Crystal Structure of Diol Dehydratase Reveals a New Mode of B12 Binding and the Mechanism of Activation.

• SHIBATA Naoki

  Department of Life Science Faculty of Science Himeji Institute of Technology

• YASUOKA Noritake

  Department of Life Science Faculty of Science Himeji Institute of Technology

Bibliographic Information

Other Title

• 新規のビタミンＢ１２結合様式を持つジオールデヒドラターゼの立体構造と補酵素活性化機構
• サイキン ノ ケンキュウ カラ シンキ ノ ビタミン B12 ケツゴウ ヨウシキ オ モツ ジオールデヒドラターゼ ノ リッタイ コウゾウ ト ホ コウソ カッセイカ キコウ

Abstract

Diol dehydratase is an adenosylcobalamin-dependant enzyme that catalyzes conversion from 1, 2-diol compounds to corresponding aldehydes. The crystal structure of the enzyme shows that B₁₂ compounds are incorporated with the DBI-on mode. The enzyme has a potassium ion at the active site, where the substrate coordinates to it. The structure of the enzyme complexed with adeninylpentylcobalamin reveals the activation mechanism of adenosylcobalamin.

Journal

• Nihon Kessho Gakkaishi

  Nihon Kessho Gakkaishi 42 (4), 354-360, 2000

  The Crystallographic Society of Japan

Details

• CRID: 1390282679064302592
• NII Article ID: 10004673743
• NII Book ID: AN00188364
• DOI: 10.5940/jcrsj.42.354
• ISSN: 18845576
• ISSN: 03694585
• NDL BIB ID: 5466840
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I5466840
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed