Abstract A β-ketoacyl-ACP reductase (FabG) gene from Bacillus sp. ECU0013 was heterologously overexpressed in Escherichia coli and the encoded protein was purified to homogeneity. The recombinant reductase could reduce a broad spectrum of prochiral ketones including aromatic ketones and keto esters and showed the highest activity in the asymmetric reduction of ethyl 2-oxo-4-phenylbutyrate (OPBE). Using E. coli cells ...
[Lloyd-Jones, Guy C.; Wall, Philip D.; Slaughter, Jennifer L.; Parker, Alexandra J.; Laffan, David P. Tetrahedron, 2006 , vol. 62, # 49 p. 11402 - 11412]
[Lloyd-Jones, Guy C.; Wall, Philip D.; Slaughter, Jennifer L.; Parker, Alexandra J.; Laffan, David P. Tetrahedron, 2006 , vol. 62, # 49 p. 11402 - 11412]