An alternative route for UDP-diacylglucosamine hydrolysis in bacterial lipid A biosynthesis.

ABSTRACT: The outer leaflet of the outer membranes of Gram-negative bacteria is composed primarily of lipid A, the hydrophobic anchor of lipopolysaccharide. Like Escherichia coli, most Gram-negative bacteria encode one copy of each of the nine genes required for lipid A biosynthesis. An important exception exists in the case of the fourth enzyme, LpxH, a peripheral membrane protein that hydrolyzes UDP-2,3-diacylglucosamine to form 2,3-diacylglucosamine 1-phosphate and UMP by catalyzing the attack of water at the alpha-P atom. Many Gram-negative organisms, including all alpha-proteobacteria and diverse environmental isolates, lack LpxH. Here, we report a distinct UDP-2,3-diacylglucosamine pyrophosphatase, designated LpxI, which has no sequence similarity to LpxH but generates the same products by a d

SUBMITTER: Metzger LE 

PROVIDER: S-EPMC2914816 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature