lipopolysaccharide heptosyltransferase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: a lipopolysaccharide + ADP-L-glycero-beta-D-manno-heptose = a heptosylated lipopolysaccharide + ADP + H+. [MetaCyc:RXN0-5061, MetaCyc:RXN0-5122, MetaCyc:RXN0-5127]

Lipopolysaccharide heptosyltransferase activity is a key enzymatic function involved in the biosynthesis of lipopolysaccharide (LPS), a major component of the outer membrane of Gram-negative bacteria. LPS is a complex glycolipid responsible for various biological activities, including the activation of immune responses and the establishment of bacterial virulence. The enzyme catalyzes the transfer of a heptosyl moiety from a donor molecule, typically UDP-heptose, to a lipid acceptor, which is a precursor molecule of the LPS core oligosaccharide. This transfer reaction is essential for the assembly of the LPS core, which is the structural backbone of the molecule. The heptosyl moiety forms glycosidic bonds with the lipid A moiety of LPS, extending the core oligosaccharide chain. The heptosyltransferase activity is crucial for the proper folding and assembly of the LPS molecule, ensuring its stability and function. It also plays a critical role in the pathogenicity of Gram-negative bacteria by contributing to the formation of a protective outer membrane that shields the bacteria from the host's immune system. Mutations in the genes encoding heptosyltransferases can lead to defects in LPS biosynthesis, resulting in impaired bacterial growth, survival, and virulence.'
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Proteins (1)

Compounds (2)