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
ec01100  Metabolic pathways
ec01130  Biosynthesis of antibiotics
Orthology
K18316  carbapenam-3-carboxylate synthase
K18582  carbapenam-3-carboxylate synthase
Genes
SERA: Ser39006_009920
SERQ: CWC46_09915
DZE: Dd1591_0213
DAQ: DAQ1742_04174(cpmA)
PAO: Pat9b_5317
PLU: plu0182(cpmA)
PLUM: A4R40_00880
PTT: VY86_09615
PRG: RB151_027380(carA_2)
BGP: BGL_2c27620
SCT: SCAT_p0832(thnM)
SFA: Sfla_0156
STRP: F750_6865
 » show all
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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