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Record Nr. |
UNINA9910254029703321 |
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Autore |
Jenner Matthew |
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Titolo |
Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases / / by Matthew Jenner |
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Pubbl/distr/stampa |
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Cham : , : Springer International Publishing : , : Imprint : Springer, , 2016 |
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ISBN |
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Edizione |
[1st ed. 2016.] |
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Descrizione fisica |
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1 online resource (189 p.) |
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Collana |
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Springer Theses, Recognizing Outstanding Ph.D. Research, , 2190-5053 |
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Disciplina |
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Soggetti |
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Mass spectrometry |
Enzymology |
Biochemical engineering |
Medical biochemistry |
Mass Spectrometry |
Biochemical Engineering |
Medical Biochemistry |
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Lingua di pubblicazione |
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Formato |
Materiale a stampa |
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Livello bibliografico |
Monografia |
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Note generali |
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Description based upon print version of record. |
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Nota di bibliografia |
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Includes bibliographical references at the end of each chapters. |
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Nota di contenuto |
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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. |
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Sommario/riassunto |
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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-mass spectrometry (ESI-MS) and simple N-acetyl cysteamine (SNAC) substrate mimics, Matthew Jenner has successfully studied the specificity of a range of KS domains from the bacillaene and psymberin PKSs with regard to the initial acylation step of KS-catalysis. 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 |
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