In enzymology, a lipopolysaccharide 3-alpha-galactosyltransferase (EC 2.4.1.44) is an enzyme that catalyzes the chemical reaction
| lipopolysaccharide 3-alpha-galactosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.44 | ||||||||
| CAS no. | 9073-98-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- UDP-galactose + lipopolysaccharide 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.
Structural studies
editAs of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1GA8 and 1SS9.
References
edit- 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 (9): 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 (6): 3769–74. doi:10.1016/S0021-9258(18)32731-5. PMID 6403519.
