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Rhodococcus erythropolis Oleate Hydratase: a New Member in the Oleate Hydratase Family Tree—Biochemical and Structural Studies
ChemCatChem ( IF 3.8 ) Pub Date : 2017-12-04 , DOI: 10.1002/cctc.201701350
Jan Lorenzen 1 , Ronja Driller 2 , Ayk Waldow 2 , Farah Qoura 1 , Bernhard Loll 2, 3 , Thomas Brück 1
Affiliation  

Recently, the enzyme family of oleate hydratases (OHs: EC 4.2.1.53) has gained increasing scientific and economic interest, as these FAD‐binding bacterial enzymes do not require cofactor recycling and possess high thermal and pH stability. Their products, hydroxy fatty acids, are used in specialty chemical applications including surfactant and lubricant formulations. The “oleate hydratase engineering database”, established by Schmid et al. (2017), divides all OHs into 11 families (HFam1 to 11). To date, only two crystal structures of homodimeric OHs from the families HFam2 and HFam11 have been reported. In this study, we biophysically characterized an OH belonging to the HFam3 family, originating from the marine bacterium Rhodococcus erythropolis, for the first time. The crystal structure revealed that this new OH (OhyRe) surprisingly is a monomer in its active form. This particular feature provides new avenues for enzyme engineering and recycling through immobilization.

中文翻译:

红球菌油酸水合酶:油酸水合酶家族树的新成员—生化和结构研究

近年来,油酸水合酶(OHs:EC 4.2.1.53)的酶家族获得了越来越高的科学和经济利益,因为这些与FAD结合的细菌酶不需要辅助因子的循环并且具有很高的热稳定性和pH稳定性。他们的产品羟基脂肪酸用于特殊化学应用,包括表面活性剂和润滑剂配方。Schmid等人建立的“油酸水合酶工程数据库”。(2017),将所有OH分为11个家族(HFam1至11)。迄今为止,仅报道了来自HFam2和HFam11家族的同型二聚OH的两个晶体结构。在这项研究中,我们对属于HFam3家族的OH进行了生物学上的表征,其起源于海洋细菌红球菌(Rhodococcus erythropolis),这是第一次。晶体结构表明,这种新的OH(OhyRe)令人惊讶地是其活性形式的单体。此特定功能为酶工程化和通过固定化回收提供了新途径。
更新日期:2017-12-04
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