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 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. ACHN-975 CHIR-090 CS250 LPC-233 PF-5081090 TP0586532
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