延胡索酸酶偏离米氏动力学。
Deviation from Michaelis-Menten kinetics for fumarase.
作者信息
Crabbe M J, Bardsley W G
出版信息
Biochem J. 1976 Aug 1;157(2):333-7. doi: 10.1042/bj1570333.
Abstract
A study of the steady-state kinetics of fumarase over an extended concentration range, using novel methods of analysis, reveals an initial-rate equation of at least fourth degree for malate as substrate at pH 7.0, with no kinetically significant dead-end complex formation even up to concentrations of 100 mM. In the absence of demonstrable enzyme-aggregation phenomena, this is interpreted as indicating co-operative effects overlooked previously, although a mixture of isoenzymes, each individually of high degree and giving a complex curve, may be a contributing factor.
摘要
一项使用新分析方法对富马酸酶在扩展浓度范围内的稳态动力学进行的研究表明，在pH 7.0时，以苹果酸为底物的初始速率方程至少为四次方程，即使在高达100 mM的浓度下也没有动力学上显著的终产物复合物形成。在没有明显的酶聚集现象的情况下，这被解释为表明先前被忽视的协同效应，尽管同工酶的混合物，每种同工酶单独具有高度并给出复杂曲线，可能是一个促成因素。
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引用本文的文献
1
Lack of deviation from Michaelis--Menten kinetics for pig heart fumarase.猪心富马酸酶未偏离米氏动力学。
Biochem J. 1980 Sep 1;189(3):653-4. doi: 10.1042/bj1890653.
2
Deviations from Michaelis-Menten kinetics. The possibility of complicated curves for simple kinetic schemes and the computer fitting of experimental data for acetylcholinesterase, acid phosphatase, adenosine deaminase, arylsulphatase, benzylamine oxidase, chymotrypsin, fumarase, galactose dehydrogenase, beta-galactosidase, lactate dehydrogenase, peroxidase and xanthine oxidase.与米氏动力学的偏差。简单动力学机制出现复杂曲线的可能性以及对乙酰胆碱酯酶、酸性磷酸酶、腺苷脱氨酶、芳基硫酸酯酶、苄胺氧化酶、胰凝乳蛋白酶、延胡索酸酶、半乳糖脱氢酶、β-半乳糖苷酶、乳酸脱氢酶、过氧化物酶和黄嘌呤氧化酶的实验数据进行计算机拟合。
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3
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本文引用的文献
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2
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3
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