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1
State and accessibility of zinic in yeast alcohol dehydrogenase.酵母乙醇脱氢酶中锌的状态与可及性
Biochem J. 1976 Apr 1;155(1):155-61. doi: 10.1042/bj1550155.
2
The reactions of 1,10-phenanthroline with yeast alcohol dehydrogenase.1,10-菲咯啉与酵母乙醇脱氢酶的反应
Biochem J. 1977 Oct 1;167(1):237-44. doi: 10.1042/bj1670237.
3
The intrinsic zinc atoms of yeast alcohol dehydrogenase.酵母乙醇脱氢酶的内在锌原子。
Biochem Biophys Res Commun. 1975 Dec 15;67(4):1494-500. doi: 10.1016/0006-291x(75)90195-3.
4
L-histidinol dehydrogenase, a Zn2+-metalloenzyme.L-组氨醇脱氢酶,一种锌金属酶。
Arch Biochem Biophys. 1989 Aug 1;272(2):311-7. doi: 10.1016/0003-9861(89)90224-5.
5
Spectroscopic investigation of binary and ternary coenzyme complexes of yeast alcohol dehydrogenase.酵母乙醇脱氢酶二元和三元辅酶复合物的光谱研究。
Eur J Biochem. 1976 Jul 1;66(2):277-84. doi: 10.1111/j.1432-1033.1976.tb10517.x.
6
Optical spectroscopy of nicotinoprotein alcohol dehydrogenase from Amycolatopsis methanolica: a comparison with horse liver alcohol dehydrogenase and UDP-galactose epimerase.甲醇拟无枝酸菌烟碱蛋白醇脱氢酶的光学光谱:与马肝醇脱氢酶和UDP-半乳糖差向异构酶的比较
Biochemistry. 1998 Mar 3;37(9):3068-77. doi: 10.1021/bi972115u.
7
Investigation of a catalytic zinc binding site in Escherichia coli L-threonine dehydrogenase by site-directed mutagenesis of cysteine-38.通过对半胱氨酸-38进行定点诱变研究大肠杆菌L-苏氨酸脱氢酶中的催化锌结合位点。
Arch Biochem Biophys. 1998 Oct 15;358(2):211-21. doi: 10.1006/abbi.1998.0845.
8
The presence of zinc in the restriction enzyme Eco RI.限制性内切酶Eco RI中锌的存在。
J Biol Chem. 1982 Jul 25;257(14):7911-4.
9
Inactivation of chicken liver pyruvate carboxylase by 1,10-phenanthroline.1,10-菲咯啉对鸡肝丙酮酸羧化酶的失活作用。
Biochem J. 1988 Jun 1;252(2):501-7. doi: 10.1042/bj2520501.
10
Liver alcohol dehydrogenase: evidence for a new cobalt/zinc hybrid.肝脏乙醇脱氢酶:一种新型钴/锌杂合物的证据。
Biochem Biophys Res Commun. 1976 Oct 4;72(3):886-92. doi: 10.1016/s0006-291x(76)80215-x.

引用本文的文献

1
Probing adenosine nucleotide-binding proteins with an affinity-labeled nucleotide probe and mass spectrometry.使用亲和标记的核苷酸探针和质谱法探测腺苷核苷酸结合蛋白。
Anal Chem. 2007 Aug 1;79(15):5547-56. doi: 10.1021/ac0622375. Epub 2007 Jun 30.
2
The reactions of 1,10-phenanthroline with yeast alcohol dehydrogenase.1,10-菲咯啉与酵母乙醇脱氢酶的反应
Biochem J. 1977 Oct 1;167(1):237-44. doi: 10.1042/bj1670237.

本文引用的文献

1
The role of zinc in alcohol dehydrogenase. V. The effect of metal-binding agents on thestructure of the yeast alcohol dehydrogenase molecule.锌在乙醇脱氢酶中的作用。V. 金属结合剂对酵母乙醇脱氢酶分子结构的影响。
J Biol Chem. 1960 Nov;235:3188-92.
2
The role of zinc in alcohol dehydrogenases. III. The kinetics of a time-dependent inhibition of yeast alcohol dehydrogenase by 1,10-phenanthroline.锌在乙醇脱氢酶中的作用。III. 1,10-菲咯啉对酵母乙醇脱氢酶时间依赖性抑制的动力学
J Biol Chem. 1958 May;232(1):465-74.
3
The role of zinc in alcohol dehydrogenases. II. The kinetics of the instantaneous reversible inhibition of yeast alcohol dehydrogenase by 1,10-phenanthroline.锌在醇脱氢酶中的作用。II. 1,10-菲咯啉对酵母醇脱氢酶的瞬时可逆抑制动力学
J Biol Chem. 1958 May;232(1):453-64.
4
Kinetic studies on the rôle of zinc and diphosphopyridine nucleotide in the activity of yeast alcohol dehydrogenase.锌和二磷酸吡啶核苷酸在酵母醇脱氢酶活性中作用的动力学研究。
J Biol Chem. 1956 Jul;221(1):491-500.
5
Yeast alcohol dehydrogenase: molecular weight, coenzyme binding, and reaction equilibria.酵母乙醇脱氢酶:分子量、辅酶结合及反应平衡
J Biol Chem. 1954 Mar;207(1):225-44.
6
The interaction of 1-anilino-8-naphthalene sulphonate with yeast alcohol dehydrogenase.1-苯胺基-8-萘磺酸盐与酵母乙醇脱氢酶的相互作用
FEBS Lett. 1971 Jun 2;15(1):17-20. doi: 10.1016/0014-5793(71)80068-6.
7
The importance of SH-groups for enzymic activity. 7. The amino acid sequence around the essential SH-group of pig heart lactate dehydrogenase, isoenzyme I.巯基对酶活性的重要性。7. 猪心乳酸脱氢酶同工酶I必需巯基周围的氨基酸序列。
Eur J Biochem. 1967 Jun;1(4):476-81. doi: 10.1111/j.1432-1033.1967.tb00095.x.
8
The binding of dihydronicotinamide--adenine dinucleotide and pyridine-3-aldehyde--adenine dinucleotide by yeast alcohol dehydrogenase.酵母乙醇脱氢酶对二氢烟酰胺-腺嘌呤二核苷酸和吡啶-3-醛-腺嘌呤二核苷酸的结合作用
Biochem J. 1970 Dec;120(4):821-30. doi: 10.1042/bj1200821.
9
Differential chemical reactivities of zinc in horse liver alcohol dehydrogenase.马肝醇脱氢酶中锌的不同化学反应活性
Biochemistry. 1970 Oct 13;9(21):4078-86. doi: 10.1021/bi00823a008.
10
The structure of horse liver alcohol dehydrogenase.马肝醇脱氢酶的结构。
FEBS Lett. 1974 Aug 25;44(2):200-4. doi: 10.1016/0014-5793(74)80725-8.

酵母乙醇脱氢酶中锌的状态与可及性

State and accessibility of zinic in yeast alcohol dehydrogenase.

作者信息

Leskovac V, Trivić S, Latkovska M

出版信息

Biochem J. 1976 Apr 1;155(1):155-61. doi: 10.1042/bj1550155.

DOI:10.1042/bj1550155
PMID:180979
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1172812/
Abstract
  1. Yeast alcohol dehydrogenase (EC 1.1.1.1) is inhibited in the presence of 1,10-phenanthroline. 2. A conformational change in the enzyme's structure is induced by 1,10-phenanthroline, and is abolished in the presence of NADH. 1,10-Phenanthroline binds to the enzyme competitively with respect to NADH, with a stoicheiometry of 2 mol of 1,10-phenanthroline/144000g of enzyme. 3. 1,10-Phenanthroline induces a time-dependent dissociation of Zn2+ from the enzyme, which is in correlation with its inhibitions. 4. Spectrophotometric measurement indicates that the dissociation of half (2 zinc atoms/tetramer) of the total zinc content of the enzyme correlates with the full inhibition of its activity. Measurement of the tightly bound Zn2+ by atomic absorption photometry confirms this. 5. A proposition is advanced that the tetrameric molecule of yeast alcohol dehydrogenase possesses an inherent asymmetry, with four monomeric subunits being arranged in two mutually symmetrical pairs.
摘要
  1. 酵母乙醇脱氢酶(EC 1.1.1.1)在1,10-菲咯啉存在时受到抑制。2. 1,10-菲咯啉可诱导该酶结构发生构象变化,而在烟酰胺腺嘌呤二核苷酸(NADH)存在时这种变化消失。1,10-菲咯啉相对于NADH与该酶竞争性结合,化学计量比为2摩尔1,10-菲咯啉/144000克酶。3. 1,10-菲咯啉可诱导锌离子(Zn2+)从该酶上发生时间依赖性解离,这与其抑制作用相关。4. 分光光度法测量表明,该酶总锌含量的一半(每四聚体2个锌原子)解离与酶活性的完全抑制相关。通过原子吸收光度法对紧密结合的Zn2+进行测量证实了这一点。5. 有人提出一个观点,即酵母乙醇脱氢酶的四聚体分子具有内在不对称性,四个单体亚基以两个相互对称的对排列。