(Skp1-protein)-hydroxyproline N-acetylglucosaminyltransferase

(Skp1-protein)-hydroxyproline N-acetylglucosaminyltransferase
Identifiers
EC number 2.4.1.229
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

In enzymology, a [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase (EC 2.4.1.229) is an enzyme that catalyzes the chemical reaction

UDP-N-acetylglucosamine + [Skp1-protein]-hydroxyproline UDP + [Skp1-protein]-O-(N-acetyl-D-glucosaminyl)hydroxyproline

Thus, the two substrates of this enzyme are UDP-N-acetylglucosamine and Skp1-protein-hydroxyproline, whereas its two products are UDP and Skp1-protein-O-(N-acetyl-D-glucosaminyl)hydroxyproline.

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:[Skp1-protein]-hydroxyproline N-acetyl-D-glucosaminyl-transferase. Other names in common use include Skp1-HyPro GlcNAc-transferase, UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide, GlcNAc-transferase, UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase, and UDP-GlcNAc:hydroxyproline polypeptide GlcNAc-transferase.

References

    • CM; Morris, HR; Panico, M; Paxton, T; Dell, A; Kaplan, L; West, CM (2002). "Molecular cloning and expression of a UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc-transferase that modifies Skp1 in the cytoplasm of dictyostelium". J. Biol. Chem. 277 (48): 46328&ndash, 37. doi:10.1074/jbc.M208024200. PMID 12244115.
    • Teng-Umnuay P, van der Wel H, West CM (1999). "Identification of a UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase in the cytoplasm of Dictyostelium". J. Biol. Chem. 274 (51): 36392&ndash, 402. doi:10.1074/jbc.274.51.36392. PMID 10593934.
    • West CM, van der Wel H, Gaucher EA (2002). "Complex glycosylation of Skp1 in Dictyostelium: implications for the modification of other eukaryotic cytoplasmic and nuclear proteins". Glycobiology. 12 (2): 17R&ndash, 27R. doi:10.1093/glycob/12.2.17R. PMID 11886837.


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