Inhibition of Human Aldehyde Dehydrogenase Isozymes by Propiolaldehyde
- 1 May 1984
- journal article
- research article
- Published by Wiley in Alcohol, Clinical and Experimental Research
- Vol. 8 (3) , 302-307
- https://doi.org/10.1111/j.1530-0277.1984.tb05516.x
Abstract
Propiolaldehyde–a metabolite of pargytine (Shirota et al., 1979) can function as an inhibitor or as a substrate of human aldehyde dehydrogenase (EC 1.2.1.3), dependent on conditions. In the presence of high concentration of NAD, propiolaldehyde is a substrate for both the cytoplasmic E, isozyme and the mitochondrial E2 isozyme. The K. values are comparable to those with other short chain aldehydes; the maximal velocity is also similar for E2 but lower by about threefold for E. Preincubation with propiolaldehyde in the absence of NAD produces inactivation with K values of 1.6 μM for E, and 1.8 μ for E2. NAD, but not propanal, protects both isozymes against inactivation with propiolaldehyde.This publication has 16 references indexed in Scilit:
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