Role of the Essential Thiol Groups of Yeast Alcohol Dehydrogenase

Overview

Journal Biochem J

Specialty Biochemistry

Date 1972 Jan 1

PMID 4342383

Citations 10

Authors

F M Dickinson

Affiliations

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Abstract

1. Yeast alcohol dehydrogenase inactivated by reaction with iodoacetamide retains 85% of the original NADH-binding capacity as measured under conditions of saturating coenzyme concentration. 2. The dissociation constant of the enzyme-NADH complex is unaffected by inactivation of the enzyme with iodoacetamide, and the affinity of the enzyme for NAD(+) and pyridine-3-aldehyde-adenine dinucleotide (PAAD(+)) appears to be similarly unaffected. 3. Enzyme inactivated with iodoacetamide has lost the ability to form normal ternary complexes of the type enzyme-NADH-acetamide and enzyme-PAAD(+)-hydroxylamine that are characteristic of the native enzyme.

Citing Articles

A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates.

Dickinson F, Monger G Biochem J. 1973; 131(2):261-70.

PMID: 4352908 PMC: 1177466. DOI: 10.1042/bj1310261.

A study of the pH- and temperature-dependence of the reactions of yeast alcohol dehydrogenase with ethanol, acetaldehyde and butyraldehyde as substrates.

Dickenson C, Dickinson F Biochem J. 1975; 147(2):303-11.

PMID: 241323 PMC: 1165444. DOI: 10.1042/bj1470303.

Estimation of rate and dissociation constants involving ternary complexes in reactions catalysed by yeast alcohol dehydrogenase.

Dickinson F, Dickenson C Biochem J. 1978; 171(3):629-37.

PMID: 208510 PMC: 1184007. DOI: 10.1042/bj1710629.

Inhibition by ethanol, acetaldehyde and trifluoroethanol of reactions catalysed by yeast and horse liver alcohol dehydrogenases.

Dickenson C, Dickinson F Biochem J. 1978; 171(3):613-27.

PMID: 208509 PMC: 1184006. DOI: 10.1042/bj1710613.

The reactions of 1,10-phenanthroline with yeast alcohol dehydrogenase.

Dickinson F, Berrieman S Biochem J. 1977; 167(1):237-44.

PMID: 201246 PMC: 1183641. DOI: 10.1042/bj1670237.

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