Unusual Enzymatic Hydrolysis of NAD by Solubilized Form of NAD^+ Glycohydrolase

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概要

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• 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.

• 公益社団法人日本薬学会の論文
• 2002-06-01

著者

• Hatakeyama Masanori

  Division Of Molecular Oncology Institute For Genetic Medicine And Division Of Chemistry Graduate Sch

• Tono-oka Shuichi

  Division Of Molecular Oncology Institute For Genetic Medicine Hokkaido University

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