Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / isolation & purification
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Escherichia coli Proteins / metabolism*
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Glutamates / analysis
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Glutamates / chemistry
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Glutamates / metabolism*
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Hydrogen-Ion Concentration
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Phenylhydrazines / analysis
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Phenylhydrazines / chemistry
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Phenylhydrazines / metabolism*
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism*
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Temperature
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gamma-Glutamyltransferase / genetics
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gamma-Glutamyltransferase / isolation & purification
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gamma-Glutamyltransferase / metabolism*
Substances
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Escherichia coli Proteins
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Glutamates
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Phenylhydrazines
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Recombinant Proteins
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gamma-Glutamyltransferase