Ylehd, an epoxide hydrolase with promiscuous haloalkane dehalogenase activity from tropical marine yeast Yarrowia lipolytica is induced upon xenobiotic stress.

ABSTRACT: Recalcitrant environmental pollutants, like bromoorganics and epoxides are hydrolysed with limited substrate specificities by microbial oxygenases, reductases, hydrolases and dehalogenases. Here, we report the identification and characterisation of a protein (XP_504164) from the tropical marine yeast Yarrowia lipolytica NCIM 3589, known to degrade bromoorganics and epoxides. Multiple sequence alignment suggests it belongs to α/β superfamily with conservation of catalytic triad and oxyanion hole motifs. The corresponding gene cloned and protein (Ylehd) expressed in E. coli BL21AI exhibited epoxide hydrolase activity (24 ± 0.7 nmol s^-1 mg^-1 protein) at pH 8.0 and promiscuous haloalkane dehalogenase (1.5 ± 0.2 nmol s^-1 mg^-1 protein) at pH 4.5. Recom

SUBMITTER: Bendigiri C 

PROVIDER: S-EPMC5605520 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature