NAD(P) glycohydrolase deficiency in human erythrocytes and alteration of cytosol NADH-methemoglobin diaphorase by membrane NAD-glycohydrolase activity.
Erythrocytic NADH methemoglobin diaphorase acquires NADH-dichlorophenolindophenol diaphorase activity when enzyme-associated NAD is removed. This transformation is reversible and can be mediated by membrane NAD glycohydrolase (EC 3.2.2.5) in hemolysates as well as in intact cells exposed to hydrogen peroxide. It is abolished either in NADH methemoglobin diaphorase deficiency or in NAD(P) glycohydrolase (EC 3.2.2.6) deficiency which is common in Afro-American but not in European-American adults. Activities of erythrocytic NADP glycohydrolase and NAD glycohydrolase appear to depend on a single membrane enzyme.
D002462:Cell Membrane / Q000201:enzymology; D003600:Cytosol / Q000201:enzymology*; D008058:Dihydrolipoamide Dehydrogenase / Q000097:blood*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004912:Erythrocytes / Q000166:cytology / Q000201:enzymology*; D006801:Humans; D008706:Methemoglobin; D009699:N-Glycosyl Hydrolases / Q000097:blood*; D009243:NAD / Q000097:blood
D009243:NAD; D008706:Methemoglobin; D008058:Dihydrolipoamide Dehydrogenase; D009699:N-Glycosyl Hydrolases