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1
Partial reversal of the acetaldehyde and butyraldehyde oxidation reactions catalysed by aldehyde dehydrogenases from sheep liver.绵羊肝脏醛脱氢酶催化的乙醛和丁醛氧化反应的部分逆转
Biochem J. 1978 Nov 1;175(2):753-6. doi: 10.1042/bj1750753.
2
Kinetic properties of aldehyde dehydrogenase from sheep liver mitochondria.绵羊肝脏线粒体中醛脱氢酶的动力学特性
Biochem J. 1978 Dec 1;175(3):899-908. doi: 10.1042/bj1750899.
3
Steady-state and pre-steady kinetic studies on mitochondrial sheep liver aldehyde dehydrogenase. A comparison with the cytoplasmic enzyme.线粒体绵羊肝脏醛脱氢酶的稳态和预稳态动力学研究。与细胞质酶的比较。
Biochem J. 1978 Jun 1;171(3):527-31. doi: 10.1042/bj1710527.
4
Proton release during the pre-steady-state oxidation of aldehydes by aldehyde dehydrogenase. Evidence for a rate-limiting conformational change.醛脱氢酶对醛进行预稳态氧化过程中的质子释放。限速构象变化的证据。
Biochemistry. 1982 Aug 31;21(18):4407-13. doi: 10.1021/bi00261a033.
5
Kinetic properties of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase.绵羊肝脏细胞质醛脱氢酶高度纯化制剂的动力学特性
Biochem J. 1982 Jun 1;203(3):617-27. doi: 10.1042/bj2030617.
6
Evidence that the cytoplasmic aldehyde dehydrogenase-catalysed oxidation of aldehydes involves a different active-site group from that which catalyses the hydrolysis of 4-nitrophenyl acetate.有证据表明，细胞质醛脱氢酶催化的醛氧化反应所涉及的活性位点基团与催化4-硝基苯乙酸水解的活性位点基团不同。
Biochem J. 1988 Sep 15;254(3):903-6. doi: 10.1042/bj2540903.
7
Regulatory factors of acetaldehyde metabolism in isolated rat liver mitochondria.大鼠离体肝线粒体中乙醛代谢的调节因子
Adv Exp Med Biol. 1977;85A:203-24. doi: 10.1007/978-1-4899-5181-6_14.
8
Purification and properties of sheep-liver aldehyde dehydrogenases.绵羊肝脏醛脱氢酶的纯化及性质
Eur J Biochem. 1979 Jun 1;96(3):585-95. doi: 10.1111/j.1432-1033.1979.tb13073.x.
9
Kinetics of sheep-liver cytoplasmic aldehyde dehydrogenase.
Eur J Biochem. 1977 Jul 1;77(1):93-100. doi: 10.1111/j.1432-1033.1977.tb11645.x.
10
Kinetics and specificity of human liver aldehyde dehydrogenases toward aliphatic, aromatic, and fused polycyclic aldehydes.人肝脏醛脱氢酶对脂肪族、芳香族和稠合多环醛的动力学及特异性
Biochemistry. 1996 Apr 9;35(14):4457-67. doi: 10.1021/bi9521102.

引用本文的文献

1
Kinetic properties of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase.绵羊肝脏细胞质醛脱氢酶高度纯化制剂的动力学特性
Biochem J. 1982 Jun 1;203(3):617-27. doi: 10.1042/bj2030617.
2
The coenzyme-binding characteristics of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase.绵羊肝脏细胞质醛脱氢酶高度纯化制剂的辅酶结合特性
Biochem J. 1983 May 1;211(2):363-71. doi: 10.1042/bj2110363.
3
Aldehyde dehydrogenase. An enzyme with two distinct catalytic activities at a single type of active site.醛脱氢酶。一种在单一类型活性位点具有两种不同催化活性的酶。
Biochem J. 1985 Aug 15;230(1):261-7. doi: 10.1042/bj2300261.
4
Evidence that the slow conformation change controlling NADH release from the enzyme is rate-limiting during the oxidation of propionaldehyde by aldehyde dehydrogenase.有证据表明，在丙醛被醛脱氢酶氧化的过程中，控制NADH从该酶释放的缓慢构象变化是限速步骤。
Biochem J. 1987 Mar 15;242(3):803-8. doi: 10.1042/bj2420803.
5
Evidence that the cytoplasmic aldehyde dehydrogenase-catalysed oxidation of aldehydes involves a different active-site group from that which catalyses the hydrolysis of 4-nitrophenyl acetate.有证据表明，细胞质醛脱氢酶催化的醛氧化反应所涉及的活性位点基团与催化4-硝基苯乙酸水解的活性位点基团不同。
Biochem J. 1988 Sep 15;254(3):903-6. doi: 10.1042/bj2540903.
6
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.绵羊肝细胞质醛脱氢酶作用机制的研究。pH对醛结合反应的影响以及对该机制中质子释放位点问题的重新审视。
Biochem J. 1986 Aug 15;238(1):75-82. doi: 10.1042/bj2380075.
7
2,2'-Dithiodipyridine activates aldehyde dehydrogenase and protects the enzyme against inactivation by disulfiram.2,2'-二硫代二吡啶激活醛脱氢酶，并保护该酶免受双硫仑的失活作用。
Biochem J. 1979 Dec 1;183(3):751-3. doi: 10.1042/bj1830751.
8
Reversal of part of the aldehyde dehydrogenase reaction pathway during the hydrolysis of an ester.酯水解过程中醛脱氢酶反应途径部分的逆转。
Biochem J. 1979 Nov 1;183(2):459-62. doi: 10.1042/bj1830459.

本文引用的文献

1
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.
2
The stereospecificity of enzymatic hydrogen transfer from diphosphopyridine nucleotide.二磷酸吡啶核苷酸的酶促氢转移的立体特异性。
J Biol Chem. 1957 Sep;228(1):85-96.
3
The oxidation of acetaldehyde to acetyl coenzyme A.乙醛氧化为乙酰辅酶A。
J Biol Chem. 1953 Jun;202(2):873-90.
4
Intracellular localisation and properties of aldehyde dehydrogenases from sheep liver.绵羊肝脏中醛脱氢酶的细胞内定位及特性
Biochim Biophys Acta. 1974 May 20;350(1):121-8. doi: 10.1016/0005-2744(74)90209-5.
5
Horse liver aldehyde dehydrogenase. II. Kinetics and mechanistic implications of the dehydrogenase and esterase activity.马肝醛脱氢酶。II. 脱氢酶和酯酶活性的动力学及机制意义。
J Biol Chem. 1972 Jan 10;247(1):267-72.
6
Steady-state and pre-steady kinetic studies on mitochondrial sheep liver aldehyde dehydrogenase. A comparison with the cytoplasmic enzyme.线粒体绵羊肝脏醛脱氢酶的稳态和预稳态动力学研究。与细胞质酶的比较。
Biochem J. 1978 Jun 1;171(3):527-31. doi: 10.1042/bj1710527.
7
Some properties of aldehyde dehydrogenase from sheep liver mitochondria.绵羊肝线粒体醛脱氢酶的一些特性
Biochem J. 1977 May 1;163(2):261-7. doi: 10.1042/bj1630261.
8
The action of progesterone and diethylstilboestrol on the dehydrogenase and esterase activities of a purified aldehyde dehydrogenase from rabbit liver.孕酮和己烯雌酚对兔肝纯化醛脱氢酶脱氢酶和酯酶活性的作用。
Biochem J. 1977 Jan 1;161(1):123-30. doi: 10.1042/bj1610123.
9
Pre-steady-state kinetic studies on cytoplasmic sheep liver aldehyde dehydrogenase.细胞质绵羊肝脏醛脱氢酶的预稳态动力学研究。
Biochem J. 1977 Nov 1;167(2):469-77. doi: 10.1042/bj1670469.
10
Kinetics of sheep-liver cytoplasmic aldehyde dehydrogenase.
Eur J Biochem. 1977 Jul 1;77(1):93-100. doi: 10.1111/j.1432-1033.1977.tb11645.x.

绵羊肝脏醛脱氢酶催化的乙醛和丁醛氧化反应的部分逆转

Partial reversal of the acetaldehyde and butyraldehyde oxidation reactions catalysed by aldehyde dehydrogenases from sheep liver.

作者信息

Hart G J, Dickinson F M

出版信息

Biochem J. 1978 Nov 1;175(2):753-6. doi: 10.1042/bj1750753.

DOI:10.1042/bj1750753
PMID:217349
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1186126/
Abstract

In the presence of acetic anhydride or butyric anhydride, liver aldehyde dehydrogenases catalyse the oxidation of NADH at pH 7.0 and 25 degrees C. The maximum velocities and Michaelis constants for NADH at saturating anhydride concentrations are independent of which anhydride is used, the values being V'max. = 12 min-1 and Km for NADH = 9 micrometer for the mitochondrial enzyme and V'max = 25 min-1 and Km for NADH = 20 micrometer for the cytoplasmic enzyme. Substitution of [4A-2H]NADH for NADH resulted in 2-fold and 4-fold decreases in rate for the mitochondrial and cytoplasmic enzymes respectively.

摘要

在乙酸酐或丁酸酐存在的情况下，肝脏醛脱氢酶在pH 7.0和25℃时催化NADH的氧化。在饱和酸酐浓度下，NADH的最大反应速度和米氏常数与使用哪种酸酐无关，线粒体酶的值为V'max = 12 min-1，NADH的Km = 9微摩尔；细胞质酶的值为V'max = 25 min-1，NADH的Km = 20微摩尔。用[4A-2H]NADH替代NADH后，线粒体酶和细胞质酶的反应速率分别降低了2倍和4倍。