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...

Ful tanımlama

Detaylı Bibliyografya
Yazar: Jenner, Matthew (Yazar)
Müşterek Yazar: SpringerLink (Online service)
Materyal Türü: e-Kitap
Dil:İngilizce
Baskı/Yayın Bilgisi: Cham : Springer International Publishing : 2016.
Imprint: Springer,
Edisyon:1st ed. 2016.
Seri Bilgileri:Springer Theses, Recognizing Outstanding Ph.D. Research,
Konular:
Mass spectroscopy.
Enzymology.
Biotechnology.
Clinical biochemistry.
Mass Spectrometry.
Chemical Bioengineering.
Medical Biochemistry.
Online Erişim:Full-text access
Diğer Bilgiler
Özet: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.
Fiziksel Özellikler:XVIII, 176 p. 136 illus., 99 illus. in color. online resource.
ISBN:9783319327235
ISSN:2190-5061
DOI:10.1007/978-3-319-32723-5

Benzer Materyaller