革兰氏阴性菌UDP - N - 乙酰葡糖胺酰基转移酶的酰基 - 酰基载体蛋白特异性：与脂多糖A结构的关系
Acyl-acyl carrier protein specificity of UDP-GlcNAc acyltransferases from gram-negative bacteria: relationship to lipid A structure.
作者信息
Williamson J M, Anderson M S, Raetz C R
机构信息
Department of Biochemistry, Merck Sharp & Dohme Research Laboratories, Rahway, New Jersey 07065.
出版信息
J Bacteriol. 1991 Jun;173(11):3591-6. doi: 10.1128/jb.173.11.3591-3596.1991.
Abstract
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.
摘要
脂多糖的脂质A成分是核心糖和O抗原糖的膜锚定物，已知在不同革兰氏阴性菌中，脂质A含有与葡糖胺二糖的2,2'（N-连接）和3,3'（O-连接）位置结合的特征性R-3-羟基脂肪酸。本文报道的研究表明，决定这些脂肪酸性质的是UDP-GlcNAc-O-酰基转移酶和UDP-3-O-[(R)-3-羟基酰基]-GlcN-N-酰基转移酶的酰基-酰基载体蛋白特异性。
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