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… mais…
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… mais…
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<
Thalia.de
Nr. 47746299. Custos de envio:, Sofort per Download lieferbar, zzgl. Versandkosten. (EUR 6.00) Details...
(*) Livro esgotado significa que o livro não está disponível em qualquer uma das plataformas associadas buscamos.
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… mais…
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<
Orellfuessli.ch
Nr. 47746299. Custos de envio:, Sofort per Download lieferbar, CH. (EUR 0.00) Details...
(*) Livro esgotado significa que o livro não está disponível em qualquer uma das plataformas associadas buscamos.
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… mais…
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. Custos de envio:, 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… mais…
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. Custos de envio:, Sofort per Download lieferbar, zzgl. Versandkosten. (EUR 6.00)
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… mais…
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. Custos de envio:, Sofort per Download lieferbar, CH. (EUR 0.00)
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Dados bibliográficos do melhor livro correspondente
Dados detalhados do livro - Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases
EAN (ISBN-13): 9783319327235 Ano de publicação: 2016 Editor/Editora: Springer International Publishing
Livro na base de dados desde 2016-05-27T10:09:51-03:00 (Sao Paulo) Página de detalhes modificada pela última vez em 2023-12-12T07:56:43-03:00 (Sao Paulo) Número ISBN/EAN: 9783319327235
Número ISBN - Ortografia alternativa: 978-3-319-32723-5 Ortografia alternativa e termos de pesquisa relacionados: Autor do livro: jenner, jenne Título do livro: biochemic
Dados da editora
Autor: Matthew Jenner Título: Springer Theses; Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases Editora: Springer; Springer International Publishing 176 Páginas Ano de publicação: 2016-04-27 Cham; CH Língua: Inglês 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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