X-ray Crystal Structure of Catechol 2,3-Dioxygenase (Metapyrocatechase).

• KITA Akiko

  京都大学大学院理学研究科

• MIKI Kunio

  京都大学大学院理学研究科

Bibliographic Information

Other Title

• カテコール２，３‐ジオキシゲナーゼ（メタピロカテカーゼ）の結晶構造
• サイキン ノ ケンキュウ カラ カテコール 2 3 ジオキシゲナーゼ メタピロカテカーゼ ノ ケッショウ コウゾウ

Abstract

The three-dimensional structure of catechol 2, 3-dioxygenases (metapyrocatechase, MPC), which catalyzes the proximal extradiol cleavage reaction of catechol and 3- or 4-substituted catechol, has been determined at 2.8Å resolution. The enzyme is a homotetramer with non-crystallographic 222 symmetry and each subunit is folded into two similar domains. The active site structure reveals a distorted tetrahedral Fe (II) site coordinated by three endogenous ligands (His 153, His214, and G1u265) and an acetone molecule.

Journal

• Nihon Kessho Gakkaishi

  Nihon Kessho Gakkaishi 42 (4), 361-366, 2000

  The Crystallographic Society of Japan

Details

• CRID: 1390001204087592320
• NII Article ID: 10004673753
• NII Book ID: AN00188364
• DOI: 10.5940/jcrsj.42.361
• ISSN: 18845576
• ISSN: 03694585
• NDL BIB ID: 5466853
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I5466853
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed