酵母乙醇脱氢酶IV。还原型辅酶及其片段的结合 - Suppr | 超能文献

Yeast alcohol dehydrogenase IV. Binding of reduced coenzyme and its fragments.

作者信息

Leskovac V, Pericin D, Trivić S

出版信息

Int J Biochem. 1978;9(5):365-71. doi: 10.1016/0020-711x(78)90112-x.

DOI:10.1016/0020-711x(78)90112-x

PMID:27402

Abstract

摘要

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Yeast alcohol dehydrogenase IV. Binding of reduced coenzyme and its fragments.酵母乙醇脱氢酶IV。还原型辅酶及其片段的结合

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The sulphydryl content of yeast mitochondrial F1-ATPase and the stoichiometry of subunits.酵母线粒体F1 - ATP酶的巯基含量及亚基化学计量学

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Measurements of the concentration of active sites in preparations of yeast alcohol dehydrogenase.酵母乙醇脱氢酶制剂中活性位点浓度的测定。

Eur J Biochem. 1974 Jan 3;41(1):31-6. doi: 10.1111/j.1432-1033.1974.tb03240.x.

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The conformation of adenosine diphosphoribose and 8-bromoadenosine diphosphoribose when bound to liver alcohol dehydrogenase.腺苷二磷酸核糖和8-溴腺苷二磷酸核糖与肝脏乙醇脱氢酶结合时的构象。

Eur J Biochem. 1975 Jan 15;50(3):475-81. doi: 10.1111/j.1432-1033.1975.tb09885.x.

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Interaction between dehydrogenases and a new NAD -isomer.脱氢酶与一种新型烟酰胺腺嘌呤二核苷酸异构体之间的相互作用。

Z Naturforsch C Biosci. 1975 Nov-Dec;30(6):734-8. doi: 10.1515/znc-1975-11-1207.

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Effect of pH on the reactivity of the active-site sulfhydryl groups in yeast alcohol dehydrogenase.pH对酵母乙醇脱氢酶活性位点巯基反应性的影响

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7

Metal stoichiometry, coenzyme binding, and zinc and cobalt enchange in highly purified yeast alcohol dehydrogenase.高纯度酵母乙醇脱氢酶中的金属化学计量、辅酶结合以及锌和钴的交换

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[Specific incorporation of the coenzyme analogue (3-(3-bromoacetylpyridinio)propyl)-adenosine pyrophosphate into the alcohol dehydrogenase from yeast (author's transl)].[辅酶类似物（3 -（3 - 溴乙酰吡啶鎓）丙基） - 腺苷焦磷酸特异性掺入酵母醇脱氢酶（作者译）]

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9

Studies with analogues of nicotinamide adenine dinucleotide.烟酰胺腺嘌呤二核苷酸类似物的研究。

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10

Coenzyme binding capacity of yeast alcohol dehydrogenase.酵母乙醇脱氢酶的辅酶结合能力

Biochem Biophys Res Commun. 1978 Mar 30;81(2):422-6. doi: 10.1016/0006-291x(78)91550-4.

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Use of competitive dead-end inhibitors to determine the chemical mechanism of action of yeast alcohol dehydrogenase.使用竞争性终产物抑制剂来确定酵母乙醇脱氢酶的化学作用机制。

Mol Cell Biochem. 1998 Jan;178(1-2):219-27. doi: 10.1023/a:1006851816483.