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Newly Discovered Penicillin Acylase Activity of Aculeacin A Acylase from Actinoplanes utahensis

机译:犹他州猕猴桃的Aculeacin A酰基转移酶新发现的青霉素酰基转移酶活性

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摘要

Aculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans revealed acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins. Penicillin K was the best substrate, showing a catalytic efficiency of 34.79 mM?1 s?1. Furthermore, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5°C.
机译:链霉菌青霉菌产生的来自犹他猕猴桃的放线菌素A酰基转移酶显示出能够水解青霉素V和几种天然脂肪族青霉素的酰基转移酶活性。青霉素K是最好的底物,显示出34.79 mM?1 s?1的催化效率。此外,阿古霉素A酰基转移酶高度稳定,中点转变温度为81.5°C。

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