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Using mass spectrometry for biochemical studies on enzymatic domains from polyketide synthases[electronic resource] /

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
杜威分類號:	572.45
書名/作者:	Using mass spectrometry for biochemical studies on enzymatic domains from polyketide synthases/ by Matthew Jenner.
作者:	Jenner, Matthew.
出版者:	Cham : : Springer International Publishing :, 2016.
面頁冊數:	xviii, 176 p. : : ill., digital ;; 24 cm.
Contained By:	Springer eBooks
標題:	Polyketides - Spectra.
標題:	Mass spectrometry.
標題:	Chemistry.
標題:	Mass Spectrometry.
標題:	Enzymology.
標題:	Biochemical Engineering.
標題:	Medical Biochemistry.
ISBN:	9783319327235
ISBN:	9783319327228
內容註:	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.
摘要、提要註:	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.
電子資源:	http://dx.doi.org/10.1007/978-3-319-32723-5

Using mass spectrometry for biochemical studies on enzymatic domains from polyketide synthases[electronic resource] /
Jenner, Matthew.

Using mass spectrometry for biochemical studies on enzymatic domains from polyketide synthases[electronic resource] /by Matthew Jenner. - Cham :Springer International Publishing :2016. - xviii, 176 p. :ill., digital ;24 cm. - Springer theses,2190-5053. - Springer theses..

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.

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.

ISBN: 9783319327235

Standard No.: 10.1007/978-3-319-32723-5doiSubjects--Topical Terms:

640365
Polyketides
--Spectra.

LC Class. No.: QP752.P65

Dewey Class. No.: 572.45

Using mass spectrometry for biochemical studies on enzymatic domains from polyketide synthases[electronic resource] /
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