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首页> 外文期刊>Journal of bacteriology >Purification and characterization of a novel extracellular Streptomyces lividans 66 enzyme inactivating fusidic acid.
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Purification and characterization of a novel extracellular Streptomyces lividans 66 enzyme inactivating fusidic acid.

机译：新型胞外链霉菌绿色链霉菌66酶使夫西地酸失活的纯化和鉴定。

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摘要

The wild-type strain Streptomyces lividans 66 is resistant against the steroid-like antibiotic fusidic acid. Comparative studies of the wild-type strain and a fusidic acid-sensitive mutant allowed the identification of an extracellular enzyme which inactivates fusidic acid. With the help of a combination of ultrafiltration and chromatographies with Phenyl-Sepharose and an anion exchanger, the enzyme was highly purified. Its apparent molecular mass is 48 kDa, its optimal activity ranges between 45 and 55 degrees C, and its optimal pH is 6.0 to 9.0. It is stimulated by neither monovalent nor divalent ions. The enzyme acts as a specific esterase which removes the acetyl group at C-16 from fusidic acid. The resulting intermediate is unstable, and spontaneous lactonization between C-21 and C-16 occurs rapidly.
机译：野生型链霉菌链霉菌66对类固醇类抗生素夫西地酸具有抗性。对野生型菌株和夫西地酸敏感突变体的比较研究允许鉴定灭活夫西地酸的细胞外酶。借助于超滤和色谱结合苯基-琼脂糖和阴离子交换剂的组合，该酶被高度纯化。它的表观分子量为48 kDa，最佳活性在45至55摄氏度之间，最佳pH为6.0至9.0。一价或二价离子都不会刺激它。该酶起特定酯酶的作用，可从夫西地酸中除去C-16处的乙酰基。所得中间体不稳定，并且C-21和C-16之间的自发内酯化迅速发生。

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