|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 126.96.36.199
Enzymes and Genes:
UDP-D-galactose:(glucosyl)lipopolysaccharide-1,6-D-galactosyltransferase : waaB
In Pathway: Lipid A-core biosynthesis
Note that this reaction equation differs from the official Enzyme Commission reaction equations for this EC number.
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: lipopolysaccharide 3-α-galactosyltransferase
Enzyme Commission Synonyms: UDP-galactose:lipopolysaccharide α,3-galactosyltransferase, UDP-galactose:polysaccharide galactosyltransferase, uridine diphosphate galactose:lipopolysaccharide α-3-galactosyltransferase, uridine diphosphogalactose-lipopolysaccharide α,3-galactosyltransferase, UDP-galactose:lipopolysaccharide 3-α-D-galactosyltransferase
Enzyme Commission Summary:
Transfers α-D-galactosyl residues to D-glucose in the partially completed core of lipopolysaccharide [cf. EC 188.8.131.52 (lipopolysaccharide N-acetylglucosaminyltransferase), EC 184.108.40.206 (lipopolysaccharide glucosyltransferase I) and EC 220.127.116.11 (lipopolysaccharide glucosyltransferase II)].
Endo69: 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. PMID: 4898284
Wollin83: 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. PMID: 6403519
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