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

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

Autor: MATTHEW JENNER
Język: Angielski
Oprawa: Miękka
Wydawca: Springer International Publishing AG
Dostępność: Dostępna u dostawcy
Wysyłamy za 5-8 dni
432.51 zł
This thesis reports studies on the substrate specificity of crucial ketosynthase (KS) domains from t...

Informacje o książce

Autor
MATTHEW JENNER
Język
Angielski
Oprawa
Książka - Miękka
Data wydania
2018
strony
176
EAN
9783319813554
ISBN
9783319813554
Enbook ID
19684800
Wydawca
Springer International Publishing AG
Waga
3051
Wymiary
155 x 235 x 11

Pełny opis

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.

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