Rhodococcus erythropolis Oleate Hydratase: a New Member in the Oleate Hydratase Family Tree—Biochemical and Structural Studies. Issue 2 (4th December 2017)

• Record Type: Journal Article
• Authors: Lorenzen, Jan; Driller, Ronja; Waldow, Ayk; Qoura, Farah; Loll, Bernhard; Brück, Thomas
• Is Part Of: ChemCatChem. Volume 10:Issue 2(2018)
• Page Start: 407
• Page End: 414
• Publication Date: 2017-12-04
• Subjects: oleate hydratase -- fatty acids -- hydration -- lyases -- protein structure; Catalysis -- Periodicals; 541.39505
• DOI: 10.1002/cctc.201701350
• Languages: English
• ISSNs: 1867-3880

Abstract

Abstract: 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. Abstract : Genome mining : Oleate hydratase belonging to the HFam3 family, originating from the marine bacterium Rhodococcus erythropolis, is biophysically characterized 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.