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

  • Matthew Jenner

Part of the Springer Theses book series (Springer Theses)

About this book

Introduction

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, Matthew Jenner has successfully studied the specificity of a range of KS domains from the bacillaene and psymberin PKSs with regard to the initial acylation step of KS-catalysis. The findings in this thesis provide important insights into mechanisms of KS specificity and show that mutagenesis can be used to expand the repertoire of acceptable substrates for future PKS engineering. The documentation of this research is a useful reference and guideline for students starting a PhD in this field.

Keywords

Polyketide Synthases Mass Spectrometry Biosynthesis, Enzymes Ketosynthase Acyl Hydrolase Enzymatic Domains

Authors and affiliations

  • Matthew Jenner
    • 1
  1. 1.School of Chemistry, University of Warwick,Coventry,United Kingdom

Bibliographic information

  • DOI https://doi.org/10.1007/978-3-319-32723-5
  • Copyright Information Springer International Publishing Switzerland 2016
  • Publisher Name Springer, Cham
  • eBook Packages Chemistry and Materials Science
  • Print ISBN 978-3-319-32722-8
  • Online ISBN 978-3-319-32723-5
  • Series Print ISSN 2190-5053
  • Series Online ISSN 2190-5061
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