Article
The K346T mutant of GnT-III bearing weak in vitro and potent intracellular activity.
Biochimica et biophysica acta. General subjects - 1 Sept 2024
Hashimoto Yuta, Kawade Haruka, Bao WanXue, Morii Sayaka, Nakano Miyako, Nagae Masamichi, Murakami Reiko, Tokoro Yuko, Nakashima Misaki, Cai Zixuan, Isaji Tomoya, Gu Jianguo, Nakajima Kazuki, Kizuka Yasuhiko
Abstract excerpt
BACKGROUND: N-Acetylglucosaminyltransferase-III (GnT-III, also designated MGAT3) catalyzes the formation of a specific N-glycan branch, bisecting GlcNAc, in the Golgi apparatus. Bisecting GlcNAc is a key residue that suppresses N-glycan maturation and is associated with the pathogenesis of cancer and Alzheimer's disease. However, it remains unclear how GnT-III recognizes its substrates and how GnT-III activity is...
Topics
- Humans
- N-Acetylglucosaminyltransferases
- Substrate Specificity
- Golgi Apparatus
- Mutation
- Polysaccharides
- Catalytic Domain
- Glycosylation