EC - Xylosyl α-1,3-xylosyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
xylosyl α-1,3-xylosyltransferase
Systematic name:
UDP-α-D-xylose:[EGF-like domain protein]-3-O-[α-D-xylosyl-(1→3)-β-D-glucosyl]-L-serine 3-α-D-xylosyltransferase (configuration-retaining)



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. When present on Notch proteins, the trisaccharide functions as a modulator of the signalling activity of this protein. Formerly EC 2.4.2.n3.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0140560


  1. Sethi, M. K., Buettner, F. F., Ashikov, A., Krylov, V. B., Takeuchi, H., Nifantiev, N. E., Haltiwanger, R. S., Gerardy-Schahn, R., Bakker, H.
    Molecular cloning of a xylosyltransferase that transfers the second xylose to O-glucosylated epidermal growth factor repeats of notch.
    J. Biol. Chem. 287 : 2739-2748 (2012). [PMID: 22117070]
  2. Minamida, S., Aoki, K., Natsuka, S., Omichi, K., Fukase, K., Kusumoto, S., Hase, S.
    Detection of UDP-D-xylose: alpha-D-xyloside alpha 1→3xylosyltransferase activity in human hepatoma cell line HepG2.
    J. Biochem. 120 : 1002-1006 (1996). [PMID: 8982869]
  3. Yu, H., Takeuchi, M., LeBarron, J., Kantharia, J., London, E., Bakker, H., Haltiwanger, R. S., Li, H., Takeuchi, H.
    Notch-modifying xylosyltransferase structures support an SNi-like retaining mechanism.
    Nat. Chem. Biol. 11 : 847-854 (2015). [PMID: 26414444]

[EC created 2020]