Fucosylgalactoside 3-alpha-galactosyltransferase

In enzymology, a fucosylgalactoside 3-alpha-galactosyltransferase (EC 2.4.1.37) is an enzyme that catalyzes the chemical reaction

fucosylgalactoside 3-alpha-galactosyltransferase
Identifiers
EC no.2.4.1.37
CAS no.37257-33-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins
UDP-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R UDP + alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl(1->2)]-D-galactosyl-R

Thus, the two substrates of this enzyme are UDP-galactose and [[alpha-L-fucosyl-(1->2)-D-galactosyl-R]], whereas its two products are UDP and [[alpha-D-galactosyl-(1->3)-[alpha-L-fucosyl(1->2)]-D-galactosyl-R]].

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:alpha-L-fucosyl-(1->2)-D-galactoside 3-alpha-D-galactosyltransferase. Other names in common use include UDP-galactose:O-alpha-L-fucosyl(1->2)D-galactose, alpha-D-galactosyltransferase, UDPgalactose:glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose, 3-alpha-D-galactosyltransferase, [blood group substance] alpha-galactosyltransferase, blood-group substance B-dependent galactosyltransferase, glycoprotein-fucosylgalactoside alpha-galactosyltransferase, histo-blood group B transferase, and histo-blood substance B-dependent galactosyltransferase. This enzyme participates in 3 metabolic pathways: glycosphingolipid biosynthesis - lactoseries, glycosphingolipid biosynthesis - neo-lactoseries, and glycan structures - biosynthesis 2.

Structural studies

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As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1R7U, 1R7X, 1R80, 1R82, 2A8W, 2PGV, and 2PGY.

References

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  • Race C, Ziderman D, Watkins WM (1968). "An α-d-galactosyltransferase associated with the blood-group B character". Biochem. J. 107 (5): 733–735. doi:10.1042/bj1070733. PMC 1198729. PMID 16742598.