The NADP-linked aldehyde reductase from Trypanosoma cruzi: subcellular localization and some properties.
NADP-linked aldehyde reductase (AR; EC 1.1.1.2), partially purified from epimastigotes of Trypanosoma cruzi, was able to reduce a number of aldehydes and to oxidize several alcohols; propionaldehyde and n-propanol were the best substrates, at optimal pH values of 7 to 8, and 9 to 9.5, respectively. The AR was inhibited p-chloromercuribenzoate and iodoacetamide, but not by 1,10-phenanthroline or barbital. Digitonin treatment of whole epimastigotes, and distribution and latency in subcellular fractions, indicated that the AR is cytosolic. Like other ARs, the T. cruzi enzyme might be involved in detoxication processes, instead of coenzyme re-oxidation.
Arauzo
S
S
Instituto de Investigaciones Bioquímicas Fundación Campomar, Buenos Aires, Argentina.
Cazzulo
J J
JJ
D000429:Alcohol Oxidoreductases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D002729:Chloromercuribenzoates / Q000494:pharmacology; D007700:Kinetics; D013347:Subcellular Fractions / Q000201:enzymology; D013379:Substrate Specificity; D014349:Trypanosoma cruzi / Q000201:enzymology*; D020245:p-Chloromercuribenzoic Acid
D002729:Chloromercuribenzoates; D020245:p-Chloromercuribenzoic Acid; D000429:Alcohol Oxidoreductases; C019642:alcohol dehydrogenase (NADP+)