蛋白质修饰反应动力学。在所有可修饰基团对酶活性均至关重要的情况下，酶活性分数与蛋白质修饰程度的关系图。
Kinetics of protein modification reactions. Plot of fractional enzyme activity versus extent of protein modification in cases where all modifiable groups are essential for enzyme activity.
作者信息
Rakitzis E T
出版信息
Biochem J. 1984 Oct 1;223(1):259-62. doi: 10.1042/bj2230259.
Abstract
The plot of fractional enzyme activity versus extent of protein modification, for cases where all enzyme modifiable groups of a certain kind are essential for activity, is found to be nearly independent of the number, per enzyme active site, of modifiable groups involved. Such plots usually, by a fallacious extension of the initial portion of the plot on the extent-of-modification axis, are interpreted to mean the modification of one single group per enzyme active site (or per enzyme molecule). The possible relevance of these findings to cases in the literature is discussed.
摘要
对于某类所有可被修饰的酶基团对活性都至关重要的情况，酶活性分数与蛋白质修饰程度的关系图被发现几乎与每个酶活性位点所涉及的可修饰基团数量无关。通常，通过在修饰程度轴上对关系图初始部分进行错误的延伸，这些关系图被解释为意味着每个酶活性位点（或每个酶分子）有一个单一基团被修饰。文中讨论了这些发现与文献中相关案例的可能关联性。
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Kinetics of protein modification reactions. Plot of fractional enzyme activity versus extent of protein modification in cases where all modifiable groups are essential for enzyme activity.蛋白质修饰反应动力学。在所有可修饰基团对酶活性均至关重要的情况下，酶活性分数与蛋白质修饰程度的关系图。
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本文引用的文献
1
ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.关于别构转变的本质：一个合理的模型。
J Mol Biol. 1965 May;12:88-118. doi: 10.1016/s0022-2836(65)80285-6.
2
3
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J Theor Biol. 1980 Aug 7;85(3):553-60. doi: 10.1016/0022-5193(80)90328-8.
4
Reactivity of sulfhydryl groups of the flavoenzyme D-lactate dehydrogenase and effect on catalytic activity.黄素酶D-乳酸脱氢酶巯基的反应性及其对催化活性的影响。
Biochemistry. 1980 Jul 8;19(14):3137-44. doi: 10.1021/bi00555a004.
5
Inactivation of rat liver S-adenosylhomocysteinase by iodoacetamide.碘乙酰胺对大鼠肝脏S-腺苷同型半胱氨酸酶的失活作用。
Biochemistry. 1982 Aug 17;21(17):4171-6. doi: 10.1021/bi00260a039.
6
Study on the role of tyrosine side-chains at the active centre of emulsin beta-D-glucosidase.关于苦杏仁苷β-D-葡萄糖苷酶活性中心酪氨酸侧链作用的研究。
Biochim Biophys Acta. 1981 Dec 15;662(2):308-11. doi: 10.1016/0005-2744(81)90043-7.
7
Kinetic analysis of biphasic protein modification reactions.双相蛋白质修饰反应的动力学分析
J Math Biol. 1980 Aug;10(1):79-87. doi: 10.1007/BF00276397.
8
A single functional arginyl residue involved in the catalysis promoted by Lactobacillus casei thymidylate synthetase.一个参与干酪乳杆菌胸苷酸合成酶催化作用的单个功能性精氨酰残基。
Arch Biochem Biophys. 1980 Oct 1;204(1):340-9. doi: 10.1016/0003-9861(80)90042-9.
9
Chemical modification studies on Abrus agglutinin. Involvement of tryptophan residues in sugar binding.相思子凝集素的化学修饰研究。色氨酸残基在糖结合中的作用。
Biochem J. 1984 Feb 1;217(3):773-81. doi: 10.1042/bj2170773.
10
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Biochem J. 1984 Jan 15;217(2):341-51. doi: 10.1042/bj2170341.
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