pyl) into certain methylamine methyltransferases, an unusual tRNAPyl, with a CUA anticodon, can be charged directly with pyrrolysine by this class II aminoacyl—tRNA ligase. The enzyme is specific for pyrrolysine as substrate as it cannot be replaced by lysine or any of the other natural amino acids [1].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Blight, S.K., Larue, R.C., Mahapatra, A., Longstaff, D.G., Chang, E., Zhao, G., Kang, P.T., Green-Church, K.B., Chan, M.K. and Krzycki, J.A. Direct charging of tRNA(CUA) with pyrrolysine in vitro and in vivo. Nature 431 (2004) 333–335. [DOI] [PMID: 15329732]
2.  Polycarpo, C., Ambrogelly, A., Bérubé, A., Winbush, S.M., McCloskey, J.A., Crain, P.F., Wood, J.L. and Söll, D. An aminoacyl-tRNA synthetase that specifically activates pyrrolysine. Proc. Natl. Acad. Sci. USA 101 (2004) 12450–12454. [DOI] [PMID: 15314242]
3.  Schimmel, P. and Beebe, K. Molecular biology: genetic code seizes pyrrolysine. Nature 431 (2004) 257–258. [DOI] [PMID: 15372017]
[EC 6.1.1.26 created 2007]
 
 
EC 6.3.2.59     
Accepted name: 3-methyl-D-ornithine—L-lysine ligase
Reaction: ATP + (3R)-3-methyl-D-ornithine + L-lysine = ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Glossary: L-pyrrolysine = N6-{[(2R,3R)-3-methyl-3,4-dihydro-2H-pyrrol-2-yl]carbonyl}-L-lysine
Other name(s): N6-[(2R,3R)-3-methylornithyl]-L-lysine synthase; 3-methylornithine—L-lysine ligase; pylC (gene name)
Systematic name: (3R)-3-methyl-D-ornithine:L-lysine γ-ligase (ADP-forming)
Comments: The enzyme participates in the biosynthesis of L-pyrrolysine, a naturally occurring, genetically coded amino acid found in some methanogenic archaea and a few bacterial species. L-pyrrolysine is present in several methyltransferases that are involved in methyl transfer from methylated amine compounds to coenzyme M.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Gaston, M.A., Zhang, L., Green-Church, K.B. and Krzycki, J.A. The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine. Nature 471 (2011) 647–650. [DOI] [PMID: 21455182]
2.  Cellitti, S.E., Ou, W., Chiu, H.P., Grunewald, J., Jones, D.H., Hao, X., Fan, Q., Quinn, L.L., Ng, K., Anfora, A.T., Lesley, S.A., Uno, T., Brock, A. and Geierstanger, B.H. D-Ornithine coopts pyrrolysine biosynthesis to make and insert pyrroline-carboxy-lysine. Nat. Chem. Biol. 7 (2011) 528–530. [DOI] [PMID: 21525873]
3.  Quitterer, F., List, A., Beck, P., Bacher, A. and Groll, M. Biosynthesis of the 22nd genetically encoded amino acid pyrrolysine: structure and reaction mechanism of PylC at 1.5A resolution. J. Mol. Biol. 424 (2012) 270–282. [DOI] [PMID: 22985965]
[EC 6.3.2.59 created 2021]
 
 


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