Lipopolysaccharide 3-alpha-galactosyltransferase

From Wikipedia, the free encyclopedia

In enzymology, a lipopolysaccharide 3-alpha-galactosyltransferase (EC 2.4.1.44) is an enzyme that catalyzes the chemical reaction

UDP-galactose + lipopolysaccharide $\rightleftharpoons$ UDP + 3-alpha-D-galactosyl-[lipopolysaccharide glucose]

Thus, the two substrates of this enzyme are UDP-galactose and lipopolysaccharide, whereas its two products are UDP and [[3-alpha-D-galactosyl-[lipopolysaccharide glucose]]].

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-galactose:lipopolysaccharide 3-alpha-D-galactosyltransferase. Other names in common use include UDP-galactose:lipopolysaccharide alpha,3-galactosyltransferase, UDP-galactose:polysaccharide galactosyltransferase, uridine diphosphate galactose:lipopolysaccharide, alpha-3-galactosyltransferase, uridine diphosphogalactose-lipopolysaccharide, and alpha,3-galactosyltransferase. This enzyme participates in lipopolysaccharide biosynthesis and glycan structures - biosynthesis 2.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1GA8 and 1SS9.

[edit] References

IUBMB entry for 2.4.1.44
BRENDA references for 2.4.1.44 (Recommended.)
PubMed references for 2.4.1.44
PubMed Central references for 2.4.1.44
Google Scholar references for 2.4.1.44
Endo A, Rothfield L (1969). "Studies of a phospholipid-requiring bacterial enzyme. I Purification and properties of uridine diphosphate galactose: lipopolysaccharide alpha-3-galactosyl transferase". Biochemistry. 8: 3500–7. doi:10.1021/bi00837a003. PMID 4898284.
Wollin R, Creeger ES, Rothfield LI, Stocker BA, Lindberg AA (1983). "Salmonella typhimurium mutants defective in UDP-D-galactose:lipopolysaccharide alpha 1,6-D-galactosyltransferase. Structural, immunochemical, and enzymologic studies of rfaB mutants". J. Biol. Chem. 258: 3769–74. PMID 6403519.