Directed mutagenesis alters the stereochemistry of catalysis by isolated 
ketoreductase domains from the erythromycin polyketide synthase

Baerga-Ortiz, A.; Popovic, B.; Siskos, A. P.; O'hare, H. M.; Spiteller, D.; Williams, M. G.; Campillo, N.; Spencer, J. B.; Leadlay, P. F.

doi:10.1016/j.chembiol.2006.01.004

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Directed mutagenesis alters the stereochemistry of catalysis by isolated ketoreductase domains from the erythromycin polyketide synthase

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Spiteller, D.
Department of Bioorganic Chemistry, MPI for Chemical Ecology, Max Planck Society;

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Citation

Baerga-Ortiz, A., Popovic, B., Siskos, A. P., O'hare, H. M., Spiteller, D., Williams, M. G., et al. (2006). Directed mutagenesis alters the stereochemistry of catalysis by isolated ketoreductase domains from the erythromycin polyketide synthase. Chemistry & Biology, 13(3), 277-285. doi:10.1016/j.chembiol.2006.01.004.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-9E7B-E

Abstract

The ketoreductase (KR) domains eryKR(1) and eryKR(2) from the erythromycin-producing polyketide synthase (PKS) reduce 3-ketoacyl-thioester intermediates with opposite stereospecificity. Modeling of eryKR(1) and eryKR(2) showed that conserved amino acids