1ajq
From Proteopedia
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[[Category: ligand induced conformational change]] | [[Category: ligand induced conformational change]] | ||
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Revision as of 12:44, 30 October 2007
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PENICILLIN ACYLASE COMPLEXED WITH THIOPHENEACETIC ACID
Overview
The enzyme penicillin acylase (penicillin amidohydrolase EC 3.5.1. 11), catalyses the cleavage of the amide bond in the benzylpenicillin, (penicillin G) side-chain to produce phenylacetic acid and, 6-aminopenicillanic acid (6-APA). The enzyme is of great pharmaceutical, importance, as the product 6-APA is the starting point for the synthesis, of many semi-synthetic penicillin antibiotics. Studies have shown that the, enzyme is specific for hydrolysis of phenylacetamide derivatives, but is, more tolerant of features in the rest of the substrate. It is this, property that has led to many other applications for the enzyme, and, greater knowledge of the enzyme's structure and specificity could, facilitate engineering of the enzyme, enhancing its potential for chemical, and industrial ... [(full description)]
About this Structure
1AJQ is a [Protein complex] structure of sequences from [Escherichia coli] with CA and SPA as [ligands]. Active as [Penicillin amidase], with EC number [3.5.1.11]. Structure known Active Sites: CAA and CAT. Full crystallographic information is available from [OCA].
Reference
Ligand-induced conformational change in penicillin acylase., Done SH, Brannigan JA, Moody PC, Hubbard RE, J Mol Biol. 1998 Nov 27;284(2):463-75. PMID:9813130
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