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Structural features of cephalosporin acylase reveal the basis of autocatalytic activation

Authors
Cho, Ki JoonKim, Jin KwangLee, Ji-HyeShin, Hye JeongPark, Sung SooKim, Kyung Hyun
Issue Date
11-Dec-2009
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords
Autoproteolysis; Precursor activation; Cephalosporin acylase; Slow-processing mutant; Intermediate structure
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.390, no.2, pp.342 - 348
Indexed
SCIE
SCOPUS
Journal Title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume
390
Number
2
Start Page
342
End Page
348
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/118750
DOI
10.1016/j.bbrc.2009.09.134
ISSN
0006-291X
Abstract
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 2.0-2.5 angstrom 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. (C) 2009 Elsevier Inc. All rights reserved.
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