Lipopolysaccharide glucosyltransferase I
In enzymology, a lipopolysaccharide glucosyltransferase I (EC 2.4.1.58) is an enzyme that catalyzes the chemical reaction
- UDP-glucose + lipopolysaccharide
UDP + D-glucosyl-lipopolysaccharide
Thus, the two substrates of this enzyme are UDP-glucose and lipopolysaccharide, whereas its two products are UDP and D-glucosyl-lipopolysaccharide.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucose:lipopolysaccharide glucosyltransferase. Other names in common use include UDP-glucose:lipopolysaccharide glucosyltransferase I, lipopolysaccharide glucosyltransferase, uridine diphosphate glucose:lipopolysaccharide glucosyltransferase, I, and uridine diphosphoglucose-lipopolysaccharide glucosyltransferase. This enzyme participates in lipopolysaccharide biosynthesis and glycan structures - biosynthesis 2.
References
- Muller E, Hinckley A, Rothfield L (1972). "Studies of phospholipid-requiring bacterial enzymes. 3. Purification and properties of uridine diphosphate glucose:lipopolysaccharide glucosyltransferase I". J. Biol. Chem. 247 (8): 2614–22. PMID 4553445.
- Rothfield L, Osborn MJ and Horecker BL (1964). "Biosynthesis of bacterial lipopolysaccharide. II. Incorporation of glucose and galactose catalyzed by particulate and soluble enzymes in salmonella". J. Biol. Chem. 239: 2788–2795. PMID 14217875.
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