| EC |
6.3.3.6 |
| Accepted name: |
carbapenam-3-carboxylate synthase |
| Reaction: |
ATP + (2S,5S)-5-carboxymethylproline = AMP + diphosphate + (3S,5S)-carbapenam 3-carboxylate |
| Other name(s): |
CarA (ambiguous); CPS (ambiguous); carbapenam-3-carboxylate ligase; 6-methyl-(2S,5S)-5-carboxymethylproline cyclo-ligase (AMP-forming) |
| Systematic name: |
(2S,5S)-5-carboxymethylproline cyclo-ligase (AMP-forming) |
| Comments: |
The enzyme is involved in the biosynthesis of the carbapenem β-lactam antibiotic (5R)-carbapen-2-em-3-carboxylate in the bacterium Pectobacterium carotovorum. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Gerratana, B., Stapon, A. and Townsend, C.A. Inhibition and alternate substrate studies on the mechanism of carbapenam synthetase from Erwinia carotovora. Biochemistry 42 (2003) 7836–7847. [DOI] [PMID: 12820893] |
| 2. |
Miller, M.T., Gerratana, B., Stapon, A., Townsend, C.A. and Rosenzweig, A.C. Crystal structure of carbapenam synthetase (CarA). J. Biol. Chem. 278 (2003) 40996–41002. [DOI] [PMID: 12890666] |
| 3. |
Raber, M.L., Arnett, S.O. and Townsend, C.A. A conserved tyrosyl-glutamyl catalytic dyad in evolutionarily linked enzymes: carbapenam synthetase and β-lactam synthetase. Biochemistry 48 (2009) 4959–4971. [DOI] [PMID: 19371088] |
| 4. |
Arnett, S.O., Gerratana, B. and Townsend, C.A. Rate-limiting steps and role of active site Lys443 in the mechanism of carbapenam synthetase. Biochemistry 46 (2007) 9337–9345. [DOI] [PMID: 17658887] |
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| [EC 6.3.3.6 created 2013 as 6.3.1.16, transferred 2013 to EC 6.3.3.6] |
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