Acyl-acyl carrier protein specificity of UDP-GlcNAc acyltransferases from gram-negative bacteria: relationship to lipid A structure.
Lipid A, the component of lipopolysaccharide that provides the membrane anchor of the core and O-antigen sugars, is known to contain characteristic R-3-hydroxy fatty acids bound to the 2,2' (N-linked) and 3,3' (O-linked) positions of the glucosamine disaccharide in different gram-negative bacteria. The studies reported here show that it is the acyl-acyl carrier protein specificities of the enzymes UDP-GlcNAc-O-acyltransferase and UDP-3-O-[(R)-3-hydroxyacyl]-GlcN-N-acyltransferase that determine the nature of these fatty acids.
Williamson
J M
JM
Department of Biochemistry, Merck Sharp & Dohme Research Laboratories, Rahway, New Jersey 07065.
Anderson
M S
MS
Raetz
C R
CR
D000150:Acinetobacter / Q000201:enzymology*; D000213:Acyl Carrier Protein / Q000737:chemistry*; D000215:Acylation; D000217:Acyltransferases / Q000737:chemistry*; D004755:Enterobacteriaceae; D008050:Lipid A / Q000737:chemistry*; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D012242:Rhodobacter sphaeroides / Q000201:enzymology*
D000213:Acyl Carrier Protein; D008050:Lipid A; D000217:Acyltransferases; C050304:acyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine acyltransferase