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UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine Deacetylase (LpxC)
- Target
- LpxC
- Molecular classification
- Enzyme, Metalloenzyme, Deacetylase
01
Overview
UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase (LpxC) is a zinc-dependent metalloenzyme found in Gram-negative bacteria that catalyzes the committed step in lipid A biosynthesis by removing the acetyl group from UDP-3-O-(R)-3-hydroxymyristoyl-N-acetylglucosamine to produce UDP-3-O-(R)-hydroxymyristoyl-glucosamine and acetate. This reaction is essential for the formation of lipid A, which anchors lipopolysaccharide (LPS) to the outer membrane of Gram-negative bacteria. LpxC is a validated antibacterial target due to its essential role in bacterial cell viability and its absence in mammals. Inhibitors of LpxC disrupt lipid A synthesis, leading to bacterial cell death.
- Other names
- UDP-3-O-acyl-N-acetylglucosamine deacetylaseUDP-3-O-[3-hydroxymyristoyl]-N-acetylglucosamine deacetylaseUDP-3-O-N-acetylglucosamine deacetylase
02
Mechanism of action
Inhibition of LpxC, leading to disruption of lipid A biosynthesis
03
Biological functions
Lipid A biosynthesis
04
Disease associations
Infection
05
Safety considerations
Potential for broad-spectrum antibacterial activity impacting commensal bacteriaDevelopment of resistance
06
Interacting drugs
Hydroxamate-based LpxC inhibitors
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