Kinetic properties of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase.
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The action of cytoplasmic aldehyde dehydrogenase on methyl p-nitrophenyl carbonate and p-nitrophenyl dimethylcarbamateThe binding of NADH to cytoplasmic aldehyde dehydrogenase after modification with p-nitrophenyl dimethylcarbamateCharacterization of E. coli tetrameric aldehyde dehydrogenases with atypical properties compared to other aldehyde dehydrogenases.Biophysical studies of an NAD(P)(+)-dependent aldehyde dehydrogenase from Bacillus licheniformis.Gene cloning and biochemical characterization of a NAD(P)+ -dependent aldehyde dehydrogenase from Bacillus licheniformis.Effect of pyrophosphate ions and alkaline pH on the kinetics of propionaldehyde oxidation by sheep liver cytosolic aldehyde dehydrogenase.Effects of Mg2+, Ca2+ and Mn2+ on sheep liver cytoplasmic aldehyde dehydrogenase.Effect of disulfiram on the pre-steady-state burst in the reactions of sheep liver cytoplasmic aldehyde dehydrogenase.Aldehyde dehydrogenase. An enzyme with two distinct catalytic activities at a single type of active site.The coenzyme-binding characteristics of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenaseThe effects of Mg2+ on certain steps in the mechanisms of the dehydrogenase and esterase reactions catalysed by sheep liver aldehyde dehydrogenase. Support for the view that dehydrogenase and esterase activities occur at the same site on the enzyme.Cellular distribution and properties of human blood aldehyde dehydrogenase.Steady-state kinetic analysis of aldehyde dehydrogenase from human erythrocytes.Kinetics of p-nitrophenyl pivalate hydrolysis catalysed by cytoplasmic aldehyde dehydrogenase.Studies on the mechanism of sheep liver cytosolic aldehyde dehydrogenase.Studies on the mechanism of sheep liver cytosolic aldehyde dehydrogenase. The effect of pH on the aldehyde binding reactions and a re-examination of the problem of the site of proton release in the mechanism.Evidence that the slow conformation change controlling NADH release from the enzyme is rate-limiting during the oxidation of propionaldehyde by aldehyde dehydrogenaseThe role of the metal ion in the mechanism of the K+-activated aldehyde dehydrogenase of Saccharomyces cerevisiae.Studies of the esterase activity of cytosolic aldehyde dehydrogenase with resorufin acetate as substrate.Engineering an aldehyde dehydrogenase toward its substrates, 3-hydroxypropanal and NAD+, for enhancing the production of 3-hydroxypropionic acid.
P2860
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P2860
Kinetic properties of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase.
description
1982 nî lūn-bûn
@nan
1982年の論文
@ja
1982年論文
@yue
1982年論文
@zh-hant
1982年論文
@zh-hk
1982年論文
@zh-mo
1982年論文
@zh-tw
1982年论文
@wuu
1982年论文
@zh
1982年论文
@zh-cn
name
Kinetic properties of highly p ...... lasmic aldehyde dehydrogenase.
@en
Kinetic properties of highly p ...... lasmic aldehyde dehydrogenase.
@nl
type
label
Kinetic properties of highly p ...... lasmic aldehyde dehydrogenase.
@en
Kinetic properties of highly p ...... lasmic aldehyde dehydrogenase.
@nl
prefLabel
Kinetic properties of highly p ...... lasmic aldehyde dehydrogenase.
@en
Kinetic properties of highly p ...... lasmic aldehyde dehydrogenase.
@nl
P2860
P356
P1433
P1476
Kinetic properties of highly p ...... lasmic aldehyde dehydrogenase.
@en
P2093
P2860
P304
P356
10.1042/BJ2030617
P407
P577
1982-06-01T00:00:00Z