An acetylation site in lectin domain modulates the biological activity of polypeptide GalNAc-transferse-2

ZLOCOWSKI N; LORENZ, VIRGINIA; BENNETT EP; CLAUSEN H; NORES GA; IRAZOQUI FJ

WALTER DE GRUYTER & CO

Lugar: Berlin; Año: 2013 vol. 394 p. 69 - 69

p style="LINE-HEIGHT: normal; MARGIN: 0cm 0cm 0pt; TEXT-AUTOSPACE: ; mso-layout-grid-align: none" class="MsoNormal">Polypeptide GalNAc-transferases (ppGalNAc-Ts) are a family of enzymes that catalyze the initiation of mucintype O -glycosylation. All ppGalNAc-T family members contain a common (QXW) 3 motif, which is present in the R-type lectin group. The acetylation site K521 is part of the QKW motif of â -trefoil in the lectin domain of ppGalNAc-T2. We used a combination of acetylation and site-directed