In enzymology, a lipopolysaccharide N-acetylmannosaminouronosyltransferase (EC 2.4.1.180) is an enzyme that catalyzes the chemical reaction
UDP-N-acetyl-beta-D-mannosaminouronate + lipopolysaccharide ⇌ {\displaystyle \rightleftharpoons } UDP + N-acetyl-beta-D-mannosaminouronosyl-1,4-lipopolysaccharide Thus, the two substrates of this enzyme are UDP-N-acetyl-beta-D-mannosaminouronate and lipopolysaccharide, whereas its two products are UDP and N-acetyl-beta-D-mannosaminouronosyl-1,4-lipopolysaccharide. This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-beta-D-mannosaminouronate:lipopolysaccharide N-acetyl-beta-D-mannosaminouronosyltransferase. Other names in common use include ManNAcA transferase, uridine-diphosphoacetylmannosaminuronatetranferase, N-acetylglucosaminylpyrophosphorylundecaprenol glucosyltransferase, and acetylmannosaminuronosyltransferase.
References
Barr K, Ward S, Meier-Dieter U, Mayer H, Rick PD (1988). "Characterization of an Escherichia coli rff mutant defective in transfer of N-acetylmannosaminuronic acid (ManNAcA) from UDP-ManNAcA to a lipid-linked intermediate involved in enterobacterial common antigen synthesis". J. Bacteriol. 170 (1): 228–33. doi:10.1128/jb.170.1.228-233.1988. PMC 210631. PMID 3275612.
