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Publication Abstract from PubMed

Cephalosporin acylase (CA), a member of the N-terminal nucleophile hydrolase family, is activated through two steps of intramolecular autoproteolysis, the first mediated by a serine residue, and the second by a glutamate, which releases the pro-segment and produces an active enzyme. In this study, we have determined the crystal structures of mutants which could affect primary or secondary auto-cleavage and of sequential intermediates of a slow-processing mutant at 2.0-2.5A resolutions. The pro-segments of the mutants undergo dynamic conformational changes during activation and adopt surprisingly different loop conformations from one another. However, the autoproteolytic site was found to form a catalytically competent conformation with a solvent water molecule, which was essentially conserved in the CA mutants.

Structural features of cephalosporin acylase reveal the basis of autocatalytic activation.,Cho KJ, Kim JK, Lee JH, Shin HJ, Park SS, Kim KH Biochem Biophys Res Commun. 2009 Dec 11;390(2):342-8. Epub 2009 Oct 2. PMID:19800869^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.