0000000000201286
AUTHOR
Jinyu Zou
showing 2 related works from this author
Structure of Aspergillus niger epoxide hydrolase at 1.8 A resolution: implications for the structure and function of the mammalian microsomal class o…
2000
AbstractBackground: Epoxide hydrolases have important roles in the defense of cells against potentially harmful epoxides. Conversion of epoxides into less toxic and more easily excreted diols is a universally successful strategy. A number of microorganisms employ the same chemistry to process epoxides for use as carbon sources.Results: The X-ray structure of the epoxide hydrolase from Aspergillus niger was determined at 3.5 Å resolution using the multiwavelength anomalous dispersion (MAD) method, and then refined at 1.8 Å resolution. There is a dimer consisting of two 44 kDa subunits in the asymmetric unit. Each subunit consists of an α/β hydrolase fold, and a primarily helical lid over the…
Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site
2003
Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an alpha/beta hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis, solved using single-wavelength anomalous dispersion from a selenomethionine-substituted protein and refined at 1.2 A resolution. This enzyme represents a completely different structure and a novel one-step mechanism. The fold features a highly curved six-stranded mixed beta-sheet, with four alpha-helices packed onto it to create a …