UDP-3-O-acyl-N-acetylglucosamine deacetylase
class of enzymes

UDP-3-O-acyl-N-acetylglucosamine deacetylase (EC 3.5.1.108), also known as LpxC, is a zinc-dependent enzyme involved in bacterial lipid A biosynthesis, catalyzing the removal of the acetyl group from UDP-3-O-acyl-N-acetylglucosamine, a key step in the production of lipopolysaccharides in the outer membrane of gram-negative bacteria.
This enzyme catalyses the chemical reaction:
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine + H2O
⇌
{\displaystyle \rightleftharpoons }
UDP-3-O-[(3R)-3-hydroxymyristoyl]-D-glucosamine + acetate
Nomenclature
UDP-3-O-acyl-N-acetylglucosamine deacetylase is also known as:
UDP-3-O-((3R)-3-hydroxymyristoyl)-N-acetylglucosamine amidohydrolase
LpxC enzyme
LpxC deacetylase
deacetylase LpxC
UDP-3-O-acyl-GlcNAc deacetylase
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
UDP-(3-O-acyl)-N-acetylglucosamine deacetylase
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase)
Inhibitors
Various inhibitors of LpxC have been developed as potential antibiotics, though none have yet reached clinical trials.
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This entry incorporates text from “UDP-3-O-acyl-N-acetylglucosamine deacetylase” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.