Structure of the human GlcNAc-1-phosphotransferase αβ subunits reveals regulatory mechanism for lysosomal enzyme glycan phosphorylation

Keyphrases

• Phosphorylation 100%
• Regulatory Mechanism 100%
• Lysosomal Enzymes 100%
• Glycans 100%
• GlcNAc-1-phosphotransferase 100%
• Phosphotransferase 100%
• Lysosomal Acid Lipase 40%
• Active State 40%
• Catalytic Core 40%
• Hydrolases 40%
• Vertebrates 20%
• Lysosome 20%
• Protein Binding 20%
• Mannose 20%
• N-acetylglucosamine 20%
• GlcNAc 20%
• Hockey Stick 20%
• Mannose-6-phosphate 20%
• Cryo-EM Structure 20%
• Substrate Binding 20%
• Phosphate-P 20%
• N-linked Glycans 20%
• Phosphate Recognition 20%
• Catalytic Site 20%
• Catalytic Pocket 20%
• Binding Determinants 20%
• Inactive State 20%
• Recognition System 20%
• Selective Substrate 20%
• Heterohexamer 20%

Biochemistry, Genetics and Molecular Biology

• Enzyme 100%
• Phosphotransferase 100%
• Polysaccharide 100%
• Hydrolase 57%
• Lysosome 14%
• Solution and Solubility 14%
• Binding Protein 14%
• N-Acetylglucosamine 14%
• Mannose 6-Phosphate 14%
• Cryoelectron Microscopy 14%
• Mannose 14%