KEGG   ENZYME: 5.4.99.58Help
Entry
EC 5.4.99.58                Enzyme                                 

Name
methylornithine synthase;
PylB
Class
Isomerases;
Intramolecular transferases;
Transferring other groups
BRITE hierarchy
Sysname
L-lysine carboxy-aminomethylmutase
Reaction(IUBMB)
L-lysine = (3R)-3-methyl-D-ornithine [RN:R10010]
Reaction(KEGG)
Substrate
L-lysine [CPD:C00047]
Product
(3R)-3-methyl-D-ornithine [CPD:C20277]
Comment
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.
History
EC 5.4.99.58 created 2012
Pathway
Lysine biosynthesis
Microbial metabolism in diverse environments
Orthology
K16180  
methylornithine synthase
Genes
DAT: 
HRM2_15240(bioB2)
DSY: 
DHD: 
DDH: 
DAE: 
DGI: 
TJR: 
DOR: 
DMI: 
TPZ: 
AAR: 
MAC: 
MA_0154(bioB)
MBA: 
MBY: 
MBW: 
MBAR: 
MBAK: 
MMA: 
MMAZ: 
MMJ: 
MVC: 
MEK: 
MLS: 
METM: 
MEF: 
MEQ: 
MSJ: 
MSZ: 
MSW: 
MTHE: 
MTHR: 
MHOR: 
MBU: 
Mbur_2085(pylB)
MMET: 
MMH: 
MEV: 
MZH: 
MPY: 
Mpsy_1722(bioB)
MHZ: 
TAR: 
MAX: 
MER: 
MEAR: 
MARC: 
 » show all
Taxonomy
Reference
1  [PMID:21455182]
  Authors
Gaston MA, Zhang L, Green-Church KB, Krzycki JA
  Title
The complete biosynthesis of the genetically encoded amino acid pyrrolysine from  lysine.
  Journal
Nature. 471 (2011) 647-50.
  Sequence
[mac:MA_0154]
Reference
2  [PMID:22095926]
  Authors
Quitterer F, List A, Eisenreich W, Bacher A, Groll M
  Title
Crystal structure of methylornithine synthase (PylB): insights into the pyrrolysine biosynthesis.
  Journal
Angew. Chem. Int. Ed. Engl. 51 (2012) 1339-42.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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