Gtp is required to stabilize and display transamidation activity of transglutaminase 2

Ju Hong Jeon, Sung Yup Cho, Chai Wan Kim, Dong Myung Shin, Joon Chul Kweon, Kyung Ho Choi, Sang Chul Park, In Gyu Kim

Research output: Contribution to journalArticlepeer-review

16 Scopus citations


Transglutaminase 2 (TGase 2) is a bifunctional enzyme that catalyzes calcium-dependent transamidation and GTP binding/ hydrolysis. The transamidation activity is proposed to be associated with several neurodegenerative disorders such as Alzheimer's and Hungtinton's disease. However, the regulation mechanism by which TGase 2 causes neurodegeneration is unknown. In this study, we show that two activities of TGase 2 have a differential stability; transamidation activity is less stable than GTP hydrolytic activity, and that GTP was required to stabilize and to display transamidation activity. Moreover, GTP binding-defective mutant of TGase 2 did not show any transamidation activity in transfection experiments. These results indicate that GTP binding is crucial for transamidation activity of TGase 2, suggesting that protein cross-linking by TGase 2 might be associated with G-protein coupled receptor signaling system. Thus, our data could contribute to understand the regulation of TGase 2 activity and TGase 2-associated pathogenesis.

Original languageEnglish (US)
Pages (from-to)818-822
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - 2002


  • Enzyme stability
  • GTP binding/hydrolysis
  • Transamidation
  • Transglutaminase 2

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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