锌离子和还原型辅酶在马肝乙醇脱氢酶催化芳香醛还原过程中形成瞬态化学中间体的作用。 - Suppr

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Roles of zinc ion and reduced coenzyme in the formation of a transient chemical intermediate during the equine liver alcohol dehydrogenase catalyzed reduction of an aromatic aldehyde.

作者信息

Dunn M F, Hutchison J S

出版信息

Biochemistry. 1973 Nov 20;12(24):4882-92. doi: 10.1021/bi00748a012.

DOI:10.1021/bi00748a012

PMID:4357551

Abstract

摘要

相似文献

Roles of zinc ion and reduced coenzyme in the formation of a transient chemical intermediate during the equine liver alcohol dehydrogenase catalyzed reduction of an aromatic aldehyde.锌离子和还原型辅酶在马肝乙醇脱氢酶催化芳香醛还原过程中形成瞬态化学中间体的作用。

Biochemistry. 1973 Nov 20;12(24):4882-92. doi: 10.1021/bi00748a012.

Mechanistic studies on equine liver alcohol dehydrogenase. I. The stoichiometry relationship of the coenzyme binding sites to the catalytic sites active in the reduction of aromatic aldehydes in the transient state.马肝乙醇脱氢酶的机制研究。I. 辅酶结合位点与在瞬态下还原芳香醛的催化位点的化学计量关系。

Biochemistry. 1970 Jan 6;9(1):185-92. doi: 10.1021/bi00803a024.

Roles of zinc ion and reduced coenzyme in horse liver alcohol dehydrogenase catalysis. The mechanism of aldehyde activation.

Biochemistry. 1975 Jul 15;14(14):3176-82. doi: 10.1021/bi00685a022.

Influence of coenzyme structure on the transient chemical intermediate formed during horse-liver alcohol-dehydrogenase-catalyzed reduction of aromatic aldehydes.辅酶结构对马肝醇脱氢酶催化芳香醛还原过程中形成的瞬态化学中间体的影响。

Biochim Biophys Acta. 1986 Feb 14;869(3):265-74. doi: 10.1016/0167-4838(86)90066-x.

Mechanistic studies on horse liver alcohol dehydrogenase. The influence of the different premixings on the transient kinetics of aldehyde reductions.

Biochemistry. 1972 Jun 6;11(12):2303-10. doi: 10.1021/bi00762a015.

Synergism between coenzyme and aldehyde binding to liver alcohol dehydrogenase.辅酶与醛结合对肝脏乙醇脱氢酶的协同作用。

Eur J Biochem. 1983 Jul 1;133(3):651-5. doi: 10.1111/j.1432-1033.1983.tb07513.x.

Electronic substituent effects during the liver alcohol dehydrogenase catalyzed reduction of aromatic aldehydes.

Biochemistry. 1974 Jan 1;13(1):60-4. doi: 10.1021/bi00698a010.

Active-site-specific reconstituted cobalt(II) horse-liver alcohol dehydrogenase. Changes of the spectra of the substrate trans-4-(N,N-dimethylamino)-cinnamaldehyde and of the catalytic cobalt ion upon ternary complex formation with NADH and 1,4,5,6-tetrahydronicotinamide--adenine dinucleotide.

Eur J Biochem. 1979 Oct;100(1):267-70. doi: 10.1111/j.1432-1033.1979.tb02057.x.

Circular dichroism of liver alcohol dehydrogenase complexes with auramine O.

Biochemistry. 1973 Aug 28;12(18):3459-66. doi: 10.1021/bi00742a016.

Lewis acid complexes wchich show spectroscopic similarities to an alcohol dehydrogenase ternary complex.与醇脱氢酶三元复合物表现出光谱相似性的路易斯酸配合物。

Biochemistry. 1977 Jun 28;16(13):2922-31. doi: 10.1021/bi00632a019.

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Biochem J. 1997 Sep 15;326 ( Pt 3)(Pt 3):717-24. doi: 10.1042/bj3260717.

Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids.嗜热栖热放线菌乙醇脱氢酶：活性位点金属及其配体氨基酸的表征

Protein Sci. 1997 Feb;6(2):450-8. doi: 10.1002/pro.5560060223.

Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivatives.特定金属缺失和钴取代的马肝醇脱氢酶衍生物活性位点的晶体结构。

Proc Natl Acad Sci U S A. 1983 Sep;80(17):5289-93. doi: 10.1073/pnas.80.17.5289.

Neutral metal-bound water is the base catalyst in liver alcohol dehydrogenase.与金属结合的中性水是肝脏乙醇脱氢酶中的碱性催化剂。

Proc Natl Acad Sci U S A. 1983 May;80(9):2584-8. doi: 10.1073/pnas.80.9.2584.

Structural properties of long- and short-chain alcohol dehydrogenases. Contribution of NAD+ to stability.长链和短链醇脱氢酶的结构特性。NAD⁺对稳定性的作用。

Biochem J. 1991 Jun 1;276 ( Pt 2)(Pt 2):433-8. doi: 10.1042/bj2760433.

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