The Structure of a Ketoreductase Determines the Organization of the β-Carbon Processing Enzymes of Modular Polyketide Synthases
Open Access
- 1 April 2006
- Vol. 14 (4) , 737-748
- https://doi.org/10.1016/j.str.2006.01.009
Abstract
No abstract availableKeywords
This publication has 40 references indexed in Scilit:
- Structure and molecular organization of mammalian fatty acid synthaseNature Structural & Molecular Biology, 2005
- Site-directed mutagenesis to enable and improve crystallizability of Candida tropicalis (3R)-hydroxyacyl-CoA dehydrogenaseBiochemical and Biophysical Research Communications, 2004
- Characterization of the β-Carbon Processing Reactions of the Mammalian Cytosolic Fatty Acid Synthase: Role of the Central CoreBiochemistry, 2004
- Cofactor-Induced Conformational Rearrangements Establish a Catalytically Competent Active Site and a Proton Relay Conduit in FabGStructure, 2004
- The Structure of Docking Domains in Modular Polyketide SynthasesChemistry & Biology, 2003
- Enhanced genome annotation using structural profiles in the program 3D-PSSM 1 1Edited by J. ThorntonJournal of Molecular Biology, 2000
- Erythromycin Biosynthesis: The β-Ketoreductase Domains Catalyze the Stereospecific Transfer of the 4-pro-SHydride of NADPHJournal of the American Chemical Society, 1998
- The Molecular Basis of Celmer's Rules: The Stereochemistry of the Condensation Step in Chain Extension on the Erythromycin Polyketide SynthaseBiochemistry, 1997
- A functional chimeric modular polyketide synthase generated via domain replacementChemistry & Biology, 1996
- Crystal Structure ofEscherichia coliQOR Quinone Oxidoreductase Complexed with NADPHJournal of Molecular Biology, 1995