Übersicht			Auf mobile öffnen

Lieferstatus:	Auf Bestellung (Lieferzeit unbekannt)
Veröffentlichung:	Mai 2018
Genre:	Naturwissensch., Medizin, Technik
	B / Biochemical Engineering / biochemistry / Bioprocess Engineering / Chemical biology / Chemistry and Materials Science / Clinical biochemistry / Enzymology / mass spectrometry / Medical Biochemistry / MEDICINAL CHEMISTRY
ISBN:	9783319813554
EAN-Code:	9783319813554
Verlag:	Springer Nature EN
Einband:	Kartoniert
Sprache:	English
Serie:	Springer Theses
Dimensionen:	H 235 mm / B 155 mm / D
Gewicht:	3051 gr
Seiten:	176
Illustration:	XVIII, 176 p. 136 illus., 99 illus. in color., schwarz-weiss Illustrationen, farbige Illustrationen
Zus. Info:	Previously published in hardcover
Bewertung:	Titel bewerten / Meinung schreiben

Inhalt:

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.