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The binding of nicotinamide-adenine dimucleotide to glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus.烟酰胺腺嘌呤二核苷酸与嗜热脂肪芽孢杆菌的3-磷酸甘油醛脱氢酶的结合
Biochem J. 1975 Dec;151(3):747-9. doi: 10.1042/bj1510747.
2
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Biochem Biophys Res Commun. 2001 May 4;283(2):347-50. doi: 10.1006/bbrc.2001.4779.
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NAD+ analogue binding to glyceraldehyde-3-phosphate dehydrogenase.
Eur J Biochem. 1983 Dec 1;137(1-2):67-73. doi: 10.1111/j.1432-1033.1983.tb07796.x.
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Dimers generated from tetrameric phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus are inactive but exhibit cooperativity in NAD binding.由嗜热脂肪芽孢杆菌的四聚体磷酸化甘油醛-3-磷酸脱氢酶生成的二聚体没有活性，但在NAD结合方面表现出协同性。
Biochemistry. 1999 Dec 7;38(49):16084-91. doi: 10.1021/bi9912802.
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Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus.嗜热脂肪芽孢杆菌3-磷酸甘油醛脱氢酶的序列与结构
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D-glyceraldehyde-3-phosphate dehydrogenase. The purification and characterisation of the enzyme from the thermophiles Bacillus stearothermophilus and Thermus aquaticus.D-甘油醛-3-磷酸脱氢酶。嗜热脂肪芽孢杆菌和嗜热水生栖热菌中该酶的纯化及特性研究
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8
The nicotinamide subsite of glyceraldehyde-3-phosphate dehydrogenase studied by site-directed mutagenesis.通过定点诱变研究甘油醛-3-磷酸脱氢酶的烟酰胺亚位点。
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Conformational variability of NAD+ in the free and bound states: a nicotinamide sandwich in NAD+ crystals.游离态和结合态NAD⁺的构象变异性：NAD⁺晶体中的烟酰胺夹心结构
Science. 1984 Nov 23;226(4677):969-71. doi: 10.1126/science.6239374.

引用本文的文献

1
Mechanism of negative cooperativity in glyceraldehyde-3-phosphate dehydrogenase deduced from ligand competition experiments.从配体竞争实验推导的3-磷酸甘油醛脱氢酶负协同性机制
Proc Natl Acad Sci U S A. 1980 Sep;77(9):5055-59. doi: 10.1073/pnas.77.9.5055.

本文引用的文献

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The purification of nicotinamide adenine dinucleotide and kinetic effects of nucleotide impurities.烟酰胺腺嘌呤二核苷酸的纯化及核苷酸杂质的动力学效应
J Biol Chem. 1963 Apr;238:1538-43.
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Glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus.嗜热脂肪芽孢杆菌的3-磷酸甘油醛脱氢酶
FEBS Lett. 1971 Mar 16;13(4):217-220. doi: 10.1016/0014-5793(71)80539-2.
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Thermodynamics of nicotinamide-adenine dinucleotide addition to the glyceraldehyde 3-phosphate dehydrogenases of yeast and of rabbit skeletal muscle. An equilibrium and calorimetric analysis over a range of temperatures.烟酰胺腺嘌呤二核苷酸添加到酵母和兔骨骼肌磷酸甘油醛脱氢酶中的热力学。在一定温度范围内的平衡和量热分析。
Biochemistry. 1971 Mar 2;10(5):779-86. doi: 10.1021/bi00781a009.
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Preparation and active-site specific properties of sturgeon muscle glyceraldehyde-3-phoshate dehydrogenase.
Biochemistry. 1973 Oct 9;12(21):4290-300. doi: 10.1021/bi00745a038.
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The binding of oxidized and reduced nicotinamide adenine-dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase.
Eur J Biochem. 1972 Mar 27;26(2):220-36. doi: 10.1111/j.1432-1033.1972.tb01760.x.
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Binding of NAD + and NADH to rabbit-muscle glyceraldehydephosphate dehydrogenase.NAD⁺和NADH与兔肌肉甘油醛-3-磷酸脱氢酶的结合
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Positive and negative cooperativity in yeast glyceraldehyde 3-phosphate dehydrogenase.
Biochemistry. 1970 Aug 18;9(17):3337-42. doi: 10.1021/bi00819a007.
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The binding of NAD+ to rabbit muscle glyceraldehyde-3-phosphate dehydrogenase studied by protein fluorescence quenching.通过蛋白质荧光猝灭研究NAD⁺与兔肌肉磷酸甘油醛脱氢酶的结合。
Biochim Biophys Acta. 1971 Apr 14;235(1):27-31. doi: 10.1016/0005-2744(71)90029-5.
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Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. II. Stopped-flow studies at pH 8-5 and 40 degrees C.烟酰胺腺嘌呤二核苷酸与酵母甘油醛-3-磷酸脱氢酶的协同结合。II. pH 8.5和40℃下的停流研究。
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10
Co-operative binding of nicotinamide-adenine dinucleotide to yeast glyceraldehyde-3-phosphate dehydrogenase. I. Equilibrium and temperature-jump studies at pH 8-5 and 40 degrees C.烟酰胺腺嘌呤二核苷酸与酵母甘油醛-3-磷酸脱氢酶的协同结合。I. 在pH 8.5和40℃条件下的平衡和温度跃变研究
J Mol Biol. 1971 May 28;58(1):29-50. doi: 10.1016/0022-2836(71)90230-0.

烟酰胺腺嘌呤二核苷酸与嗜热脂肪芽孢杆菌的3-磷酸甘油醛脱氢酶的结合

The binding of nicotinamide-adenine dimucleotide to glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus.

作者信息

Allen G, Harris J I

出版信息

Biochem J. 1975 Dec;151(3):747-9. doi: 10.1042/bj1510747.

DOI:10.1042/bj1510747
PMID:175789
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1172424/
Abstract

The binding of NAD+ to glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) from Bacillus stearothermophilus has been studied by measurement of protein fluorescence quenching. Slight negative co-operativity was observed in the binding of the third and fourth coenzyme molecules to the tetrameric enzyme. The first two coenzyme molecules were tightly bound. In this respect the enzyme resembles that from sturgeon muscle rather than that from yeast.

摘要

通过测量蛋白质荧光猝灭，研究了NAD⁺与嗜热脂肪芽孢杆菌甘油醛-3-磷酸脱氢酶（EC 1.2.1.12）的结合情况。在第三个和第四个辅酶分子与四聚体酶的结合中观察到轻微的负协同效应。前两个辅酶分子紧密结合。在这方面，该酶类似于鲟鱼肌肉中的酶，而不是酵母中的酶。