一种降解洗涤剂的微生物中伯烷基硫酸酯酶和芳基硫酸酯酶的作用机制。
The mechanism of action of primary alkylsulphohydrolase and arylsulphohydrolase from a detergent-degrading micro-organism.
作者信息
Cloves J M, Dodgson K S, Games D E, Shaw D J, White G F
出版信息
Biochem J. 1977 Dec 1;167(3):843-6. doi: 10.1042/bj1670843.
Abstract
Previous studies have shown that secondary alkylsulphohydrolases from certain detergent-degrading micro-organisms are unusual esterases in that they catalyse fission of the C-O bond of the alkyl sulphate ester linkage. The position of bond fission catalysed by a primary alkylsulphatase and an arylsulphohydrolase present in Pseudomonas C12B has now been investigated. The primary alkylsulphatase behaved like the secondary alkylsulphohydrolases in cleaving the C-O bond of potassium heptan-1-yl sulphate. In contrast, the arylsulphohydrolase, in common with other similar enzymes previously studied, catalysed the fission of the O-S bond of potassium p-nitrophenyl sulphate.
摘要
以往的研究表明，某些降解洗涤剂的微生物中的仲烷基硫酸酯酶是特殊的酯酶，因为它们催化烷基硫酸酯键的C-O键断裂。现在已经研究了假单胞菌C12B中存在的伯烷基硫酸酯酶和芳基硫酸酯酶催化的键断裂位置。伯烷基硫酸酯酶在裂解庚烷-1-基硫酸钾的C-O键时，表现得与仲烷基硫酸酯酶相似。相反，芳基硫酸酯酶与先前研究的其他类似酶一样，催化对硝基苯硫酸钾的O-S键断裂。
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