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.
Tono-oka
S
S
Section of Chemistry, Institute of Immunological Science, Hokkaido University, Sapporo, Japan. tonny@imm.hokudai.ac.jp
Azuma
I
I
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