EC 188.8.131.52 - (carboxyethyl)arginine β-lactam-synthase
IntEnz Enzyme Nomenclature
L-2-N-(2-carboxyethyl)arginine cyclo-ligase (AMP-forming)
23620 [IUBMB]N2-(2-carboxyethyl)-L-arginineN(2)-(2-carboxyethyl)-L-arginineName origin: UniProt - CHECKED (C)Formula: C9H18N4O4
Charge: 0ChEBI compound status: CHECKED (C)ATPATPName origin: UniProt - CHECKED (C)Formula: C10H12N5O13P3
Charge: -4ChEBI compound status: CHECKED (C)<?>AMPAMPName origin: UniProt - CHECKED (C)Formula: C10H12N5O7P
Charge: -2ChEBI compound status: CHECKED (C)deoxyamidinoproclavaminatedeoxyamidinoproclavaminateName origin: UniProt - CHECKED (C)Formula: C9H16N4O3
Charge: 0ChEBI compound status: CHECKED (C)diphosphatediphosphateName origin: UniProt - CHECKED (C)Formula: HO7P2
Charge: -3ChEBI compound status: CHECKED (C)
Forms part of the pathway for the biosythesis of the β-lactamase inhibitor clavulanate in Streptomyces clavuligerus. It has been proposed  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
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: 7388-7398 (2001).
New reactions in clavulanic acid biosynthesis.Curr. Opin. Chem. Biol. 6: 583-589 (2002). [PMID: 12413541]
β-Lactam synthetase: a new biosynthetic enzyme.Proc. Natl. Acad. Sci. USA 95: 9082-9086 (1998). [PMID: 9689037]
[EC 184.108.40.206 created 2003]