Terminal diols as efficient substrates for transglycosylational activity of NAD glycohydrolase.
Linear terminal alkane-diols have been shown to function as more efficient substrates of the transglycosylational activity of NAD+ glycohydrolase (NADase) than the corresponding respective 1-alkanols. A series of eight alkane-diols from ethane-1,2- to nonane-1,9-diols underwent an O-ADP-ribosylation in the incubation reaction with NAD/NADase to provide the corresponding ribosylated products. The structural properties of these products were characterized by 1H NMR and MS spectrometries. No substantial double ADP-ribosylation of the two hydroxy functions was observed which was initially expected in the diols of higher carbon number.
Section of Chemistry, Institute of Immunological Science, Hokkaido University, Sapporo, Japan. tonny@imm.hokudai.ac.jp
S
S
Tono-oka
I
I
Azuma
D000438:Alcohols / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D006031:Glycosylation; D009682:Magnetic Resonance Spectroscopy; D009244:NAD+ Nucleosidase / Q000378:metabolism*; D016339:Spectrometry, Mass, Fast Atom Bombardment; D013379:Substrate Specificity
D000438:Alcohols; D009244:NAD+ Nucleosidase