The structure of the colorectal cancer-associated enzyme GalNAc-T12 reveals how nonconserved residues dictate its function [Biochemistry]
Polypeptide N-acetylgalactosaminyl transferases (GalNAc-Ts) initiate mucin type O-glycosylation by catalyzing the transfer of N-acetylgalactosamine (GalNAc) to Ser or Thr on a protein substrate. Inactive and partially active variants of the isoenzyme GalNAc-T12 are present in subsets of patients with colorectal cancer, and several of these variants alter nonconserved residues with...
Source: Proceedings of the National Academy of Sciences - Category: Science Authors: Amy J. Fernandez, Earnest James Paul Daniel, Sai Pooja Mahajan, Jeffrey J. Gray, Thomas A. Gerken, Lawrence A. Tabak, Nadine L. Samara Tags: Biological Sciences Source Type: research
More News: Academies | Biochemistry | Cancer | Cancer & Oncology | Colorectal Cancer | Legislation | Science