Structure and Reaction Mechanism of γ-Glutamyltranspeptidases

• FUKUYAMA Keiichi

  Department of Biological Sciences, Graduate School of Science, Osaka University Present address: Department of Applied Chemistry, Graduate School of Engineering, Osaka University

• WADA Kei

  Organization for Promotion of Tenure Track, University of Miyazaki

Bibliographic Information

Other Title

• γ-グルタミルトランスペプチダーゼの立体構造と特異的反応
• g-グルタミルトランスペプチダーゼ ノ リッタイ コウゾウ ト トクイテキ ハンノウ

Abstract

γ-Glutamyltranspeptidase（GGT） is a heterodimic enzyme that undergoes post-translational processing and catalyzes the hydrolysis of γ-glutamyl bond in such compounds as glutathione and/or the transfer of the γ-glutamyl group to other amino acids and peptides. We have determined the several crystal structures of GGT orthologs and their complex structures with the substrate/product and inhibitors as well as GGT precursor. These structures demonstrate the mechanism of the maturation, catalytic reaction and substrate recognition of GGT.

Journal

• Nihon Kessho Gakkaishi

  Nihon Kessho Gakkaishi 55 (6), 340-344, 2013

  The Crystallographic Society of Japan

Details

• CRID: 1390282679065687808
• NII Article ID: 130003386011
• NII Book ID: AN00188364
• DOI: 10.5940/jcrsj.55.340
• ISSN: 18845576
• ISSN: 03694585
• NDL BIB ID: 025122619
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I025122619
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed