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Structural and functional studies of two esterases (Est25and Est‐Y29) from metagenome library
Author(s) -
Kim Seungbum,
Yoon Sangyoung,
Jo Do Hyun,
Kim T. Doohun,
Ryu Yeonwoo
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.lb92
Subject(s) - ketoprofen , enzyme , chemistry , substrate (aquarium) , metagenomics , stereochemistry , kinetic resolution , drug , substrate specificity , biochemistry , combinatorial chemistry , catalysis , pharmacology , biology , enantioselective synthesis , chromatography , gene , ecology
Enzymes with high enantioselectivity are highly useful for making several industrial processes such as preparation of pharmaceutical intermediates. Two esterases (Est 25 and Est‐Y29), which are identified from a metagenomic library, catalyze the kinetic resolution of (R/S)‐ketoprofen ethylester for the production of the anti‐inflammatory drug, (S)‐ketoprofen. Substrate binging site of these esterases were mutated to increase their stability and enantioselectiviy of enzyme. W68K and L255W of Est 25 and F137W and R237A of Est Y29, present much higher enantioselectivity.