Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.495817
Title: Structural and biochemical studies of the actinorhodin polyketide synthase ketoreductase
Author: Teartasin, Watchrra
Awarding Body: UNIVERSITY OF BRISTOL
Current Institution: University of Bristol
Date of Award: 2008
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Abstract:
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: uk.bl.ethos.495817  DOI: Not available
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