Applications of protein engineering to members of the old yellow enzyme family.
In the 20 years since Massey's initial report in 1995, interest in using alkene reductases to prepare chiral intermediates for synthesis has grown rapidly. While native alkene reductases often show very high stereoselectivities toward favorable substrates, these enzymes have somewhat size-restricted active sites that limit their substrate ranges to small alkenes. In addition, most alkene reductases have the same stereoselectivities, which makes it difficult to access the "other" product enantiomers. Protein engineering strategies have been used to address both of these issues and good progress has been made in several cases. This review summarizes published examples through late 2014 and focuses on studies of six enzymes: Saccharomyces pastorianus OYE 1, tomato OPR1, Zymomonas mobilis NCR, Enterobacter cloacae PB2 PETN reductase, Bacillus subtilis YqjM and Pichia stipitis OYE 2.6.
Department of Chemistry, University of Florida, 126 Sisler Hall, Gainesville, FL 32611, USA.
Erica D
ED
Amato
Department of Chemistry, University of Florida, 126 Sisler Hall, Gainesville, FL 32611, USA. Electronic address: jds2@chem.ufl.edu.
Jon D
JD
Stewart
D001709:Biotechnology; D009252:NADPH Dehydrogenase; D015202:Protein Engineering
D009252:NADPH Dehydrogenase
Alkene; Cofactor; Old yellow enzyme; Protein engineering; Reduction