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一株嗜盐细菌分离株中有机磷酸酐酶的纯化及性质

Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate.

作者信息

DeFrank J J, Cheng T C

机构信息

U.S. Army Chemical Research, Development & Engineering Center, Aberdeen Proving Ground, Maryland 21010-5423.

出版信息

J Bacteriol. 1991 Mar;173(6):1938-43. doi: 10.1128/jb.173.6.1938-1943.1991.

Abstract

A moderately halophilic bacterial isolate has been found to possess high levels of enzymatic activity against several highly toxic organophosphorus compounds. The predominant enzyme, designated organophosphorus acid anhydrase 2, has been purified 1,000-fold to homogeneity and characterized. The enzyme is a single polypeptide with a molecular weight of 60,000. With diisopropylfluorophosphate as a substrate, the enzyme has optimum activity at pH 8.5 and 50 degrees C, and it is stimulated by manganese and cobalt.

摘要

已发现一种中度嗜盐细菌分离株对几种剧毒有机磷化合物具有高水平的酶活性。主要酶被命名为有机磷酸酐酶2,已纯化至同质状态,纯化倍数达1000倍,并对其进行了表征。该酶是一种分子量为60000的单一多肽。以二异丙基氟磷酸为底物时,该酶在pH 8.5和50℃下具有最佳活性,并且受到锰和钴的刺激。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cf63/207724/4af6a0a3ea25/jbacter00096-0112-a.jpg

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