EC |
6.3.3.4 |
Accepted name: |
(carboxyethyl)arginine β-lactam-synthase |
Reaction: |
ATP + L-N2-(2-carboxyethyl)arginine = AMP + diphosphate + deoxyamidinoproclavaminate |
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For diagram of clavulanate biosynthesis, click here |
Other name(s): |
L-2-N-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming) |
Systematic name: |
L-N2-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming) |
Comments: |
Forms part of the pathway for the biosythesis of the β-lactamase inhibitor clavulanate in Streptomyces clavuligerus. It has been proposed [3] that L-N2-(2-carboxyethyl)arginine is first converted into an acyl-AMP by reaction with ATP and loss of diphosphate, and that the β-lactam ring is then formed by the intramolecular attack of the β-nitrogen on the activated carboxy group. |
Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
References: |
1. |
Zhou, J., Kelly, W.L., Bachmann, B.O., Gunsior, M., Townsend, C.A. and Solomon, E.I. Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional α-KG-dependent non-heme iron enzyme: Correlation with mechanisms and reactivities. J. Am. Chem. Soc. 123 (2001) 7388–7398. [DOI] [PMID: 11472170] |
2. |
Townsend, C.A. New reactions in clavulanic acid biosynthesis. Curr. Opin. Chem. Biol. 6 (2002) 583–589. [DOI] [PMID: 12413541] |
3. |
Bachmann, B.O., Li, R. and Townsend, C.A. β-Lactam synthetase: a new biosynthetic enzyme. Proc. Natl. Acad. Sci. USA 95 (1998) 9082–9086. [DOI] [PMID: 9689037] |
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[EC 6.3.3.4 created 2003] |
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