GTP, an inhibitor of transglutaminases, is hydrolyzed by tissue-type transglutaminase (TGase 2) but not by epidermal-type transglutaminase (TGase 3).
Epidermal-type transglutaminase (TGase 3) is devoid of GTPase activity, but its TGase activity is inhibited by GTP as in the case of tissue-type TGase (TGase 2). In addition, the inhibition was not affected by the presence of higher concentrations of Ca ion. These results indicate that GTP interacts with TGase 3 in a manner different from its action on TGase 2.
Hitomi
K
K
Department of Applied Molecular Biosciences, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Japan. hitomi@agr.nagoya-u.ac.jp
Ikura
K
K
Maki
M
M
D000818:Animals; D002135:Calcium-Binding Proteins / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000378:metabolism* / Q000494:pharmacology; D019204:GTP-Binding Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006160:Guanosine Triphosphate / Q000378:metabolism* / Q000494:pharmacology; D006168:Guinea Pigs; D006801:Humans; D006868:Hydrolysis; D051379:Mice; D000091345:Protein Glutamine gamma Glutamyltransferase 2; D011503:Transglutaminases / Q000037:antagonists & inhibitors / Q000378:metabolism*
D002135:Calcium-Binding Proteins; D004791:Enzyme Inhibitors; D006160:Guanosine Triphosphate; C498713:Tgm3 protein, mouse; D000091345:Protein Glutamine gamma Glutamyltransferase 2; C498712:TGM3 protein, human; D011503:Transglutaminases; D019204:GTP-Binding Proteins