ACYL-ACYL CARRIER PROTEIN SPECIFICITY OF UDP-GLCNAC ACYLTRANSFERASES FROM GRAM-NEGATIVE BACTERIA - RELATIONSHIP TO LIPID-A STRUCTURE

被引:56
作者
WILLIAMSON, JM [1 ]
ANDERSON, MS [1 ]
RAETZ, CRH [1 ]
机构
[1] MERCK SHARP & DOHME LTD,DEPT BIOCHEM,POB 2000,RAHWAY,NJ 07065
关键词
D O I
10.1128/jb.173.11.3591-3596.1991
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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-[f(R)-3-hydroxyacyl]-GlcN-N-acyltransferase that determine the nature of these fatty acids.
引用
收藏
页码:3591 / 3596
页数:6
相关论文
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