| EC |
2.4.1.376 |
| Accepted name: |
EGF-domain serine glucosyltransferase |
| Reaction: |
UDP-α-D-glucose + [protein with EGF-like domain]-L-serine = UDP + [protein with EGF-like domain]-3-O-(β-D-glucosyl)-L-serine |
| Other name(s): |
POGLUT1 (gene name) (ambiguous); rumi (gene name) (ambiguous) |
| Systematic name: |
UDP-α-D-glucose:[protein with EGF-like domain]-L-serine O-β-glucosyltransferase (configuration-inverting) |
| Comments: |
The enzyme, found in animals and insects, is involved in the biosynthesis of the α-D-xylosyl-(1→3)-α-D-xylosyl-(1→3)-β-D-glucosyl trisaccharide on epidermal growth factor-like (EGF-like) domains. Glycosylation takes place at the serine in the C-X-S-X-P-C motif. The enzyme is bifunctional also being active with UDP-α-xylose as donor (EC 2.4.2.63, EGF-domain serine xylosyltransferase). When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Li, Z., Fischer, M., Satkunarajah, M., Zhou, D., Withers, S.G. and Rini, J.M. Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1). Nat. Commun. 8:185 (2017). [PMID: 28775322] |
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| [EC 2.4.1.376 created 2020] |
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