Procollagen glucosyltransferase
Procollagen glucosyltransferase | |||||||||
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Identifiers | |||||||||
EC number | 2.4.1.66 | ||||||||
CAS number | 9028-08-4 | ||||||||
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 procollagen glucosyltransferase (EC 2.4.1.66) is an enzyme that catalyzes the chemical reaction
- UDP-glucose + 5-(D-galactosyloxy)-L-lysine-procollagen UDP + 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen
Thus, the two substrates of this enzyme are UDP-glucose and 5-(D-galactosyloxy)-L-lysine-procollagen, whereas its two products are UDP and 1,2-D-glucosyl-5-D-(galactosyloxy)-L-lysine-procollagen.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:5-(D-galactosyloxy)-L-lysine-procollagen D-glucosyltransferase. Other names in common use include galactosylhydroxylysine glucosyltransferase, collagen glucosyltransferase, collagen hydroxylysyl glucosyltransferase, galactosylhydroxylysyl glucosyltransferase, UDP-glucose-collagenglucosyltransferase, and uridine diphosphoglucose-collagen glucosyltransferase.
References
- Bosmann HB, Eylar EH (1968). "Attachment of carbohydrate to collagen. Isolation, purification and properties of the glucosyl transferase". Biochem. Biophys. Res. Commun. 30 (1): 89–94. doi:10.1016/0006-291X(68)90717-1. PMID 5637038.
- Bosmann HB, Eylar EH (1968). "Collagen-glucosyl transferase in fibriblasts transformed by oncogenic viruses". Nature. 218 (5141): 582–3. doi:10.1038/218582a0. PMID 4968368.
- Butler WT, Cunningham LW (1966). "Evidence for the linkage of a disaccharide to hydroxylysine in tropocollagen". J. Biol. Chem. 241 (17): 3882–8. PMID 4288358.
- Kivirikko KI; Myllyla R (1979). Hall, D.A.; Jackson, D.S., eds. International Review of Connective Tissue Research. New York: Academic Press. 8: 23. Missing or empty
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