| 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] |
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| [EC 5.4.99.58 created 2012] |
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