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Enhancement of the Promiscuous Aldolase and Dehydration Activities of 4‐Oxalocrotonate Tautomerase by Protein Engineering
Author(s) -
Zandvoort Ellen,
Geertsema Edzard M.,
Quax Wim J.,
Poelarends Gerrit J.
Publication year - 2012
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200225
Subject(s) - aldolase a , aldol condensation , chemistry , yield (engineering) , dehydration , acetaldehyde , aldol reaction , benzaldehyde , protein engineering , cinnamaldehyde , enzyme , biochemistry , organic chemistry , metabolic engineering , stereochemistry , ethanol , catalysis , materials science , metallurgy
Double play: The enzyme 4‐oxalocrotonate tautomerase (4‐OT) catalyzes not only the initial cross‐coupling of acetaldehyde and benzaldehyde to yield 3‐hydroxy‐3‐phenylpropanal, but also the subsequent dehydration of this aldol compound to yield cinnamaldehyde as the final product. Mechanism‐inspired engineering provided an active site mutant (F50A) with strongly enhanced aldol condensation activity.