Published in Biochem J on August 15, 1986
The action of cytoplasmic aldehyde dehydrogenase on methyl p-nitrophenyl carbonate and p-nitrophenyl dimethylcarbamate. Biochem J (1989) 0.92
The role of the metal ion in the mechanism of the K+-activated aldehyde dehydrogenase of Saccharomyces cerevisiae. Biochem J (1987) 0.88
The binding of NADH to cytoplasmic aldehyde dehydrogenase after modification with p-nitrophenyl dimethylcarbamate. Biochem J (1989) 0.80
Kinetic studies of liver alcohol dehydrogenase. Biochem J (1962) 4.60
Some properties of aldehyde dehydrogenase from sheep liver mitochondria. Biochem J (1977) 2.12
Kinetics of sheep-liver cytoplasmic aldehyde dehydrogenase. Eur J Biochem (1977) 2.00
Pre-steady-state kinetic studies on cytoplasmic sheep liver aldehyde dehydrogenase. Biochem J (1977) 1.66
Purification and properties of sheep-liver aldehyde dehydrogenases. Eur J Biochem (1979) 1.53
Kinetic properties of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase. Biochem J (1982) 1.50
The coenzyme-binding characteristics of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase. Biochem J (1983) 1.23
Partial reversal of the acetaldehyde and butyraldehyde oxidation reactions catalysed by aldehyde dehydrogenases from sheep liver. Biochem J (1978) 1.21
Studies on the mechanism of sheep liver cytosolic aldehyde dehydrogenase. Biochem J (1985) 1.18
Proton release during the pre-steady-state oxidation of aldehydes by aldehyde dehydrogenase. Evidence for a rate-limiting conformational change. Biochemistry (1982) 1.06
High concentrations of aldehydes slow the reaction of cytoplasmic aldehyde dehydrogenase with thiol-group modifiers. Biochem J (1985) 0.92
The kinetics and mechanism of liver alcohol dehydrogenase with primary and secondary alcohols as substrates. Biochem J (1966) 2.30
Some properties of aldehyde dehydrogenase from sheep liver mitochondria. Biochem J (1977) 2.12
The specificities and configurations of ternary complexes of yeast and liver alcohol dehydrogenases. Biochem J (1967) 1.61
Kinetic properties of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase. Biochem J (1982) 1.50
The binding of dihydronicotinamide--adenine dinucleotide and pyridine-3-aldehyde--adenine dinucleotide by yeast alcohol dehydrogenase. Biochem J (1970) 1.38
Aldehyde mutase. Nature (1965) 1.32
A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates. Biochem J (1973) 1.30
Substrate specificity and stereospecificity of alcohol dehydrogenases. Nature (1967) 1.28
The coenzyme-binding characteristics of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase. Biochem J (1983) 1.23
Partial reversal of the acetaldehyde and butyraldehyde oxidation reactions catalysed by aldehyde dehydrogenases from sheep liver. Biochem J (1978) 1.21
Effects of Mg2+, Ca2+ and Mn2+ on sheep liver cytoplasmic aldehyde dehydrogenase. Biochem J (1982) 1.19
Studies on the mechanism of sheep liver cytosolic aldehyde dehydrogenase. Biochem J (1985) 1.18
Role of the essential thiol groups of yeast alcohol dehydrogenase. Biochem J (1972) 1.17
Kinetic properties of aldehyde dehydrogenase from sheep liver mitochondria. Biochem J (1978) 1.12
Long-chain alcohol and aldehyde dehydrogenase activities in Acinetobacter calcoaceticus strain HO1-N. J Gen Microbiol (1992) 1.09
The ALD6 gene of Saccharomyces cerevisiae encodes a cytosolic, Mg(2+)-activated acetaldehyde dehydrogenase. Yeast (1997) 1.06
Purification and properties of rabbit muscle L-glycerol 3-phosphate dehydrogenase. Biochem J (1973) 1.06
Estimation of rate and dissociation constants involving ternary complexes in reactions catalysed by yeast alcohol dehydrogenase. Biochem J (1978) 1.04
Substrate activation and inhibition in coenzyme-substrate reactions cyclohexanol oxidation catalysed by liver alcohol dehydrogenase. Biochem J (1966) 1.04
A study of the pH- and temperature-dependence of the reactions of yeast alcohol dehydrogenase with ethanol, acetaldehyde and butyraldehyde as substrates. Biochem J (1975) 1.04
The role of an essential histidine residue of yeast alcohol dehydrogenase. Eur J Biochem (1975) 1.03
A study of the kinetics and mechanism of rabbit muscle L-glycerol 3-phosphate dehydrogenase. Biochem J (1974) 1.02
A study of the oxidation of butan-1-ol and propan-2-ol by nicotinamide-adenine dinucleotide catalysed by yeast alcohol dehydrogenase. Biochem J (1975) 0.95
Oxidation of medium-chain acyl-CoA esters by extracts of Aspergillus niger: enzymology and characterization of intermediates by HPLC. Microbiology (1999) 0.94
A study of the ionic properties of the essential histidine residue of yeast alcohol dehydrogenase in complexes of the enzyme with its coenzymes and substrates. Biochem J (1977) 0.94
Some properties of pig kidney-cortex aldehyde reductase. Biochem J (1980) 0.93
Inhibition by ethanol, acetaldehyde and trifluoroethanol of reactions catalysed by yeast and horse liver alcohol dehydrogenases. Biochem J (1978) 0.92
Identification and disruption of the gene encoding the K(+)-activated acetaldehyde dehydrogenase of Saccharomyces cerevisiae. FEMS Microbiol Lett (1998) 0.91
Studies on carbon monoxide binding by shark haemoglobin. Biochem J (1981) 0.89
The removal of cytosolic-type aldehyde dehydrogenase from preparations of sheep liver mitochondrial aldehyde dehydrogenase and the unusual properties of the purified mitochondrial enzyme in assays. Biochem J (1984) 0.88
The preparation of pure salt-free nicotinamide coenzymes. Anal Biochem (1977) 0.86
Kinetic studies of the mechanism of pig kidney aldehyde reductase. Biochem J (1981) 0.86
A study of the coenzyme-binding characteristics of rabbit muscle L-glycerol 3-phosphate dehydrogenase. Biochem J (1974) 0.85
The reactions of 1,10-phenanthroline with yeast alcohol dehydrogenase. Biochem J (1977) 0.85
Long-chain acyl-CoA ester intermediates of beta-oxidation of mono- and di-carboxylic fatty acids by extracts of Corynebacterium sp. strain 7E1C. Biochem J (1992) 0.84
The kinetics of ox kidney biliverdin reductase in the pre-steady state. Evidence that the dissociation of bilirubin is the rate-determining step. Biochem J (1989) 0.82
Some comparisons of pig and sheep liver cytosolic aldehyde dehydrogenases. Comp Biochem Physiol B (1989) 0.79
Some properties of an alcohol dehydrogenase partially purified from baker's yeast grown without added zinc. Biochem J (1976) 0.78
ATP: citrate lyase from Aspergillus nidulans. Biochem Soc Trans (1997) 0.77
Kinetic studies of the mechanism of sheep liver cytoplasmic aldehyde dehydrogenase. Prog Clin Biol Res (1982) 0.77
Kinetic studies of dogfish liver glutamate dehydrogenase. Biochem J (1979) 0.75
Concentration effects in assays of sheep liver mitochondrial aldehyde dehydrogenase and their interpretation in terms of enzyme dissociation. Prog Clin Biol Res (1985) 0.75
Carbonyl metabolising enzymes in alkane-grown microorganisms. Adv Exp Med Biol (1993) 0.75
Abortive complex formation and substrate activation and inhibition effects with sheep liver cytosolic aldehyde dehydrogenase. Prog Clin Biol Res (1987) 0.75
Product-inhibition studies with yeast and horse liver alcohol dehydrogenases [proceedings]. Biochem Soc Trans (1977) 0.75
Enzyme storage--to freeze or not to freeze? Biochem Soc Trans (1989) 0.75