1jw0
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(New page: 200px<br /><applet load="1jw0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jw0, resolution 2.5Å" /> '''Structure of cephalos...)
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Revision as of 16:30, 20 November 2007
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Structure of cephalosporin acylase in complex with glutarate
Overview
BACKGROUND: Semisynthetic cephalosporins are primarily synthesized from, 7-aminocephalosporanic acid (7-ACA), which is obtained by environmentally, toxic chemical deacylation of cephalosporin C (CPC). Thus, the enzymatic, conversion of CPC to 7-ACA by cephalosporin acylase (CA) would be of great, interest. However, CAs use glutaryl-7-ACA (GL-7-ACA) as a primary, substrate and the enzyme has low turnover rates for CPC. RESULTS: The, binary complex structures of CA with GL-7-ACA and glutarate (the, side-chain of GL-7-ACA) show extensive interactions between the glutaryl, moiety of GL-7-ACA and the seven residues that form the side-chain pocket., These interactions explain why the D-alpha-aminoadipyl side-chain of CPC, yields a poorer substrate than GL-7-ACA. CONCLUSIONS: This understanding, of the nature of substrate specificity may be useful in the design of an, enzyme with an improved performance for the conversion of CPC to 7-ACA., Additionally, the catalytic mechanism of the deacylation reaction was, revealed by the ligand bound structures.
About this Structure
1JW0 is a Protein complex structure of sequences from Brevundimonas diminuta with GUA as ligand. Full crystallographic information is available from OCA.
Reference
Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity., Kim Y, Hol WG, Chem Biol. 2001 Dec;8(12):1253-64. PMID:11755403
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