二苯并噻吩脱硫酶的纯化、表征及结晶。

T Ohshiro, Y Izumi
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引用次数: 15

摘要

从红红红球菌D-1中纯化出参与二苯并噻吩(DBT)脱硫的DszC和DszA,分别为DBT单加氧酶和DBT砜单加氧酶。对这两种酶进行了结晶和酶学表征。我们在非dbt脱硫菌Paenibacillus polymyxa a -1中发现了高活性的黄素还原酶,该酶对DszC和a的活性至关重要,并对其进行了纯化和表征。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Purification, characterization and crystallization of enzymes for dibenzothiophene desulfurization.

DszC and DszA, DBT monooxygenase and DBT sulfone monooxygenase, respectively, involved in dibenzothiophene (DBT) desulfurization, were purified to homogeneity from Rhodococcus erythropolis D-1. The two enzymes were crystallized and enzymologically characterized. We found a high activity of flavin reductase in the non-DBT-desulfurizing bacterium, Paenibacillus polymyxa A-1, which is essential for DszC and A activities, and purified to homogeneity and characterized the enzyme.

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