Enzymatic synthesis of γ-glutamylglutamine, a stable glutamine analogue, by γ-glutamyltranspeptidase from Escherichia coli K-12.
The optimal reaction conditions for the synthesis of γ-glutamylglutamine using γ-glutamyltranspeptidase from Escherichia coli were determined. The maximum yield of γ-glutamylglutamine (110 mM) was obtained using 250 mM L: -glutamine and 1.1 U γ-glutamyltranspeptidase/ml at pH 10.5 and at 37°C for 7 h; the conversion of glutamine to γ-glutamylglutamine was 88%.
El Sayed
Ashraf Sabry Abdel Fatah
AS
Division of Applied Biology, Graduate School of Science and Technology, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto, 606-8585, Japan.
Fujimoto
Shino
S
Yamada
Chiaki
C
Suzuki
Hideyuki
H
D004151:Dipeptides / Q000378:metabolism*; D048168:Escherichia coli K12 / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000302:isolation & purification* / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D013696:Temperature; D013997:Time Factors; D005723:gamma-Glutamyltransferase / Q000302:isolation & purification* / Q000378:metabolism*
D004151:Dipeptides; D029968:Escherichia coli Proteins; C047442:gamma-glutamylglutamine; D005723:gamma-Glutamyltransferase