title: Transglutaminase activity of human ER-60.
abstract: 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.
authors.affiliation: Graduate School of Agriculture, Kyoto University, Uji, Japan.
authors.forename: Hirokazu
authors.initials: H
authors.lastname: Okudo
authors.forename: Makoto
authors.initials: M
authors.lastname: Kito
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Moriyama
authors.forename: Tadashi
authors.initials: T
authors.lastname: Ogawa
authors.forename: Reiko
authors.initials: R
authors.lastname: Urade
mesh_terms: D001665:Binding Sites; D002118:Calcium / Q000494:pharmacology; D003538:Cystamine / Q000494:pharmacology; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D004926:Escherichia coli; D006801:Humans; D006863:Hydrogen-Ion Concentration; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism; D011503:Transglutaminases / Q000037:antagonists & inhibitors / Q000378:metabolism*
chemical_list: D011994:Recombinant Proteins; D011503:Transglutaminases; D003546:Cysteine Endopeptidases; C077733:ER-60 protease; D003538:Cystamine; D002118:Calcium