1gm9
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CRYSTAL STRUCTURES OF PENICILLIN ACYLASE ENZYME-SUBSTRATE COMPLEXES: STRUCTURAL INSIGHTS INTO THE CATALYTIC MECHANISM
OverviewOverview
The crystal structure of penicillin G acylase from Escherichia coli has, been determined to a resolution of 1.3 A from a crystal form grown in the, presence of ethylene glycol. To study aspects of the substrate specificity, and catalytic mechanism of this key biotechnological enzyme, mutants were, made to generate inactive protein useful for producing enzyme-substrate, complexes. Owing to the intimate association of enzyme activity and, precursor processing in this protein family (the Ntn hydrolases), most, attempts to alter active-site residues lead to processing defects., Mutation of the invariant residue Arg B263 results in the accumulation of, a protein precursor form. However, the mutation of Asn B241, a residue, implicated in stabilisation of the tetrahedral intermediate during, ... [(full description)]
About this StructureAbout this Structure
1GM9 is a [Protein complex] structure of sequences from [Escherichia coli] with CA, EDO and SOX as [ligands]. Active as [[1]], with EC number [3.5.1.11]. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structures of penicillin acylase enzyme-substrate complexes: structural insights into the catalytic mechanism., McVey CE, Walsh MA, Dodson GG, Wilson KS, Brannigan JA, J Mol Biol. 2001 Oct 12;313(1):139-50. PMID:11601852
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