1gq7: Difference between revisions
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Revision as of 16:12, 30 October 2007
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PROCLAVAMINATE AMIDINO HYDROLASE FROM STREPTOMYCES CLAVULIGERUS
OverviewOverview
During biosynthesis of the clinically used beta-lactamase inhibitor, clavulanic acid, one of the three steps catalysed by clavaminic acid, synthase is separated from the other two by a step catalysed by, proclavaminic acid amidino hydrolase (PAH), in which the guanidino group, of an intermediate is hydrolysed to give proclavaminic acid and urea. PAH, shows considerable sequence homology with the primary metabolic arginases, which hydrolyse arginine to ornithine and urea, but does not accept, arginine as a substrate. Like other members of the bacterial sub-family of, arginases, PAH is hexameric in solution and requires Mn2+ ions for, activity. Other metal ions, including Co2+, can substitute for Mn2+. Two, new substrates for PAH were identified, N-acetyl-(L)-arginine and, ... [(full description)]
About this StructureAbout this Structure
1GQ7 is a [Single protein] structure of sequence from [Streptomyces clavuligerus] with MN as [ligand]. Active as [Agmatinase], with EC number [3.5.3.11]. Structure known Active Site: MNA. Full crystallographic information is available from [OCA].
ReferenceReference
Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis., Elkins JM, Clifton IJ, Hernandez H, Doan LX, Robinson CV, Schofield CJ, Hewitson KS, Biochem J. 2002 Sep 1;366(Pt 2):423-34. PMID:12020346
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