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猪胰α-淀粉酶的动力学;双位点酶的理论模型。

Kinetics of hog pancreas alpha-amylase; theoretical model of the dual-site enzyme.

作者信息

Hutny J

出版信息

Acta Biochim Pol. 1981;28(2):123-34.

PMID:6172918
Abstract

The model of the multiple attack mechanism has been proposed for the enzyme consisting of two hypothetical subunits or domains identical in structure and function. The theoretical coefficients of multiple attack: effectiveness and average number of unitary movements, have been computed for such a dual-site model of pancreatic alpha-amylase. Those coefficients affect the values of maximum velocity and Michaelis constant, respectively. Two possible manners of the subunit coupling were considered: symmetric and sequential. The dual-site model with a symmetric type of coupling appeared to be kinetically indistinguishable from the single-site model.

摘要

对于由两个结构和功能相同的假设亚基或结构域组成的酶,已提出多重攻击机制模型。已针对胰腺α淀粉酶的这种双位点模型计算了多重攻击的理论系数:有效性和单位运动的平均数。这些系数分别影响最大速度和米氏常数的值。考虑了亚基偶联的两种可能方式:对称和顺序。具有对称偶联类型的双位点模型在动力学上似乎与单位点模型无法区分。

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