Molecular mechanism of autocatalytic processing of γ-glutamyltranspeptidase
| Project/Area Number |
13660090
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | KYOTO UNIVERSITY |
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Principal Investigator |
SUZUKI Hideyuki Kyoto Univ., Grad. Sch. Of Biostudies, Associate Prof., 生命科学研究科, 助教授 (10202136)
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| Project Period (FY) |
2001 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2002: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2001: ¥2,300,000 (Direct Cost: ¥2,300,000)
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| Keywords | glutathione / γ-glutamyltransferase / γ-glutamyltranspeptidase / autocatalytic processing / processing / post-translational processing / プロセッシング |
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| Research Abstract |
γ-Glutamyltranspeptidase is the key enzyme in glutathione metabolism and we previously presented evidence suggesting that it belongs to the N-terminal nucleophile hydrolase superfamily. Enzymatically active γ-glutamyltranspeptidase, which consists of one large subunit and one small subunit, is generated from an inactive common precursor through post-translational proteolytic processing. The processing mechanism for γ-glutamyltranspeptidase of Escherichia coli K-12 has been analyzed by means of in vitro studies using purified precursors. We here show that the processing of a precursor of γ-glutamyltranspeptidase is an intramolecular autocatalytic event and that the catalytic nucleophile for the processing reaction is the oxygen atom of the side-chain of Thr-391 (N-terminal residue of the small (β) subunit), which is also the nucleophile for the enzymatic reaction.
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Report
(3 results)
Research Products
(23 results)
