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

A new method for the synthesis of β-N-(γ-L(+)-glutamyl)phenylhydrazine is presented. This compound was prepared from L-glutamine and phenylhydrazine through a transpeptidation reaction of Escherichia coli γ-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 γ-glutamyltranspeptidase/ml, and pH 9 in approx. 800 ml. After 6 h at 37 °C, the product was obtained with a conversion rate of 93 % (mol/mol). γ-Glutamyltranspeptidase was reversibly inhibited only when phenylhydrazine was above 300 mM.

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