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Literature summary for 2.7.8.17 extracted from

  • Lukong, K.E.; Elsliger, M.A.; Mort, J.S.; Potier, M.; Pshezhetsky, A.V.
    Identification of UDP-N-acetylglucosamine-phosphotransferase-binding sites on the lysosomal proteases, cathepsins A, B, and D (1999), Biochemistry, 38, 73-80.
    View publication on PubMed
Search for more literature for 2.7.8.17

Inhibitors

Inhibitors Comment Organism Structure
additional information most potent inhibition of phosphorylation by homologous peptides derived from the regions located on cathepsin molecules opposite to oligosaccharide chains which are phosphorylated by phosphotransferase Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the recognition and catalytic site of the phosphotransferase are located on different subunits Rattus norvegicus ?
-
 ?
UDP-N-acetyl-D-glucosamine + cathepsin A capthepsin A and cathepsin D have one closely related phosphotransferase recognition site represented by a structurally and topologically conserved beta-hairpin loop Rattus norvegicus UMP + ?
-
 ?
UDP-N-acetyl-D-glucosamine + cathepsin D capthepsin A and cathepsin D have one closely related phosphotransferase recognition site represented by a structurally and topologically conserved beta-hairpin loop Rattus norvegicus UMP + ?
-
 ?

Subunits

Subunits Comment Organism
More the recognition and catalytic site of the phosphotransferase are located on different subunits Rattus norvegicus