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Molecular Basis of Celmer's Rules: Stereochemistry of Catalysis by Isolated Ketoreductase Domains from Modular Polyketide Synthases

Molecular Basis of Celmer's Rules: Stereochemistry of Catalysis by Isolated Ketoreductase Domains from Modular Polyketide Synthases

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SISKOS, Alexandros P., Abel BAERGA-ORTIZ, Shilpa BALI, Viktor STEIN, Hassan MAMDANI, Dieter SPITELLER, Bojana POPOVIC, Jonathan B. SPENCER, James STAUNTON, Kira J. WEISSMAN, Peter F. LEADLAY, 2005. Molecular Basis of Celmer's Rules: Stereochemistry of Catalysis by Isolated Ketoreductase Domains from Modular Polyketide Synthases. In: Chemistry & Biology. 12(10), pp. 1145-1153. ISSN 1074-5521. Available under: doi: 10.1016/j.chembiol.2005.08.017

@article{Siskos2005-10Molec-15509, title={Molecular Basis of Celmer's Rules: Stereochemistry of Catalysis by Isolated Ketoreductase Domains from Modular Polyketide Synthases}, year={2005}, doi={10.1016/j.chembiol.2005.08.017}, number={10}, volume={12}, issn={1074-5521}, journal={Chemistry & Biology}, pages={1145--1153}, author={Siskos, Alexandros P. and Baerga-Ortiz, Abel and Bali, Shilpa and Stein, Viktor and Mamdani, Hassan and Spiteller, Dieter and Popovic, Bojana and Spencer, Jonathan B. and Staunton, James and Weissman, Kira J. and Leadlay, Peter F.} }

Baerga-Ortiz, Abel 2011-10-20T08:25:44Z Siskos, Alexandros P. Staunton, James Spiteller, Dieter Spiteller, Dieter Popovic, Bojana Mamdani, Hassan Leadlay, Peter F. Molecular Basis of Celmer's Rules: Stereochemistry of Catalysis by Isolated Ketoreductase Domains from Modular Polyketide Synthases Baerga-Ortiz, Abel Publ. in: Chemistry & Biology ; 12 (2005), 10. - S. 1145-1153 Leadlay, Peter F. 2005-10 Staunton, James deposit-license 2011-10-20T08:25:44Z Stein, Viktor Spencer, Jonathan B. Bali, Shilpa Popovic, Bojana Stein, Viktor eng Spencer, Jonathan B. Weissman, Kira J. Siskos, Alexandros P. A system is reported for the recombinant expression of individual ketoreductase (KR) domains from modular polyketide synthases (PKSs) and scrutiny of their intrinsic specificity and stereospecificity toward surrogate diketide substrates. The eryKR1 and the tylKR1 domains, derived from the first extension module of the erythromycin PKS and the tylosin PKS, respectively, both catalyzed reduction of (2R, S)-2-methyl-3-oxopentanoic acid N-acetylcysteamine thioester, with complete stereoselectivity and stereospecificity, even though the substrate is not tethered to an acyl carrier protein or an intact PKS multienzyme. In contrast, and to varying degrees, the isolated enzymes eryKR2, eryKR5, and eryKR6 exercised poorer control over substrate selection and the stereochemical course of ketoreduction. These data, together with modeling of diketide binding to KR1 and KR2, demonstrate the fine energetic balance between alternative modes of presentation of ketoacylthioester substrates to KR active sites. Bali, Shilpa Mamdani, Hassan Weissman, Kira J.

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