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The Multiplicity of Polypeptide GalNAc‐Transferase: Assays, Inhibitors, and Structures
Author(s) -
Hu Youtian,
Feng Juan,
Wu Fang
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201800303
Subject(s) - glycosylation , hypophosphatemic rickets , transferase , mucin , glycoprotein , chemistry , biochemistry , mechanism (biology) , biology , computational biology , enzyme , vitamin d and neurology , rickets , philosophy , epistemology , endocrinology
Mucin‐type O ‐glycosylation is the dominant form of glycosylation in eukaryotes and plays an important role in various physiological processes. The polypeptide GalNAc‐transferase (GalNAc‐T) catalyzes the first step in the attachment of mucin‐type O ‐glycosylation. GalNAc‐T was recently uncovered to be linked with cancer, atherogenic dyslipidemia, and X‐linked hypophosphatemic rickets. Therefore, it has attracted increasing interest as a new target for exploring the underlying mechanism and developing new treatments for related diseases. Decades of studies on GalNAc‐T have laid a stable foundation for understanding the catalytic mechanism, determining atom‐resolution three‐dimensional structures, and developing various types of biochemical assays as well as small‐molecule inhibitor leads. Here, we systematically summarize this invaluable knowledge on GalNAc‐T and cultivate new perspectives to foster breakthrough points for mucin‐type O ‐glycosylation.