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Role of zinc in horse liver alcohol dehydrogenase. Coenzyme and substrate binding.

作者信息

Iweibo I, Weiner H

出版信息

Biochemistry. 1972 Mar 14;11(6):1003-10. doi: 10.1021/bi00756a009.

DOI:10.1021/bi00756a009
PMID:4335285
Abstract
摘要

相似文献

1
Role of zinc in horse liver alcohol dehydrogenase. Coenzyme and substrate binding.锌在马肝醇脱氢酶中的作用。辅酶与底物结合。
Biochemistry. 1972 Mar 14;11(6):1003-10. doi: 10.1021/bi00756a009.
2
Relation of the auramine O binding site to the active site of horse liver alcohol dehydrogenase.金胺O结合位点与马肝醇脱氢酶活性位点的关系。
Biochemistry. 1971 Jul 6;10(14):2695-700. doi: 10.1021/bi00790a006.
3
Kinetic evidence for a binary complex isomerization in the liver alcohol dehydrogenase reaction mechanism.肝脏乙醇脱氢酶反应机制中二元复合物异构化的动力学证据。
Arch Biochem Biophys. 1971 Dec;147(2):825-7. doi: 10.1016/0003-9861(71)90445-0.
4
The site of auramine O binding to horse liver alcohol dehydrogenase.金胺O与马肝乙醇脱氢酶的结合位点。
J Biol Chem. 1972 Jan 25;247(2):334-41.
5
THE EFFECTS OF COENZYMES AND SUBSTRATES ON THE RATE OF ZINC EXCHANGE IN HORSE LIVER ALCOHOL DEHYDROGENASE.辅酶和底物对马肝醇脱氢酶中锌交换速率的影响。
Biochemistry. 1964 Jul;3:944-9. doi: 10.1021/bi00895a017.
6
Complexes of liver alcohol dehydrogenase. Further studies on the rate of inactivation.
Eur J Biochem. 1970 May 1;14(1):14-26. doi: 10.1111/j.1432-1033.1970.tb00255.x.
7
Role of zinc in horse liver alcohol dehydrogenase. Influence on structure and conformational changes.锌在马肝乙醇脱氢酶中的作用。对结构和构象变化的影响。
Biochemistry. 1972 Mar 14;11(6):1010-8. doi: 10.1021/bi00756a010.
8
Kinetic equivalence of the active sites of alcohol dehydrogenase from horse liver.马肝醇脱氢酶活性位点的动力学等效性
Eur J Biochem. 1975 May;54(1):65-73. doi: 10.1111/j.1432-1033.1975.tb04114.x.
9
Electronic, hydrophobic, and steric effects of binding of inhibitors to the horse liver alcohol dehydrogenase-reduced pyridine coenzyme binary complex.抑制剂与马肝醇脱氢酶-还原吡啶辅酶二元复合物结合的电子、疏水和空间效应。
Biochemistry. 1972 Jan 18;11(2):170-9. doi: 10.1021/bi00752a006.
10
Electron paramagnetic resonance study of the interaction of a spin-labeled analog of adenosine diphosphoribose with paramagnetic cobalt(II) liver alcohol dehydrogenase.腺苷二磷酸核糖自旋标记类似物与顺磁性钴(II)肝醇脱氢酶相互作用的电子顺磁共振研究
FEBS Lett. 1974 Feb 1;39(1):21-3. doi: 10.1016/0014-5793(74)80007-4.

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1
Evidence for co-operativity in coenzyme binding to tetrameric Sulfolobus solfataricus alcohol dehydrogenase and its structural basis: fluorescence, kinetic and structural studies of the wild-type enzyme and non-co-operative N249Y mutant.辅酶与四聚体嗜热栖热菌醇脱氢酶结合中的协同作用证据及其结构基础:野生型酶和非协同N249Y突变体的荧光、动力学和结构研究
Biochem J. 2005 Jun 1;388(Pt 2):657-67. doi: 10.1042/BJ20041539.
2
Structure of the complex of active site metal-depleted horse liver alcohol dehydrogenase and NADH.活性位点金属缺失的马肝醇脱氢酶与NADH复合物的结构
EMBO J. 1983;2(5):685-9. doi: 10.1002/j.1460-2075.1983.tb01485.x.