Transglutaminase Activity of Human ER-60

• Published in: Bioscience, biotechnology, and biochemistry Vol. 66; no. 6; pp. 1423 - 1426
• Main Authors: OKUDO, Hirokazu, KITO, Makoto, MORIYAMA, Tatsuya, OGAWA, Tadashi, URADE, Reiko
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.01.2002; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: Analytical, structural and metabolic biochemistry; Binding Sites; Biological and medical sciences; Calcium - pharmacology; Cystamine - pharmacology; Cysteine Endopeptidases - metabolism; Enzymes and enzyme inhibitors; Escherichia coli; Fundamental and applied biological sciences. Psychology; Humans; Hydrogen-Ion Concentration; protein disulfide isomerase; Recombinant Proteins - antagonists & inhibitors; Recombinant Proteins - metabolism; Transferases; transglutaminase; Transglutaminases - antagonists & inhibitors; Transglutaminases - metabolism; Human; Protein-glutamine γ-glutamyltransferase; Enzymatic activity; Enzyme; Aminoacyltransferases; Transferases
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.66.1423

Human recombinant ER-60 was confirmed to have transglutaminase activity by a microtiter plate assay. Transglutaminase activity of ER-60 did not require calcium and was inhibited by cystamine, a substrate analogue. In addition, the transglutaminase activity of ER-60 was not inhibited by SH-blocking reagents. These results suggest that the properties of the transglutaminase activity of ER-60 are different from those in the cases of known mammalian transglutaminases of which the active site includes a cysteine residue.