Identification of UDP-N-acetylglucosamine-phosphotransferase-Binding Sites on the Lysosomal Proteases, Cathepsins A, B, and D

A key step in the targeting of soluble lysosomal enzymes is their recognition and phosphorylation by a 540 kDa multisubunit enzyme, UDP-N-acetylglucosamine-phosphotransferase (phosphotransferase). The molecular mechanism of recognition is still unknown, but previous experiments suggested that the ph...

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Veröffentlicht in:	Biochemistry (Easton) 1999-01, Vol.38 (1), p.73-80
Hauptverfasser:	Lukong, Kiven E, Elsliger, Marc-Andre, Mort, John S, Potier, Michel, Pshezhetsky, Alexey V
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Carboxypeptidases - antagonists & inhibitors Carboxypeptidases - chemistry Carboxypeptidases - metabolism Cathepsin A Cathepsin B - antagonists & inhibitors Cathepsin B - chemistry Cathepsin B - metabolism Cathepsin D - antagonists & inhibitors Cathepsin D - chemistry Cathepsin D - metabolism Computer Simulation Crystallography, X-Ray Humans Lysosomes - enzymology Models, Molecular Peptides - chemical synthesis Peptides - pharmacology Phosphorylation - drug effects Protein Structure, Tertiary Rats Transferases (Other Substituted Phosphate Groups) - chemistry Transferases (Other Substituted Phosphate Groups) - metabolism
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