Catalytic and glycan-binding abilities of ppGalNAc-T2 are regulated by

ZLOKOWSKI N; SENDRA VG; VILLAREAL M; JORGE A; NUÑEZ Y; BENNET EP; KLAUSEN H; NORES GA; IRAZOQUI FJ

ACADEMIC PRESS INC ELSEVIER SCIENCE

Año: 2011 vol. 410 p. 140 - 140

font face="Arial"> Post-translational acetylation is an important molecular regulatory mechanism affecting the biological activity of proteins. Polypeptide GalNAc transferases (ppGalNAc-Ts) are a family of enzymes that catalyze initiation of mucin-type Oglycosylation. All ppGalNAc-Ts in mammals are type II transmembrane proteins having a Golgi lumenal region that contains a catalytic domain with glycosyltransferase activity, and a C-terminal R-type ("ricin-like") lectin domain. We investigated the effect of acetylation on catalytic activity of glycosyltransferase, and on fine carbohydrate-binding specificity of the R-type lectin domain of ppGalNAc-T2. Acetylation effect on ppGalNAc-T2 biological activity in vitro was studied using a p