Unusual Enzymatic Hydrolysis of NAD by Solubilized Form of NAD〔+〕 Glycohydrolase

• Tono-oka Shuichi

  Division of Molecular Oncology, Institute for Genetic Medicine, Hokkaido University

• Hatakeyama Masanori

  Division of Molecular Oncology, Institute for Genetic Medicine, Hokkaido University

書誌事項

タイトル別名

• Unusual Enzymatic Hydrolysis of NAD by Solubilized Form of NAD+ Glycohydrolase.

抄録

Using solubilized form (sNADase) of membrane-bound porcine brain NAD⁺ glycohydrolase (pNADase), the NADase-catalyzed hydrolysis and transglycosidation reactions of NAD (1) were examined. Unexpectedly, products in the reactions were found to be nicotinamide (5′-O-diphosphono)-β-D-ribofuranoside (4) and adenosine (5). Adenosine 5′-diphosphate (ADP)-ribose (2) and nicotinamide (3) as well as a transglycosylated product, which are formed in a usual NAD/pNADase reaction system, were scarcely produced in the NAD/sNADase system. Setting aside the mechanical aspects of this unusual cleaving, it is quite interesting that the sNADase-catalyzed hydrolytic reaction of NAD resulted in the selective cleavage of the P–O bond of the adenosine side without the appreciable hydrolysis of the labile quaternary nicotinamide-ribose pyridinium linkage.

収録刊行物

• ＣＨＥＭＩＣＡＬ　＆　ＰＨＡＲＭＡＣＥＵＴＩＣＡＬ　ＢＵＬＬＥＴＩＮ

  ＣＨＥＭＩＣＡＬ　＆　ＰＨＡＲＭＡＣＥＵＴＩＣＡＬ　ＢＵＬＬＥＴＩＮ 50 (6), 831-833, 2002

  公益社団法人 日本薬学会

キーワード

• membrane-bound particulate NADase
• solubilized NADase
• NAD
• site-selective phosphatase-like activity

詳細情報

• CRID: 1390001204164176768
• NII論文ID: 110003616252
• NII書誌ID: AA00602100
• DOI: 10.1248/cpb.50.831
• COI: 1:CAS:528:DC%2BD38XkvFOltLo%3D
• ISSN: 13475223
• ISSN: 00092363
• NDL書誌ID: 6177689
• PubMed: 12045341
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I6177689
• Web Site: http://www.jstage.jst.go.jp/article/cpb/50/6/50_6_831/_pdf
• 本文言語コード: en
• データソース種別:
  • JaLC
  • NDL
  • Crossref
  • PubMed
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可