COVALENT BINDING OF LIPID TO PROTEIN - DIGLYCERIDE AND AMIDE-LINKED FATTY-ACID AT N-TERMINAL END OF MUREIN-LIPOPROTEIN OF ESCHERICHIA-COLI OUTER MEMBRANE
COVALENT BINDING OF LIPID TO PROTEIN - DIGLYCERIDE AND AMIDE-LINKED FATTY-ACID AT N-TERMINAL END OF MUREIN-LIPOPROTEIN OF ESCHERICHIA-COLI OUTER MEMBRANE
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DOI：
10.1111/j.1432-1033.1973.tb02757.x
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发表时间：
1973-01-01
期刊：
影响因子：
--
通讯作者：
BRAUN, V
中科院分区：
文献类型：
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作者：
HANTKE, K;BRAUN, V
描述了脂质的新结构及其与蛋白质（大肠杆菌外膜的胞壁质脂蛋白）的共价连接。位于多肽链 N 末端的甘油基半胱氨酸（S-（丙烷-2',3'-二醇）-3-硫代-2-氨基丙酸）是两个酯键脂肪酸的附着位点。额外的脂肪酸以酰胺形式结合到 N 末端基团上。半胱氨酸上的甘油二酯残基可能源自磷脂途径，因为脂肪酸组成与来自相同细胞的磷脂非常相似。相比之下，65% 的酰胺连接脂肪酸是棕榈酸酯。主要脂肪酸是棕榈酸（53%）、顺式异油酸（20.7%）、9,10-亚甲基十六烷酸（10.6%）和棕榈油酸（9.4%）。甘油基半胱氨酸的结构是通过化学降解含有脂肪酸的化合物、通过[35S]硫酸盐、[35S]半胱氨酸、 [14C]胱氨酸、[甲基-3H]蛋氨酸和[2-3H]甘油以及通过化学合成。甘油基半胱氨酸作为肽 (Ser)-Ser-Am-Ala-Lys 的成分被分离出来。脂肽序列的C端部分与已知的多肽链序列的N端部分重叠。用溴化氰切割后，通过分离 N 端多肽片段（位置 1-31）来确认其 N 端位置。其中含有脂质。
A new structure of a lipid and its covalent linkage to a protein (murein‐lipoprotein of theEscherichia coliouter membrane) is described. Glycerylcysteine (S‐(propane‐2′,3′‐diol)‐3‐thio‐2‐aminopropanic acid) at the N‐terminal end of the polypeptide chain is the attachment site of two ester‐bound fatty acids. An additional fatty acid is bound as amide to the N‐terminal group. The diglyceride residue on the cysteine could be derived from the phospholipid pathway since the fatty acid composition is very similar to that of the phospholipids from the same cells. In contrast, 65% of the amide‐linked fatty acid is palmitate. The main fatty acids are palmitic acid (53%),cis‐vaccenic acid (20.7%), 9,10‐methylene‐hexadecanoic acid (10.6%) and palmitoleic acid (9.4%).The structure of glycerylcysteine was established by chemical degradation of the compound containing the fatty acids, by incorporation studies of [35S]sulfate, [35S]cysteine, [14C]cystine, [methyl‐3H]methionine and [2‐3H]glycerol and by chemical synthesis. Glycerylcysteine was isolated as a constituent of the peptide (Ser)‐Ser‐Am‐Ala‐Lys. The C‐terminal part of the lipopeptide sequence overlaps with the N‐terminal end of the known sequence of the polypeptide chain. Its N‐terminal position was confirmed by isolation of the N‐terminal polypeptide fragment (position 1–31) after cleavage with cyanogen bromide. This contained the lipid.