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 + H<sub>2</sub>O UDP-3-O-[(3R)-3-hydroxymyristoyl]-<small>D</small>-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.
References
External links