A novel NADPH/NADH-dependent aldehyde reduction enzyme isolated from the tapeworm Moniezia expansa.
An aldehyde reduction enzyme has been purified from the cytosol of the tapeworm, Moniezia expansa, by chromatofocusing and Reactive-Red chromatography. The enzyme is monomeric (subunit 34 kDa) and can utilise NADH and NADPH as co-factors. Substrates of the enzyme include alkanals, alka-2,4-dienals and alk-2-enals, established secondary products of lipid peroxidation. The enzyme reduced methylglyoxal, another possible natural substrate (M. expansa lacks glyoxalase I activity). The parasite enzyme may help form a final line of defence against cytotoxic aldehydes arising from host immune initiated lipid peroxidation.
Brophy
P M
PM
Department of Biological Science, University College of Wales, Aberystwyth, UK.
Crowley
P
P
Barrett
J
J
D000429:Alcohol Oxidoreductases / Q000302:isolation & purification*; D000818:Animals; D002589:Cestoda / Q000201:enzymology*; D002845:Chromatography; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D007525:Isoelectric Focusing; D013379:Substrate Specificity
D000429:Alcohol Oxidoreductases; C019642:alcohol dehydrogenase (NADP+)