A组链球菌中脂磷壁酸酶促脱酰作用的特性与定位
Characterization and localization of the enzymatic deacylation of lipoteichoic acid in group A streptococci.
作者信息
Kessler R E, van de Rijn I, McCarty M
出版信息
J Exp Med. 1979 Dec 1;150(6):1498-509. doi: 10.1084/jem.150.6.1498.
Abstract
Protoplasts of a group A streptococcal strain were shown to contain enzymatic activity capable of converting lipoteichoic acid (LTA) to deacylated lipoteichoic acid (dLTA). The enzyme(s) appear to be located mainly in the membrane, although activity was also found in the cytoplasm. Determination of the sites of cleavage within the LTA molecule was approached by comparing the chemical composition of LTA and native dLTA. Native dLTA, as distinguished from chemically deacylated LTA, was isolated from buffer in which live streptococci had been resuspended and incubated. The chemical data suggest that the enzyme(s) was(were) lipolytic in nature; that is, the conversion of LTA to dLTA was the result of cleavage of the ester linkages between the fatty acids and the remainder of the LTA molecule.
摘要
研究表明，A 组链球菌菌株的原生质体含有能够将脂磷壁酸（LTA）转化为去酰基脂磷壁酸（dLTA）的酶活性。这些酶似乎主要位于细胞膜中，不过在细胞质中也发现了活性。通过比较 LTA 和天然 dLTA 的化学组成来确定 LTA 分子内的裂解位点。与化学去酰基 LTA 不同，天然 dLTA 是从悬浮有活链球菌并进行孵育的缓冲液中分离得到的。化学数据表明，这些酶本质上是脂解酶；也就是说，LTA 向 dLTA 的转化是脂肪酸与 LTA 分子其余部分之间酯键断裂的结果。
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