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-mas… Mehr…
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. KS-catalysed chain elongation reactions have also been conducted and monitored by ESI-MS/MS. All KS domains studied exhibited higher substrate specificity at the elongation step than in the preceeding acylation step. Furthermore, a mechanism of reversible acylation is proposed using the PsyA ACP1-KS1 di-domain. 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. eBook Matthew Jenner PDF, Springer, 27.04.2016, Springer, 2016<
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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-mas… Mehr…
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. KS-catalysed chain elongation reactions have also been conducted and monitored by ESI-MS/MS. All KS domains studied exhibited higher substrate specificity at the elongation step than in the preceeding acylation step. Furthermore, a mechanism of reversible acylation is proposed using the PsyA ACP1-KS1 di-domain. 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. eBook Matthew Jenner 27.04.2016, Springer, Springer<
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Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases - 1st ed. 2016: ab 96.49 € eBooks > Fachthemen & Wissenschaft > Wissenschaften allgemein, Sp… Mehr…
Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases - 1st ed. 2016: ab 96.49 € eBooks > Fachthemen & Wissenschaft > Wissenschaften allgemein, Springer-Verlag GmbH<
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(*) Derzeit vergriffen bedeutet, dass dieser Titel momentan auf keiner der angeschlossenen Plattform verfügbar ist.
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-mas… Mehr…
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. KS-catalysed chain elongation reactions have also been conducted and monitored by ESI-MS/MS. All KS domains studied exhibited higher substrate specificity at the elongation step than in the preceeding acylation step. Furthermore, a mechanism of reversible acylation is proposed using the PsyA ACP1-KS1 di-domain. 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. eBook Matthew Jenner PDF, Springer, 27.04.2016, Springer, 2016<
Nr. 47746299. Versandkosten:, Sofort per Download lieferbar, zzgl. Versandkosten. (EUR 8.00)
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-mas… Mehr…
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. KS-catalysed chain elongation reactions have also been conducted and monitored by ESI-MS/MS. All KS domains studied exhibited higher substrate specificity at the elongation step than in the preceeding acylation step. Furthermore, a mechanism of reversible acylation is proposed using the PsyA ACP1-KS1 di-domain. 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. eBook Matthew Jenner 27.04.2016, Springer, Springer<
Nr. 47746299. Versandkosten:, Sofort per Download lieferbar, CH. (EUR 0.00)
Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases - 1st ed. 2016: ab 96.49 € eBooks > Fachthemen & Wissenschaft > Wissenschaften allgemein, Sp… Mehr…
Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases - 1st ed. 2016: ab 96.49 € eBooks > Fachthemen & Wissenschaft > Wissenschaften allgemein, Springer-Verlag GmbH<
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Detailangaben zum Buch - Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases
EAN (ISBN-13): 9783319327235 Erscheinungsjahr: 2016 Herausgeber: Springer International Publishing
Buch in der Datenbank seit 2016-05-27T15:09:51+02:00 (Berlin) Detailseite zuletzt geändert am 2024-04-25T09:07:27+02:00 (Berlin) ISBN/EAN: 9783319327235
ISBN - alternative Schreibweisen: 978-3-319-32723-5 Alternative Schreibweisen und verwandte Suchbegriffe: Autor des Buches: jenner, jenne Titel des Buches: biochemic
Daten vom Verlag:
Autor/in: Matthew Jenner Titel: Springer Theses; Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases Verlag: Springer; Springer International Publishing 176 Seiten Erscheinungsjahr: 2016-04-27 Cham; CH Sprache: Englisch 96,29 € (DE) 99,00 € (AT) 118,00 CHF (CH) Available XVIII, 176 p. 136 illus., 99 illus. in color.
EA; E107; eBook; Nonbooks, PBS / Chemie/Theoretische Chemie; Spektroskopie, Spektrochemie, Massenspektrometrie; Verstehen; Polyketide Synthases; Mass Spectrometry; Biosynthesis, Enzymes; Ketosynthase; Acyl Hydrolase; Enzymatic Domains; biochemical engineering; B; Mass Spectrometry; Enzymology; Chemical Bioengineering; Medical Biochemistry; Chemistry and Materials Science; Chemische Biologie; Biotechnologie; Medizinische Chemie, Pharmazeutische Chemie; BB
Introduction.- Materials and Methods.- Substrate Specificity of Ketosynthase Domains Part I: β-Branched Acyl Chains.- Substrate Specificity of Ketosynthase Domains Part II: Amino Acid-Containing Acyl Chains.- Synthesis of Acyl-Acyl Carrier Proteins and their use in Studying Polyketide Synthase Enzymology.- Substrate Specificity of Ketosynthase Domains Part III: Elongation-Based Substrate Specificity. Nominated as an Outstanding Ph.D. thesis by the University of Nottingham Describes novel use of intact MS for the study of enzyme acylation and elongation Comprehensive and accessible review of trans-AT PKS enzymology Majority of thesis published in high-impact journals Includes supplementary material: sn.pub/extras
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