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

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 s...

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Autor principal: Jenner, Matthew (Autor)
Autor Corporativo: SpringerLink (Online service)
Formato: Electrónico eBook
Idioma:Inglés
Publicado: Cham : Springer International Publishing : Imprint: Springer, 2016.
Edición:1st ed. 2016.
Colección:Springer Theses, Recognizing Outstanding Ph.D. Research,
Temas:
Mass spectroscopy.
Enzymology.
Biotechnology.
Clinical biochemistry.
Mass Spectrometry.
Chemical Bioengineering.
Medical Biochemistry.
Acceso en línea:Texto Completo

MARC

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245 1 0 |a Using Mass Spectrometry for Biochemical Studies on Enzymatic Domains from Polyketide Synthases  |h [electronic resource] /  |c by Matthew Jenner. 
250 |a 1st ed. 2016. 
264 1 |a Cham :  |b Springer International Publishing :  |b Imprint: Springer,  |c 2016. 
300 |a XVIII, 176 p. 136 illus., 99 illus. in color.  |b online resource. 
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490 1 |a Springer Theses, Recognizing Outstanding Ph.D. Research,  |x 2190-5061 
505 0 |a 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. 
520 |a 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 substrates for future PKS engineering. The documentation of this research is a useful reference and guideline for students starting a PhD in this field. 
650 0 |a Mass spectroscopy. 
650 0 |a Enzymology. 
650 0 |a Biotechnology. 
650 0 |a Clinical biochemistry. 
650 1 4 |a Mass Spectrometry. 
650 2 4 |a Enzymology. 
650 2 4 |a Chemical Bioengineering. 
650 2 4 |a Medical Biochemistry. 
710 2 |a SpringerLink (Online service) 
773 0 |t Springer Nature eBook 
776 0 8 |i Printed edition:  |z 9783319327228 
776 0 8 |i Printed edition:  |z 9783319327242 
776 0 8 |i Printed edition:  |z 9783319813554 
830 0 |a Springer Theses, Recognizing Outstanding Ph.D. Research,  |x 2190-5061 
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912 |a ZDB-2-SXC 
950 |a Chemistry and Materials Science (SpringerNature-11644) 
950 |a Chemistry and Material Science (R0) (SpringerNature-43709) 

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