The Enzyme Database

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EC 3.5.3.22     
Accepted name: proclavaminate amidinohydrolase
Reaction: amidinoproclavaminate + H2O = proclavaminate + urea
For diagram of clavulanate biosynthesis, click here
Other name(s): PAH; proclavaminate amidino hydrolase
Systematic name: amidinoproclavaminate amidinohydrolase
Comments: Forms part of the pathway for the biosythesis of the β-lactamase inhibitor clavulanate in Streptomyces clavuligerus. It carries out an intermediary reaction between the first reaction of EC 1.14.11.21, clavaminate synthase, and the second and third reactions of that enzyme. Requires Mn2+.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Salowe, S.P., Krol, W.J., Iwatareuyl, D. and Townsend, C.A. Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction. Biochemistry 30 (1991) 2281–2292. [PMID: 1998687]
2.  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]
3.  Townsend, C.A. New reactions in clavulanic acid biosynthesis. Curr. Opin. Chem. Biol. 6 (2002) 583–589. [DOI] [PMID: 12413541]
4.  Wu, T.K., Busby, R.W., Houston, T.A., McIlwaine, D.B., Egan, L.A. and Townsend, C.A. Identification, cloning, sequencing, and overexpression of the gene encoding proclavaminate amidino hydrolase and characterization of protein function in clavulanic acid biosynthesis. J. Bacteriol. 177 (1995) 3714–3720. [DOI] [PMID: 7601835]
[EC 3.5.3.22 created 2003]
 
 


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