Biotechnology Letters

, Volume 32, Issue 12, pp 1877–1881 | Cite as

Enzymatic synthesis of γ-glutamylglutamine, a stable glutamine analogue, by γ-glutamyltranspeptidase from Escherichia coli K-12

  • Ashraf Sabry Abdel Fatah El Sayed
  • Shino Fujimoto
  • Chiaki Yamada
  • Hideyuki SuzukiEmail author
Original Research Paper


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%.


Glutamine γ-Glutamylglutamine γ-Glutamyltranspeptidase Transpeptidation 



We would like to thank Dr. Bunnta Watanabe and Prof. Jun Hiratake, Institute for Chemical Research, Kyoto University, for the NMR and MS analyses and for their productive discussion. This work was supported by a Grant-in-Aid for Scientific Research (no. 21380059) to HS from the Ministry of Education, Culture, Sports, Science and Technology of Japan. CY was supported by the 21st Century COE Program of the Ministry of Education, Culture, Sports, Science and Technology of Japan.


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Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  • Ashraf Sabry Abdel Fatah El Sayed
    • 1
    • 3
  • Shino Fujimoto
    • 1
    • 2
  • Chiaki Yamada
    • 1
    • 2
  • Hideyuki Suzuki
    • 1
    Email author
  1. 1.Division of Applied BiologyGraduate School of Science and Technology, Kyoto Institute of TechnologyKyotoJapan
  2. 2.Division of Integrated Life Science, Graduate School of BiostudiesKyoto UniversityKyotoJapan
  3. 3.Department of Microbiology and Botany, Faculty of ScienceZagazig UniversityZagazigArab Republic of Egypt

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