Article
Independent Lec1A CHO glycosylation mutants arise from point mutations in N-acetylglucosaminyltransferase I that reduce affinity for both substrates. Molecular consequences based on the crystal structure of GlcNAc-TI.
Biochemistry - 31 Jul 2001
Chen W, Unligil U M, Rini J M, Stanley P
Abstract excerpt
A key enzyme in regulating the maturation of N-linked glycans is UDP-N-acetylglucosamine:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I (GlcNAc-TI, EC 2.4.1.101). Lec1 CHO cells lack GlcNAc-TI activity and synthesize only the oligomannosyl class of N-glycans. By contrast, Lec1A CHO mutants have weak GlcNAc-TI activity due to the reduced affinity of GlcNAc-TI for both the UDP-GlcNAc and...
Topics
- Animals
- Arginine
- Aspartic Acid
- CHO Cells
- Conserved Sequence
- Cricetinae
- Cricetulus
- Crystallography, X-Ray
- Glycosylation
- Molecular Sequence Data
- Mutagenesis, Site-Directed