ExplorEnz: EC 2.4.1.66

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2.4.1.66

Accepted name:

procollagen glucosyltransferase

Reaction:

UDP-α-D-glucose + [procollagen]-(5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine = UDP + [procollagen]-(5R)-5-O-[α-D-glucosyl-(1→2)-β-D-galactosyl]-5-hydroxy-L-lysine

Other name(s):

galactosylhydroxylysine glucosyltransferase; collagen glucosyltransferase; collagen hydroxylysyl glucosyltransferase; galactosylhydroxylysyl glucosyltransferase; UDP-glucose-collagenglucosyltransferase; uridine diphosphoglucose-collagen glucosyltransferase; UDP-glucose:5-(D-galactosyloxy)-L-lysine-procollagen D-glucosyltransferase; UDP-glucose:(2S,5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine-[procollagen] D-glucosyltransferase

Systematic name:

UDP-α-D-glucose:[procollagen]-(5R)-5-O-(β-D-galactosyl)-5-hydroxy-L-lysine 2-α-D-glucosyltransferase (configuration-retaining)

Comments:

Involved in the synthesis of carbohydrate units in the complement system (cf. EC 2.4.1.50 procollagen galactosyltransferase).

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9028-08-4

References:

1.	Bosmann, H.B. and Eylar, E.H. Attachment of carbohydrate to collagen. Isolation, purification and properties of the glucosyl transferase. Biochem. Biophys. Res. Commun. 30 (1968) 89–94. [DOI] [PMID: 5637038]
2.	Bosmann, H.B. and Eylar, E.H. Collagen-glucosyl transferase in fibriblasts transformed by oncogenic viruses. Nature 218 (1968) 582–583. [PMID: 4968368]
3.	Butler, W.T. and Cunningham, L.W. Evidence for the linkage of a disaccharide to hydroxylysine in tropocollagen. J. Biol. Chem. 241 (1966) 3882–3888. [PMID: 4288358]
4.	Kivirikko, K.I. and Myllyla, R. In: Hall, D.A. and Jackson, D.S. (Ed.), International Review of Connective Tissue Research, vol. 8, Academic Press, New York, 1979, p. 23.
5.	Sricholpech, M., Perdivara, I., Nagaoka, H., Yokoyama, M., Tomer, K.B. and Yamauchi, M. Lysyl hydroxylase 3 glucosylates galactosylhydroxylysine residues in type I collagen in osteoblast culture. J. Biol. Chem. 286 (2011) 8846–8856. [DOI] [PMID: 21220425]

[EC 2.4.1.66 created 1972]