KEGG   ENZYME: 6.3.3.6Help
Entry
EC 6.3.3.6                  Enzyme                                 

Name
carbapenam-3-carboxylate synthase;
CarA (ambiguous);
CPS (ambiguous);
carbapenam-3-carboxylate ligase;
6-methyl-(2S,5S)-5-carboxymethylproline cyclo-ligase (AMP-forming)
Class
Ligases;
Forming carbon-nitrogen bonds;
Cyclo-ligases
BRITE hierarchy
Sysname
(2S,5S)-5-carboxymethylproline cyclo-ligase (AMP-forming)
Reaction(IUBMB)
ATP + (2S,5S)-5-carboxymethylproline = AMP + diphosphate + (3S,5S)-carbapenam 3-carboxylate [RN:R10556]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
(2S,5S)-5-carboxymethylproline [CPD:C17366]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
(3S,5S)-carbapenam 3-carboxylate
Comment
The enzyme is involved in the biosynthesis of the carbapenem beta-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum.
History
EC 6.3.3.6 created 2013 as 6.3.1.16, transferred 2013 to EC 6.3.3.6
Pathway
ec00332  Carbapenem biosynthesis
ec01130  Biosynthesis of antibiotics
Orthology
K18316  carbapenam-3-carboxylate synthase
K18582  carbapenam-3-carboxylate synthase
Genes
DZE: Dd1591_0213
PAO: Pat9b_5317
PLU: plu0182(cpmA)
PTT: VY86_09615
SCT: SCAT_p0832(thnM)
SCY: SCATT_p09030
SFA: Sfla_0156
STRP: F750_6865
Taxonomy
Reference
1  [PMID:12820893]
  Authors
Gerratana B, Stapon A, Townsend CA
  Title
Inhibition and alternate substrate studies on the mechanism of carbapenam synthetase from Erwinia carotovora.
  Journal
Biochemistry 42:7836-47 (2003)
DOI:10.1021/bi034361d
Reference
2  [PMID:12890666]
  Authors
Miller MT, Gerratana B, Stapon A, Townsend CA, Rosenzweig AC
  Title
Crystal structure of carbapenam synthetase (CarA).
  Journal
J Biol Chem 278:40996-1002 (2003)
DOI:10.1074/jbc.M307901200
  Sequence
Reference
3  [PMID:19371088]
  Authors
Raber ML, Arnett SO, Townsend CA
  Title
A conserved tyrosyl-glutamyl catalytic dyad in evolutionarily linked enzymes: carbapenam synthetase and beta-lactam synthetase.
  Journal
Biochemistry 48:4959-71 (2009)
DOI:10.1021/bi900432n
  Sequence
Reference
4  [PMID:17658887]
  Authors
Arnett SO, Gerratana B, Townsend CA
  Title
Rate-limiting steps and role of active site Lys443 in the mechanism of carbapenam synthetase.
  Journal
Biochemistry 46:9337-45 (2007)
DOI:10.1021/bi0618464
Other DBs
ExplorEnz - The Enzyme Database: 6.3.3.6
IUBMB Enzyme Nomenclature: 6.3.3.6
ExPASy - ENZYME nomenclature database: 6.3.3.6
BRENDA, the Enzyme Database: 6.3.3.6

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