Molecular dissection of Streptomyces trypsin on the recognition mechanism of structural protein substrates

KAKEN

About This Project

Japan Grant Number
JP21750183 (JGN)
Funding Program
Grants-in-Aid for Scientific Research
Funding Organization
Japan Society for the Promotion of Science

Kakenhi Information

Project/Area Number
21750183
Research Category
Grant-in-Aid for Young Scientists (B)
Allocation Type
  • Single-year Grants
Review Section / Research Field
  • Science and Engineering > Chemistry > Applied Chemistry > Chemistry related to living body
Research Institution
  • Kyoto University
Project Period (FY)
2009 〜 2010
Project Status
Completed
Budget Amount*help
4,550,000 Yen (Direct Cost: 3,500,000 Yen Indirect Cost: 1,050,000 Yen)

Research Abstract

Serine proteases have recently received much attention in relation to degradation of recalcitrant animal proteins, such as collagen, keratin, blood clots, and amyloid prion proteins for beneficial use of industrial waste and medical applications. In this study, a serine protease from Streptomyces omiyaensis (SOT), which is a trypsin-like enzyme, was chosen as a model enzyme for clarifying the recognition mechanism of structural protein substrates in serine proteases. We constructed chimeras between SOT and SGT using an in vivo DNA shuffling system and several mutants to identify the key residues involved in topological specificities. By comparing substrate specificities of chimeras and mutants, we found that residues 71 and 72 of SOT contribute to topological specificity and collagen binding, respectively. Furthermore, we found that Lys217 and Ala221 of SOT, which is located in the C-terminal α-helix domain, as a crucial residues for fibrinolysis.

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