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

Please use this identifier to cite or link to this item: 192.168.6.56/handle/123456789/74640

Full metadata record

DC Field	Value	Language
dc.contributor.author	Jenner, Matthew	-
dc.date.accessioned	2019-07-01T07:03:17Z	-
dc.date.available	2019-07-01T07:03:17Z	-
dc.date.issued	2016	-
dc.identifier.isbn	978-3-319-32723-5	-
dc.identifier.uri	http://10.6.20.12:80/handle/123456789/74640	-
dc.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.	en
dc.language	en	en
dc.language.iso	en	en_US
dc.publisher	Springer International Publishing Switzerland	en_US
dc.subject	Biochemical Studies	en_US
dc.title	Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases	en_US
dc.type	Book	en_US
Appears in Collections:	Chemistry

Files in This Item:

File	Description	Size	Format
2016_Book_UsingMassSpectrometryForBioche.pdf		14.29 MB	Adobe PDF	View/Open