Ontology highlight
ABSTRACT:
SUBMITTER: Candi E
PROVIDER: S-EPMC1133790 | biostudies-literature | 2004 Jul
REPOSITORIES: biostudies-literature
The Biochemical journal 20040701 Pt 1
Transglutaminases (TGases) are Ca2+-dependent enzymes capable of catalysing transamidation of glutamine residues to form intermolecular isopeptide bonds. Nine distinct TGases have been described in mammals, and two of them (types 2 and 3) are regulated by GTP/ATP. TGase2 hydrolyses GTP and is therefore a bifunctional enzyme. In the present study, we report that TGase5 is also regulated by nucleotides. We have identified the putative TGase5 GTP-binding pocket by comparative amino acid sequence al ...[more]