EC 5.4.99.58 - Methylornithine synthase

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IntEnz Enzyme Nomenclature
EC 5.4.99.58

Names

Accepted name:
methylornithine synthase
Other name:
PylB
Systematic name:
L-lysine carboxy-aminomethylmutase

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Gaston, M. A., Zhang, L., Green-Church, K. B., Krzycki, J. A.
    The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine.
    Nature 471 : 647-650 (2011). [PMID: 21455182]
  2. Quitterer, F., List, A., Eisenreich, W., Bacher, A., Groll, M.
    Crystal structure of methylornithine synthase (PylB): insights into the pyrrolysine biosynthesis.
    Angew. Chem. Int. Ed. Engl. 51 : 1339-1342 (2012). [PMID: 22095926]

[EC 5.4.99.58 created 2012]