Please use this identifier to cite or link to this item:
192.168.6.56/handle/123456789/74640
Title: | Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases |
Authors: | Jenner, Matthew |
Keywords: | Biochemical Studies |
Issue Date: | 2016 |
Publisher: | Springer International Publishing Switzerland |
Description: | Polyketides form a group of diverse and structurally complex bioactive natural products. Their biosynthesis is directed by multi-domain polyketide megasynthases (PKSs), which extend the acyl chain by a series of condensation and optional reduction steps. Phylogenetic work has shown that, in a particular group of type I systems known as trans-AT PKSs, the ketosynthase (KS) domains potentially harbour specificity towards the nature of the first four carbons of the intermediate substrate (e.g. beta-hydroxy, enoyl, methyl-branched). These results suggest a close link between KS evolution and substrate specificity. |
URI: | http://10.6.20.12:80/handle/123456789/74640 |
ISBN: | 978-3-319-32723-5 |
Appears in Collections: | Chemistry |
Files in This Item:
File | Description | Size | Format | |
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2016_Book_UsingMassSpectrometryForBioche.pdf | 14.29 MB | Adobe PDF | View/Open |
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