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A family 10 Thermoascus aurantiacus xylanase utilizes arabinose decorations of xylan as significant substrate specificity determinants

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National Technical University of Athens   

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Digital Library of National Technical University of Athens | Dspace@NTUA   

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A family 10 Thermoascus aurantiacus xylanase utilizes arabinose decorations of xylan as significant substrate specificity determinants (EN)
Christakopoulos, P (EN)
Gilbert, HJ (EN)
Vardakou, M (EN)
Lewis, RJ (EN)
Murray, JW (EN)
Flint, J (EN)
journalArticle (EN)
2014-03-01T01:21:43Z
2005 (EN)
Xylan, which is a key component of the plant cell wall, consists of a backbone of beta-1,4-linked xylose residues that are decorated with arabinofuranose, acetyl, 4-O-methyl D-glucuronic acid and ferulate. The backbone of xylan is hydrolysed by endo-beta 1,4-xylanases (xylanases); however, it is unclear whether the various side-chains of the polysaccharide are utilized by these enzymes as significant substrate specificity determinants. To address this question we have determined the crystal structure of a family 10 xylanase from Thermoascus aurantiacus, in complex with xylobiose containing an arabinofuranosyl-ferulate side-chain. We show that the distal glycone subsite of the enzyme makes extensive direct and indirect interactions with the arabinose side-chain, while the ferulate moiety is solvent-exposed. Consistent with the 3D structural data, the xylanase displays fourfold more activity against xylotriose in which the non-reducing moiety is linked to an arabinose side-chain, compared to the undecorated form of the oligosacchairde. These data indicate that the sugar decorations of xylans in the T. aurantiacus family 10 xylanase, rather than simply being accommodated, can be significant substrate specificity determinants. (c) 2005 Elsevier Ltd. All rights reserved. (EN)
Biochemistry & Molecular Biology (EN)
Multigene Family (EN)
protein interaction (EN)
Xylan (EN)
Eurotiales (EN)
Substrate Specificity (EN)
catalysis (EN)
Crystallography, X-Ray (EN)
Chromatography, High Pressure Liquid (EN)
Cell Wall (EN)
Arabinose (EN)
Xylanase (EN)
plant cell (EN)
enzyme activity (EN)
Thermoascus aurantiacus (EN)
priority journal (EN)
Xylans (EN)
Protein Structure, Tertiary (EN)
xylan endo 1,3 beta xylosidase (EN)
Thermoascus (EN)
3D structure (EN)
article (EN)
Xylose (EN)
controlled study (EN)
crystal structure (EN)
nonhuman (EN)
Kinetics (EN)
Plant Diseases (EN)
Endo-1,4-beta Xylanases (EN)
Journal of Molecular Biology (EN)
Αγγλική γλώσσα
ACADEMIC PRESS LTD ELSEVIER SCIENCE LTD (EN)
National Technical University of Athens
Digital Library of National Technical University of Athens | Dspace@NTUA
Κεντρική Βιβλιοθήκη Ε.Μ.Π.
Ιδρυματικό Αποθετήριο
Δημοσιεύσεις μελών Δ.Ε.Π. σε περιοδικά



*Η εύρυθμη και αδιάλειπτη λειτουργία των διαδικτυακών διευθύνσεων των συλλογών (ψηφιακό αρχείο, καρτέλα τεκμηρίου στο αποθετήριο) είναι αποκλειστική ευθύνη των αντίστοιχων Φορέων περιεχομένου.