Entry
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
ec01110 Biosynthesis of secondary metabolites
Orthology
K18316 carbapenam-3-carboxylate synthase
K18582 carbapenam-3-carboxylate synthase
Genes
PRG : RB151_027380(carA_2)
» show all
Taxonomy
Reference
Authors
Gerratana B, Stapon A, Townsend CA
Title
Inhibition and alternate substrate studies on the mechanism of carbapenam synthetase from Erwinia carotovora.
Journal
Reference
Authors
Miller MT, Gerratana B, Stapon A, Townsend CA, Rosenzweig AC
Title
Crystal structure of carbapenam synthetase (CarA).
Journal
Sequence
Reference
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
Sequence
Reference
Authors
Arnett SO, Gerratana B, Townsend CA
Title
Rate-limiting steps and role of active site Lys443 in the mechanism of carbapenam synthetase.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 6.3.3.6
ExPASy - ENZYME nomenclature database: 6.3.3.6
BRENDA, the Enzyme Database: 6.3.3.6