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1
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Biochem J. 1986 Apr 15;235(2):537-43. doi: 10.1042/bj2350537.
2
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本文引用的文献

1
Non-inverted versus inverted plots in enzyme kinetics.酶动力学中的非反转图与反转图
Nature. 1959 Oct 24;184:1296-8. doi: 10.1038/1841296b0.
2
Fitting of enzyme kinetic data without prior knowledge of weights.在不预先了解权重的情况下对酶动力学数据进行拟合。
Biochem J. 1981 Mar 1;193(3):1005-8. doi: 10.1042/bj1931005.
3
Kinetic studies of the mechanism of pig kidney aldehyde reductase.猪肾醛还原酶作用机制的动力学研究
Biochem J. 1981 Feb 1;193(2):485-92. doi: 10.1042/bj1930485.
4
Purification and some properties of aldehyde reductases from pig liver.猪肝中醛还原酶的纯化及某些性质
Eur J Biochem. 1980 Apr;105(3):611-21. doi: 10.1111/j.1432-1033.1980.tb04539.x.
5
Investigation of a novel liver alcohol dehydrogenase catalyzed redox-elimination reaction involving arylnitroso substrate analogues.对一种涉及芳基亚硝基底物类似物的新型肝脏乙醇脱氢酶催化氧化还原消除反应的研究。
Biochemistry. 1980 Feb 19;19(4):731-8. doi: 10.1021/bi00545a019.
6
Studies on the enzymatic reduction of C-nitroso compounds. I. Distribution of c-Nitrosoreductase activity in animal tissues and partial purification of the enzyme from porcine liver.C-亚硝基化合物的酶促还原研究。I. 动物组织中C-亚硝基还原酶活性的分布及猪肝中该酶的部分纯化。
J Biochem. 1980 Sep;88(3):847-57. doi: 10.1093/oxfordjournals.jbchem.a133039.
7
A new kinetic diagnostic for enzymatic mechanisms using alternative substrates.
Anal Biochem. 1984 Sep;141(2):413-7. doi: 10.1016/0003-2697(84)90063-0.
8
Purification and properties of an NADPH-linked aldehyde reductase from rat kidney.大鼠肾脏中一种NADPH连接的醛还原酶的纯化及性质
Biochim Biophys Acta. 1983 Nov 14;748(3):444-52. doi: 10.1016/0167-4838(83)90191-7.
9
Aldose and aldehyde reductase exhibit isocorticosteroid reductase activity.醛糖和醛还原酶表现出异皮质类固醇还原酶活性。
Eur J Biochem. 1983 Mar 15;131(2):423-6. doi: 10.1111/j.1432-1033.1983.tb07280.x.
10
A new photometric assay for blood alcohol.一种新的血液酒精光度测定法。
Anal Biochem. 1984 Feb;137(1):74-9. doi: 10.1016/0003-2697(84)90349-x.

猪肝醛还原酶的芳基亚硝基还原酶活性研究。

Investigation of the arylnitroso reductase activity of pig liver aldehyde reductase.

作者信息

Kovár J, Plocek J

出版信息

Biochem J. 1986 Apr 15;235(2):537-43. doi: 10.1042/bj2350537.

DOI:10.1042/bj2350537
PMID:3527154
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1146718/
Abstract

The reduction of p-nitroso-N-dimethylaniline, p-nitroso-N-diethylaniline, p-nitrosophenol and p-nitroso-N-phenylaniline with NADPH in the presence of aldehyde reductases 1 and 2 is described. The reactivity of these nitroso substrates is increased by hydrophobic substituents and those promoting OH- elimination from the molecule of the reduced substrate. NN-Dimethylbenzoquinonedi-iminium cation was proved to be the reaction product formed from p-nitroso-N-dimethylaniline. The kinetics of the reduction of p-nitroso-N-dimethylaniline catalysed with aldehyde reductase 1 are rather complex at pH 7, and the preferred-pathway mechanism is probably involved. The reaction sequence approaches the ordered pattern at pH 8.5. It was shown that NADPH in equilibrium NADP+ recyclization proceeds in the presence of NADP+, p-nitroso-N-dimethylaniline, cyclohexanol and aldehyde reductase 1, the alcohol oxidation being the slowest step in this reaction. However, the rate of cyclohexanol oxidation surpasses that of the dissociation of NADPH from the enzyme.

摘要

本文描述了在醛还原酶1和2存在的情况下，用NADPH还原对亚硝基-N-二甲基苯胺、对亚硝基-N-二乙苯胺、对亚硝基苯酚和对亚硝基-N-苯胺的过程。这些亚硝基底物的反应活性会因疏水性取代基以及那些促进还原底物分子消除OH-的基团而增强。已证明NN-二甲基苯醌二亚胺阳离子是由对亚硝基-N-二甲基苯胺形成的反应产物。在pH 7时，醛还原酶1催化对亚硝基-N-二甲基苯胺的还原动力学相当复杂，可能涉及优先途径机制。在pH 8.5时，反应序列接近有序模式。结果表明，在NADP+、对亚硝基-N-二甲基苯胺、环己醇和醛还原酶1存在的情况下，平衡NADP+循环中的NADPH会发生反应，醇氧化是该反应中最慢的步骤。然而，环己醇氧化的速率超过了NADPH从酶上解离的速率。