KEGG   ENZYME: 5.1.1.14Help
Entry
EC 5.1.1.14                 Enzyme                                 

Name
nocardicin A epimerase;
isonocardicin A epimerase;
nocJ (gene name)
Class
Isomerases;
Racemases and epimerases;
Acting on amino acids and derivatives
BRITE hierarchy
Sysname
nocardicin-C epimerase
Reaction(IUBMB)
(1) isonocardicin C = nocardicin C [RN:R10883];
(2) isonocardicin A = nocardicin A [RN:R03073]
Reaction(KEGG)
Substrate
isonocardicin C [CPD:C17352];
isonocardicin A [CPD:C00927]
Product
nocardicin C [CPD:C17351];
nocardicin A [CPD:C01941]
Comment
Requires pyridoxal 5'-phosphate. The enzyme, characterized from the bacterium Nocardia uniformis, is involved in the biosynthesis of the monolactam antibiotic nocardicin A. It catalyses the epimerization of the amino group at position 9' from (S)- configuration to (R)-. The enzyme can act on both isonocardicin A and isonocardicin C, but the in vivo substrate appears to be the latter [3].
History
EC 5.1.1.14 created 1992, modified 2016
Pathway
ec00261  Monobactam biosynthesis
ec01130  Biosynthesis of antibiotics
Orthology
K19105  nocardicin-A epimerase
Genes
AMI: Amir_4594
Taxonomy
Reference
1
  Authors
Wilson, B.A., Bantia, S., Salituro, G.M., Reeve, A.M. and Townsend, C.A.
  Title
Cell-free biosynthesis of nocardicin A from nocardicin E and S-adenosylmethionine.
  Journal
J Am Chem Soc 110:8238-8239 (1988)
Reference
2  [PMID:15252031]
  Authors
Kelly WL, Townsend CA.
  Title
Mutational analysis and characterization of nocardicin C-9' epimerase.
  Journal
J Biol Chem 279:38220-7 (2004)
DOI:10.1074/jbc.M405450200
Reference
3  [PMID:15629944]
  Authors
Kelly WL, Townsend CA.
  Title
Mutational analysis of nocK and nocL in the nocardicin a producer Nocardia uniformis.
  Journal
J Bacteriol 187:739-46 (2005)
DOI:10.1128/JB.187.2.739-746.2005
Other DBs
ExplorEnz - The Enzyme Database: 5.1.1.14
IUBMB Enzyme Nomenclature: 5.1.1.14
ExPASy - ENZYME nomenclature database: 5.1.1.14
BRENDA, the Enzyme Database: 5.1.1.14
CAS: 118246-75-6

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