| 书目名称 | Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases |
| 编辑 | Matthew Jenner |
| 视频video | |
| 概述 | 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- |
| 丛书名称 | Springer Theses |
| 图书封面 |  |
| 描述 | .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 mutag |
| 出版日期 | Book 2016 |
| 关键词 | Polyketide Synthases; Mass Spectrometry; Biosynthesis, Enzymes; Ketosynthase; Acyl Hydrolase; Enzymatic D |
| 版次 | 1 |
| doi | https://doi.org/10.1007/978-3-319-32723-5 |
| isbn_softcover | 978-3-319-81355-4 |
| isbn_ebook | 978-3-319-32723-5Series ISSN 2190-5053 Series E-ISSN 2190-5061 |
| issn_series | 2190-5053 |
| copyright | Springer International Publishing Switzerland 2016 |
发表于 2025-3-21 16:18:36
