Enzymatic synthesis of β-N-(γ-L(+)-glutamyl)phenylhydrazine with Escherichia coli γ-glutamyltranspeptidase

被引:17
作者
Zhang, Hongjuan [1 ,2 ]
Zhan, Yueping [1 ]
Chang, Junjun [1 ]
Liu, Junzhong [1 ]
Xu, Lisheng [1 ]
Wang, Zhiyuan [1 ]
Liu, Qian [1 ]
Jiao, Qingcai [1 ]
机构
[1] Nanjing Univ, Sch Life Sci, State Key Lab Pharmaceut Biotechnol, Nanjing 210093, Jiangsu, Peoples R China
[2] Nanjing Med Univ, Sch Pharm, Nanjing 210029, Jiangsu, Peoples R China
关键词
beta-N-(gamma-L(+)-glutamyl)phenylhydrazine; gamma-Glutamyltranspeptidase; Phenylhydrazine; Reversible inhibition; AGARITINE; DERIVATIVES;
D O I
10.1007/s10529-012-1000-x
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
A new method for the synthesis of beta-N-(gamma-l(+)-glutamyl)phenylhydrazine is presented. This compound was prepared from l-glutamine and phenylhydrazine through a transpeptidation reaction of Escherichia coli gamma-glutamyltranspeptidase although phenylhydrazine has been reported to be an inhibitor of the enzyme. The optimum reaction conditions were 60 mM l-glutamine, 300 mM phenylhydrazine, 40 U gamma-glutamyltranspeptidase/ml, and pH 9 in approx. 800 ml. After 6 h at 37 A degrees C, the product was obtained with a conversion rate of 93 % (mol/mol). gamma-Glutamyltranspeptidase was reversibly inhibited only when phenylhydrazine was above 300 mM.
引用
收藏
页码:1931 / 1935
页数:5
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