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Title: Structural and biochemical studies of the actinorhodin polyketide synthase ketoreductase
Author: Teartasin, Watchrra
ISNI:       0000 0004 2671 8272
Current Institution: University of Bristol
Date of Award: 2008
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Polyketides are a diverse group of biologically active natural products synthesized by the poiyketide synthase (PKS) family of enzymes. Bacterial Type II PKS are discrete multienzyme systems consisting of acyl carrier protein (ACP), ketosynthase (KS), chain length factor (CLF), ketoreductase (KR), aromatase (ARO) and cyclase (CYC) amongst other enzymes required for tailoring of the chain. Understanding the structure and biochemistry of the enzymes of the PKS has the potential to allow the targeted biosynthesis of novel compounds. In order to enable such modification the mechanisms by which the PKS controls chain-length, cyclization and reduction must be fully understood.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available