Published in Biochem J on February 01, 1973
Estimation of rate and dissociation constants involving ternary complexes in reactions catalysed by yeast alcohol dehydrogenase. Biochem J (1978) 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
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
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
Activity of yeast alcohol dehydrogenases on benzyl alcohols and benzaldehydes: characterization of ADH1 from Saccharomyces carlsbergensis and transition state analysis. Chem Biol Interact (2008) 0.90
The role of the metal ion in the mechanism of the K+-activated aldehyde dehydrogenase of Saccharomyces cerevisiae. Biochem J (1987) 0.88
A product-inhibition study of bovine liver glutamate dehydrogenase. Biochem J (1975) 0.88
Furfural reduction mechanism of a zinc-dependent alcohol dehydrogenase from Cupriavidus necator JMP134. Mol Microbiol (2011) 0.81
A new alcohol dehydrogenase, reactive towards methanol, from Bacillus stearothermophilus. Biochem J (1988) 0.80
Some properties of an alcohol dehydrogenase partially purified from baker's yeast grown without added zinc. Biochem J (1976) 0.78
Kinetics and reaction mechanism of yeast alcohol dehydrogenase with long-chain primary alcohols. Biochem J (1976) 0.75
Kinetic mechanism of pulmonary carbonyl reductase. Biochem J (1988) 0.75
Enzyme activity and substrate specificity of the major cinnamyl alcohol dehydrogenases in sorghum. Plant Physiol (2017) 0.75
A general method for the analysis of random bisubstrate enzyme mechanisms. J Ind Microbiol Biotechnol (2004) 0.75
Yeast alcohol dehydrogenase: molecular weight, coenzyme binding, and reaction equilibria. J Biol Chem (1954) 4.85
Kinetic studies of liver alcohol dehydrogenase. Biochem J (1962) 4.60
Some observations on the preparation and properties of dihydronicotinamide-adenine dinucleotide. Biochem J (1962) 2.63
The purification of nicotinamide adenine dinucleotide and kinetic effects of nucleotide impurities. J Biol Chem (1963) 2.59
The kinetics and mechanism of liver alcohol dehydrogenase with primary and secondary alcohols as substrates. Biochem J (1966) 2.30
KINETIC STUDIES OF LIVER ALCOHOL DEHYDROGENASE AND PH EFFECTS WITH COENZYME PREPARATIONS OF HIGH PURITY. J Biol Chem (1963) 2.04
EQUILIBRIUM REACTION RATES AND THE MECHANISMS OF LIVER AND YEAST ALCOHOL DEHYDROGENASE. J Biol Chem (1964) 1.76
PRODUCT INHIBITION STUDIES ON YEAST AND LIVER ALCOHOL DEHYDROGENASES. Biochemistry (1964) 1.42
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
Role of the essential thiol groups of yeast alcohol dehydrogenase. Biochem J (1972) 1.17
ISOTOPIC EXCHANGE AT EQUILIBRIUM AS A CRITERION OF ENZYMATIC MECHANISMS. Nature (1964) 1.12
Substrate activation and inhibition in coenzyme-substrate reactions cyclohexanol oxidation catalysed by liver alcohol dehydrogenase. Biochem J (1966) 1.04
Studies on the mechanism of enzyme-catalyzed oxidation reduction reactions. IV. A proposed mechanism for the over-all reaction catalyzed by liver alcohol dehydrogenase. Biochemistry (1962) 1.01
Effect of substrate structure on the rate of the catalytic step in the liver alcohol dehydrogenase mechanism. Biochemistry (1971) 0.91
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
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
Kinetic studies of the mechanism of pig kidney aldehyde reductase. Biochem J (1981) 0.86
The preparation of pure salt-free nicotinamide coenzymes. Anal Biochem (1977) 0.86
The reactions of 1,10-phenanthroline with yeast alcohol dehydrogenase. Biochem J (1977) 0.85
A study of the coenzyme-binding characteristics of rabbit muscle L-glycerol 3-phosphate dehydrogenase. Biochem J (1974) 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
Kinetic studies of the mechanism of sheep liver cytoplasmic aldehyde dehydrogenase. Prog Clin Biol Res (1982) 0.77
ATP: citrate lyase from Aspergillus nidulans. Biochem Soc Trans (1997) 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
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
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