Lipopolysaccharide N-acetylmannosaminouronosyltransferase

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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 $\rightleftharpoons$ 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, diphosphoacetylmannosaminuronate-, acetylglucosaminylpyrophosphorylundecaprenol, and acetylmannosaminuronosyltransferase.

[edit] References

IUBMB entry for 2.4.1.180
BRENDA references for 2.4.1.180 (Recommended.)
PubMed references for 2.4.1.180
PubMed Central references for 2.4.1.180
Google Scholar references for 2.4.1.180
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: 228–33. PMID 3275612.