Erythromycin Biosynthesis: The β-Ketoreductase Domains Catalyze the Stereospecific Transfer of the 4-pro-SHydride of NADPH
- 19 March 1998
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 120 (13), 3267-3268
- https://doi.org/10.1021/ja980028z
Abstract
No abstract availableThis publication has 20 references indexed in Scilit:
- Femtosecond Dynamics of Electron Localization at InterfacesScience, 1998
- The Molecular Basis of Celmer's Rules: The Stereochemistry of the Condensation Step in Chain Extension on the Erythromycin Polyketide SynthaseBiochemistry, 1997
- Molecular recognition of diketide substrates by a β-ketoacyl-acyl carrier protein synthase domain within a bimodular polyketide synthaseChemistry & Biology, 1997
- Gain-of-Function Mutagenesis of a Modular Polyketide SynthaseJournal of the American Chemical Society, 1997
- A functional chimeric modular polyketide synthase generated via domain replacementChemistry & Biology, 1996
- A hybrid modular polyketide synthase obtained by domain swappingChemistry & Biology, 1996
- Repositioning of a Domain in a Modular Polyketide Synthase to Promote Specific Chain CleavageScience, 1995
- Rational Design of Potent, Bioavailable, Nonpeptide Cyclic Ureas as HIV Protease InhibitorsScience, 1994
- Modular Organization of Genes Required for Complex Polyketide BiosynthesisScience, 1991
- Stereospecificity in Enzymology: Its Place in EvolutionTopics in Stereochemistry, 1989