G-6-PD Walter Reed: possible insight into "structural" NADP in G-6-PD.
A new G-6-PD variant, G-6-PD Walter Reed, causing hereditary nonspherocytic hemolytic anemia is characterized. This variant is unusual in that its stability requires the presence of high concentrations of NADP, while its Km for NADP is normal. This finding is consistent with the suggestion that G-6-PD has two separate binding sites, a high affinity "structural" site and a lower affinity catalytic site. The mutation in G-6-PD Walter Reed, like that of the previously described variant, G-6-PD Torrance, may be due to a mutation of the "structural" site for NADP.
D000745:Anemia, Hemolytic, Congenital / Q000201:enzymology*; D000746:Anemia, Hemolytic, Congenital Nonspherocytic / Q000097:blood / Q000201:enzymology* / Q000235:genetics; D001665:Binding Sites; D004789:Enzyme Activation / Q000187:drug effects; D005954:Glucosephosphate Dehydrogenase / Q000235:genetics*; D006801:Humans; D007223:Infant; D007700:Kinetics; D008297:Male; D009249:NADP / Q000494:pharmacology
D009249:NADP; D005954:Glucosephosphate Dehydrogenase