CIESC Journal ›› 2008, Vol. 59 ›› Issue (2): 431-436.

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Kinetic model of enzymatic synthesis of γ-D-glutamyl-L-tryptophan

WANG Qian, YAO Zhong, WU Minggang, XUN Zhijin, ZHOU Zhi, XU Hong, WEI Ping   

  • Online:2008-02-05 Published:2008-02-05

酶法制备γ-D-glutamyl-L-tryptophan的动力学模型

汪前,姚忠,吴明刚,荀志金,周治,徐虹,韦萍   

  1. 南京工业大学制药与生命科学学院

Abstract:

A new model of enzymatic synthesis of γ-D-Glu-L-Trp(SCV-07)from D-glutamine and L-tryptophan was developed.The Km and Kcat of transpeptidation and enzymatic hydrolysis of product (presented as K′m and K′cat) were determined as Km=5.11 mmol·L-1, Kcat =3.92 mmol·min-1, K′m=2.31 mmol·L-1 and K′cat=1.46 mmol·min-1.The sequential mechanism was used to describe the rate of transpeptidation,and the model parameters were optimized.The enzymatic synthesis of γ-D-glutamyl-L-tryptophan was investigated to verify the model.Good agreement between experimental data and calculations was obtained.The total relative errors of experimental data and calculations were less than 5%.

Key words:

γ-谷氨酰转肽酶, 反应机理, γ-D-Glu-L-Trp, 动力学模型

摘要:

以酶法合成γ-D-glutamyl-L-tryptophan (γ-D-Glu-L-Trp)为研究体系,采用D-谷氨酰胺为γ-谷氨酰基供体,L-色氨酸为受体,测定得到了转肽反应的米氏常数(K m)为5.11 mmol·L-1,催化常数(Kcat)为3.92 mmol·min-1,γ-D-Glu-L-Trp的水解反应米氏常数(K′m)为2.31 mmol·L-1,催化常数(K′cat)为1.46 mmol·min-1。采用顺序反应机制建立了酶法制备γ-D-Glu-L-Trp的过程动力学模型,并进行了参数优化。经验证,所建模型可准确预测该体系中的反应进程,模型数值解与实验值的平均相对误差小于5%。

关键词:

γ-谷氨酰转肽酶, 反应机理, γ-D-Glu-L-Trp, 动力学模型