Kinetic Studies of the Mechanism of Pig Kidney Aldehyde Reductase

Overview

Journal Biochem J

Specialty Biochemistry

Date 1981 Feb 1

PMID 7030310

Citations 4

Authors

F F Morpeth

F M Dickinson

Affiliations

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Abstract

Initial-rate measurements were made of the oxidations of pyridine-3-methanol and glycerol by NADP+ and of the reduction of the corresponding aldehydes by NADPH catalysed by pig kidney aldehyde reductase. In addition, a brief survey of the specificity of the enzyme towards aldehyde substrates and its sensitivity to the inhibitors ethacrynic acid, sodium barbitone and warfarin was made. The detailed kinetic work indicates a compulsory mechanism for aldehyde reduction, with NADPH binding before aldehyde. For alcohol oxidation, however, it is necessary to postulate the formation of kinetically significant amounts of binary complexes of the type enzyme-alcohol to explain the results. Thus, for alcohol oxidation random-order addition of substrates may occur. Inhibition studies of the kinetics of aldehyde reduction in the presence of the corresponding alcohol product provide further evidence for the existence of enzyme-alcohol complexes. Finally, detailed kinetic studies were made of the inhibition of pyridine-3-aldehyde reduction by sodium barbitone. The mechanism of the inhibition is discussed.

Citing Articles

The kinetic mechanism of the major form of ox kidney aldehyde reductase with D-glucuronic acid.

Daly A, Mantle T Biochem J. 1982; 205(2):381-8.

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Purification and characterization of the multiple forms of aldehyde reductase in ox kidney.

Daly A, Mantle T Biochem J. 1982; 205(2):373-80.

PMID: 6753832 PMC: 1158490. DOI: 10.1042/bj2050373.

Kinetic mechanism of sheep liver NADPH-dependent aldehyde reductase.

De Jongh K, Schofield P, Edwards M Biochem J. 1987; 242(1):143-50.

PMID: 3593233 PMC: 1147676. DOI: 10.1042/bj2420143.

Investigation of the arylnitroso reductase activity of pig liver aldehyde reductase.

Kovar J, Plocek J Biochem J. 1986; 235(2):537-43.

PMID: 3527154 PMC: 1146718. DOI: 10.1042/bj2350537.

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