(Skp1-protein)-hydroxyproline N-acetylglucosaminyltransferase
(Skp1-protein)-hydroxyproline N-acetylglucosaminyltransferase | |||||||||
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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 | ||||||||
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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): 46328–37. 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): 36392–402. 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–27R. doi:10.1093/glycob/12.2.17R. PMID 11886837.