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| Home / Publications / Polyketide Synthases: DEBS Thioesterase | |||||||||||||||||||||
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Polyketide Synthases: DEBS ThioesteraseThe Structure of a Ketoreductase Determines the Organization of the beta-Carbon Processing Enzymes of Modular Polyketide Synthases. Keatinge-Clay, A. T. and Stroud, R. M. (2006) Structure 14, 737-748. The
Structure of a Ketoreductase Determines the Organization of the b-Carbon
Processing Enzymes of Modular Polyketide Synthases.
Adrian T. Keatinge-Clay, and Robert M. Stroud. (2006) Structure 14,
737–748.
An antibiotic factory caught in action. Catalysis, specificity, and ACP docking site of Streptomyces coelicolor
malonyl-CoA: ACP transacylase. Crystal structure and molecular modeling
of 17-DMAG in complex with human Hsp90. Crystal structure of the priming β-ketosynthase from the
R1128 polyketide biosynthetic pathway. Insights into Channel Architecture and Substrate
Specificity from Crystal Structures of Two Macrocycle Forming Thioesterases
of Modular Polyketide Synthases. Crystal structure of the macrocycle-forming thioesterase domain of the
erythromycin polyketide synthases: Versatility from a unique substrate
channel. |
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