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1
A study of the kinetics and mechanism of yeast alcohol dehydrogenase with a variety of substrates.一项关于酵母乙醇脱氢酶与多种底物的动力学及作用机制的研究。
Biochem J. 1973 Feb;131(2):261-70. doi: 10.1042/bj1310261.
2
Estimation of rate and dissociation constants involving ternary complexes in reactions catalysed by yeast alcohol dehydrogenase.酵母乙醇脱氢酶催化反应中涉及三元复合物的速率常数和解离常数的估算。
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3
A study of the oxidation of butan-1-ol and propan-2-ol by nicotinamide-adenine dinucleotide catalysed by yeast alcohol dehydrogenase.一项关于酵母醇脱氢酶催化烟酰胺腺嘌呤二核苷酸氧化正丁醇和丙醇-2的研究。
Biochem J. 1975 Jun;147(3):541-7. doi: 10.1042/bj1470541.
4
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.关于酵母乙醇脱氢酶的必需组氨酸残基在该酶与其辅酶及底物复合物中的离子性质的研究。
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5
A study of the pH- and temperature-dependence of the reactions of yeast alcohol dehydrogenase with ethanol, acetaldehyde and butyraldehyde as substrates.一项关于酵母乙醇脱氢酶以乙醇、乙醛和丁醛为底物的反应对pH值和温度依赖性的研究。
Biochem J. 1975 May;147(2):303-11. doi: 10.1042/bj1470303.
6
Kinetics and reaction mechanism of yeast alcohol dehydrogenase with long-chain primary alcohols.酵母乙醇脱氢酶与长链伯醇的动力学及反应机制
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Inhibition by ethanol, acetaldehyde and trifluoroethanol of reactions catalysed by yeast and horse liver alcohol dehydrogenases.乙醇、乙醛和三氟乙醇对酵母和马肝醇脱氢酶催化反应的抑制作用。
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Drosophila lebanonensis alcohol dehydrogenase: pH dependence of the kinetic coefficients.黎巴嫩果蝇乙醇脱氢酶:动力学系数的pH依赖性
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9
Spectroscopic investigation of binary and ternary coenzyme complexes of yeast alcohol dehydrogenase.酵母乙醇脱氢酶二元和三元辅酶复合物的光谱研究。
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10
The specificities and configurations of ternary complexes of yeast and liver alcohol dehydrogenases.酵母和肝脏乙醇脱氢酶三元复合物的特异性及构型
Biochem J. 1967 Jul;104(1):165-72. doi: 10.1042/bj1040165.

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The Thr45Gly substitution in yeast alcohol dehydrogenase substantially decreases catalysis, alters pH dependencies, and disrupts the proton relay system.酵母醇脱氢酶中的 Thr45Gly 取代显著降低了催化活性,改变了 pH 依赖性,并破坏了质子传递系统。
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8
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Development of a high-throughput assay for rapid screening of butanologenic strains.开发高通量筛选丁醇产生菌的方法。
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10
The Enzyme Activity and Substrate Specificity of Two Major Cinnamyl Alcohol Dehydrogenases in Sorghum (), SbCAD2 and SbCAD4.高粱中两种主要肉桂醇脱氢酶SbCAD2和SbCAD4的酶活性及底物特异性
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本文引用的文献

1
Studies on the mechanism of enzyme-catalyzed oxidation reduction reactions. IV. A proposed mechanism for the over-all reaction catalyzed by liver alcohol dehydrogenase.酶催化氧化还原反应机制的研究。IV. 肝脏乙醇脱氢酶催化总反应的一种 proposed 机制。 注:“proposed”在这里直接保留英文,因为不太明确其准确的中文释义在该语境下最合适的表述,需结合更专业的知识进一步确定,比如“推测的”“提出的”等。
Biochemistry. 1962 Jan;1:47-52. doi: 10.1021/bi00907a008.
2
EQUILIBRIUM REACTION RATES AND THE MECHANISMS OF LIVER AND YEAST ALCOHOL DEHYDROGENASE.平衡反应速率以及肝脏和酵母乙醇脱氢酶的作用机制
J Biol Chem. 1964 Nov;239:3908-14.
3
ISOTOPIC EXCHANGE AT EQUILIBRIUM AS A CRITERION OF ENZYMATIC MECHANISMS.平衡状态下的同位素交换作为酶作用机制的一个标准
Nature. 1964 Aug 1;203:492-4. doi: 10.1038/203492a0.
4
PRODUCT INHIBITION STUDIES ON YEAST AND LIVER ALCOHOL DEHYDROGENASES.酵母和肝脏乙醇脱氢酶的产物抑制研究
Biochemistry. 1963 Sep-Oct;2:935-41. doi: 10.1021/bi00905a007.
5
KINETIC STUDIES OF LIVER ALCOHOL DEHYDROGENASE AND PH EFFECTS WITH COENZYME PREPARATIONS OF HIGH PURITY.肝脏乙醇脱氢酶的动力学研究以及高纯度辅酶制剂的pH效应
J Biol Chem. 1963 Aug;238:2850-8.
6
The purification of nicotinamide adenine dinucleotide and kinetic effects of nucleotide impurities.烟酰胺腺嘌呤二核苷酸的纯化及核苷酸杂质的动力学效应
J Biol Chem. 1963 Apr;238:1538-43.
7
Some observations on the preparation and properties of dihydronicotinamide-adenine dinucleotide.关于二氢烟酰胺腺嘌呤二核苷酸制备及性质的一些观察
Biochem J. 1962 Aug;84(2):240-4. doi: 10.1042/bj0840240.
8
Kinetic studies of liver alcohol dehydrogenase.肝脏乙醇脱氢酶的动力学研究
Biochem J. 1962 Aug;84(2):244-54. doi: 10.1042/bj0840244.
9
Yeast alcohol dehydrogenase: molecular weight, coenzyme binding, and reaction equilibria.酵母乙醇脱氢酶:分子量、辅酶结合及反应平衡
J Biol Chem. 1954 Mar;207(1):225-44.
10
Aldehyde mutase.醛变位酶
Nature. 1965 Apr 17;206(981):255-7. doi: 10.1038/206255a0.

一项关于酵母乙醇脱氢酶与多种底物的动力学及作用机制的研究。

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

作者信息

Dickinson F M, Monger G P

出版信息

Biochem J. 1973 Feb;131(2):261-70. doi: 10.1042/bj1310261.

DOI:10.1042/bj1310261
PMID:4352908
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1177466/
Abstract
  1. The kinetics of oxidation of ethanol, propan-1-ol, butan-1-ol and propan-2-ol by NAD(+) and of reduction of acetaldehyde and butyraldehyde by NADH catalysed by yeast alcohol dehydrogenase were studied. 2. Results for the aldehyde-NADH reactions are consistent with a compulsory-order mechanism with the rate-limiting step being the dissociation of the product enzyme-NAD(+) complex. In contrast the results for the alcohol-NAD(+) reactions indicate that some dissociation of coenzyme from the active enzyme-NAD(+)-alcohol ternary complexes must occur and that the mechanism is not strictly compulsory-order. The rate-limiting step in ethanol oxidation is the dissociation of the product enzyme-NADH complex but with the other alcohols it is probably the catalytic interconversion of ternary complexes. 3. The rate constants describing the combination of NAD(+) and NADH with the enzyme and the dissociations of these coenzymes from binary complexes with the enzyme were measured.
摘要
  1. 研究了酵母醇脱氢酶催化下,NAD(+)氧化乙醇、丙醇-1、丁醇-1和丙醇-2的动力学,以及NADH还原乙醛和丁醛的动力学。2. 醛-NADH反应的结果与强制顺序机制一致,限速步骤是产物酶-NAD(+)复合物的解离。相比之下,醇-NAD(+)反应的结果表明,辅酶必须从活性酶-NAD(+)-醇三元复合物中发生一些解离,且该机制并非严格的强制顺序。乙醇氧化中的限速步骤是产物酶-NADH复合物的解离,但对于其他醇类,限速步骤可能是三元复合物的催化相互转化。3. 测量了描述NAD(+)和NADH与酶结合以及这些辅酶从与酶的二元复合物中解离的速率常数。