Rat hepatic microsomal aldehyde dehydrogenase. Identification of 3-and 4-substituted aromatic aldehydes as substrates of the enzyme
R Martini, M Murray
Index: Martini, Robert; Murray, Michael Chemical Research in Toxicology, 1996 , vol. 9, # 1 p. 268 - 276
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Citation Number: 10
Abstract
The rat hepatic microsomal aldehyde dehydrogenase (mALDH) metabolizes aliphatic and aromatic aldehydes to the corresponding acids with NAD as the optimal cofactor. However, dehydrogenation of the aliphatic compounds is substantially more efficient. In the present study, a series of aromatic aldehydes was evaluated as substrates of the purified mALDH so that the physicochemical factors that contribute to substrate affinity could be evaluated. ...
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