Effect of Carboxyl-Terminal Truncation on the Catalytic Performance of D-Phenylglycine Aminotransferase


  • Aiya Chantarasiri Faculty of Science, Energy and Environment, King Mongkut's University of Technology North Bangkok, Rayong Campus, Rayong 21120, Thailand
  • Rachael Patterson Department of Microbiology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand
  • Vithaya Meevootisom Department of Microbiology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand
  • Suthep Wiyakrutta Department of Microbiology, Faculty of Science, Mahidol University, Bangkok 10400, Thailand


D-phenylglycine aminotransferase, Carboxyl-terminus, Catalytic performance, Bioinformatics tools.


The D -phenylglycine aminotransferase (D -PhgAT) is a novel enzyme that can be used to synthesize precursors of antibiotics. This research addressed the function of the carboxyl-terminal (C-terminal) of D-PhgAT. Its C-terminal amino acid sequence was compared to other related proteins using bioinformatics tools. The analyzed amino acid sequence was used to produce a genetically modified enzyme having a truncation of the 10 amino acid residues at the C-terminal region. The truncated D -PhgAT was purified and analyzed for catalytic performance. The results revealed that the truncated enzyme had better catalytic performance than the full-length enzyme by 37.49%. This research is a preliminary study for improving the enzymatic performance of D -PhgAT by structure-guided engineering and can be applied in the development of other enzymes.


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How to Cite

Chantarasiri, A. ., Patterson, R. ., Meevootisom, V. ., & Wiyakrutta, S. . (2022). Effect of Carboxyl-Terminal Truncation on the Catalytic Performance of D-Phenylglycine Aminotransferase. Suan Sunandha Science and Technology Journal, 3(1), 9–13. Retrieved from https://li02.tci-thaijo.org/index.php/ssstj/article/view/267



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