Autolysis of a Novel Multidomain Subtilase-cold-adapted Deseasin Mcp-01 is Ph-dependent and the Surface Loops in Its Catalytic Domain, the Linker, and the P_proprotein Domain Are Susceptible to Proteolytic Attack.
From: The State Key Lab of Microbial Technology, Marine Biotechnology Research Center, Shandong University, Jinan 250100, China.
Biochemical and biophysical research communications
- Publish Date: Jul 2007
- ISSN: 0006-291X
- Volume: 358
- Issue: 3
- Pages: 704-9
- Medium: Print
- Language: English
- Citation (JAMA): Chen Xiu-Lan, Zhang Yu-Zhong, Lu Jing-Tao, et al. Autolysis of a Novel Multidomain Subtilase-cold-adapted Deseasin Mcp-01 is Ph-dependent and the Surface Loops in Its Catalytic Domain, the Linker, and the P_proprotein Domain Are Susceptible to Proteolytic Attack.. Biochem. Biophys. Res. Commun. Jul 2007;358:704-9
Abstract
Cold-adapted deseasin MCP-01 is a novel type subtilase with a multidomain structure containing a catalytic domain, a linker, a P_proprotein domain, and a PKD domain. Its autolysis was pH-dependent due to its flexible structure. N-terminal sequence analysis of the autolytic peptides revealed four autolytic sites in the catalytic domain. Three of these are in the same loops as mesophilic subtilases and one is unlike anything previously reported. Two autolytic sites were deduced in its linker and three in its P_proprotein domain, indicating the linker and the P_proprotein domain are flexible and susceptible to proteolytic attacks. Therefore, during MCP-01 autolysis, the linker and the P_proprotein domain of MCP-01 were easily attacked by proteolysis, resulting in cleavage of the C-terminal region. At the same time, some autolytic sites in the surface loops of the catalytic domain were cleaved. This is the first report describing the autolytic mechanism of a multidomain subtilase.
Mesh Headings (Keywords): Amino Acid Sequence, Binding Sites, Buffers, Catalytic Domain, Cold, Endopeptidases, Hydrogen-Ion Concentration, Molecular Sequence Data, Peptides, Protein Conformation, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Subtilisins, Surface Properties, Time Factors
Check for Full Text / PubMed Unique Identifier (PMID): 17506991
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.