Converting an esterase into an epoxide hydrolase.
Entering the fold: A common structural motif in hydrolytic enzymes is the alpha,beta-hydrolase fold. The interconversion of one enzyme into another by introduction of mechanistically important residues is not enough; only substitution of a loop allows epoxide hydrolase activity in the esterase scaffold to be formed (see picture; structure comparison of epoxide hydrolases (green) with the esterase (orange)). The result is an enantioselective chimeric enzyme.
Jochens
Helge
H
Institute of Biochemistry, Dept. of Biotechnology & Enzyme Catalysis, University of Greifswald, Felix-Hausdorff-Strasse 4, 17487 Greifswald, Germany.
Stiba
Konstanze
K
Savile
Christopher
C
Fujii
Ryota
R
Yu
Juin-Guo
JG
Gerassenkov
Tatsiana
T
Kazlauskas
Romas J
RJ
Bornscheuer
Uwe T
UT
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D002384:Catalysis; D004851:Epoxide Hydrolases / Q000737:chemistry* / Q000235:genetics; D004950:Esterases / Q000737:chemistry* / Q000235:genetics; D019143:Evolution, Molecular; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D017510:Protein Folding; D013343:Styrenes / Q000737:chemistry; D013379:Substrate Specificity
D013343:Styrenes; D004950:Esterases; D004851:Epoxide Hydrolases