Open AccessThe NADP‐linked aldehyde reductase from Trypanosoma cruzi subcellular localization and some properties
Author(s) -
Arauzo Silvia,
Cazzulo Juan José
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03060.x
Subject(s) - iodoacetamide , propionaldehyde , digitonin , trypanosoma cruzi , biochemistry , chemistry , reductase , enzyme , aldehyde oxidase , cofactor , aldehyde , catalysis , cysteine , parasite hosting , world wide web , computer science , xanthine oxidase
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 by 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.