Brüx, Christian (2005). Strukturen der beta-D-Xylosidase aus Geobacillus stearothermophilus T-6 in verschiedenen kristallinen und funktionellen Zuständen. PhD thesis, Universität zu Köln.

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Abstract

In dieser Arbeit wird die Struktur der beta-Xylosidase aus Geobacillus stearothermophilus vorgestellt. Die Xylosidase gehört zur Glykosid-Hydrolase Familie 43. Sie zeigt ein fünf flügelige beta-Propeller Faltung. Darüber hinaus werden die Strukturen von drei katalytisch inaktiven Punktmutanten, jeweils kokristallisiert mit den natürlichen Substrat Xylobiose, beschrieben. Die daraus gewonnenen Erkenntnisse erlauben eine strukturelle Erklärung der Quartärstruktur, Reaktionsmechanismus und Spezifität des Enzyms.

Item Type: Thesis (PhD thesis)
Translated title:
TitleLanguage
Structures of the beta-D-Xylosidase from Geobacillus stearothermophilus in different crystalline and functional stateEnglish
Translated abstract:
AbstractLanguage
Here we present the structure of the beta-xylosidase from Geobacillus stearothermophilus. This xylosidase is part of the glycoside hydrolase family 43. It shows a five blade beta propeller fold. Further, the structures of three catalytic inactive point mutations, each cocrystallized with the natural substrate xylobiose, are described. These structures allow a structural understanding of quarternary structure, reaction mechanism and substrate specificity of the enzyme.English
Creators:
CreatorsEmailORCID
Brüx, Christianacc37@uni-koeln.deUNSPECIFIED
URN: urn:nbn:de:hbz:38-16865
Subjects: Life sciences
Uncontrolled Keywords:
KeywordsLanguage
xylosidase , xylose , hemicellulose , struktur , glykosidaseGerman
xylosidase , structure , glycosidase , xyloseEnglish
Faculty: Faculty of Mathematics and Natural Sciences
Divisions: Faculty of Mathematics and Natural Sciences > Institute for Biochmemistry
Language: German
Date: 2005
Date of oral exam: 6 February 2006
Referee:
NameAcademic Title
Schomburg, DietmarProf. Dr.
Full Text Status: Public
Date Deposited: 27 Mar 2006 10:26
URI: http://kups.ub.uni-koeln.de/id/eprint/1686

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