Structural features of cephalosporin acylase reveal the basis of autocatalytic activation
- Authors
- Cho, Ki Joon; Kim, Jin Kwang; Lee, Ji-Hye; Shin, Hye Jeong; Park, Sung Soo; Kim, 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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Collections - Graduate School > Department of Biotechnology and Bioinformatics > 1. Journal Articles
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