Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases

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Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases



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English | May 29, 2016 | ISBN: 3319327224 | 176 pages | PDF | 14 mb

This thesis reports studies on the substrate specificity of crucial ketosynthase (KS) domains from trans-AT Polyketide Synthases (PKSs). Using a combination of electrospray ionisation-mass spectrometry (ESI-MS) and simple N-acetyl cysteamine (SNAC) substrate mimics, the specificity of a range of KS domains from the bacillaene and psymberin PKSs have been succsessfully studied with regard to the initial acylation step of KS-catalysis.

In addition, the ability to alter the substrate tolerance of KS domains by simple point mutations in the active site has been demonstrated. A series of acyl-ACPs have been synthesised using a novel methodology and employed to probe the substrate specificity of both KS domains and the previously uncharcterised acyl hydrolase domain, PedC.

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