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Information on EC 2.4.1.229 - [Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase

for references in articles please use BRENDA:EC2.4.1.229
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IUBMB Comments
Skp1 is a cytoplasmic and nuclear protein required for the ubiquitination of cell cycle regulatory proteins and transcriptional factors. In Dictyostelium Skp1 is modified by the linear pentasaccharide Galalpha1-6Galalpha1-L-Fucalpha1-2Galbeta1-3GlcNAc, which is attached to a hydroxyproline residue at position 143. This enzyme catalyses the first step in the building up of the pentasaccharide by attaching an N-acetylglucosaminyl group to the hydroxyproline residue. It requires dithiothreitol and a divalent cation for activity.
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The enzyme appears in viruses and cellular organisms
Synonyms
gnt51, hydroxyproline-capping enzyme, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + [Skp1-protein]-trans-4-hydroxy-L-proline = UDP + [Skp1-protein]-O-(N-acetyl-alpha-D-glucosaminyl)-trans-4-hydroxy-L-proline
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; Requires dithiothreitol and a divalent cation for activity. This enzyme commences the building up of a pentasaccharide (Galalpha1-6Galalpha1-L-Fucalpha1-2Galbeta1-3GlcNAc) on Hyp-143 of the Dictyostelium protein Skp1, which is required for the ubiquitination of cell-cycle regulatory proteins and transcription factors. The fucose residue is probably in the alpha configuration. The specificity of the enzyme for Skp1-Hyp-143 and its high affinity for this substrate suggests that it is the GlcNAc-transferase that modifies Skp1 in vivo
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