Kojima, Keisuke and Sunagawa, Naoki and Mikkelsen, Nils and Hansson, Henrik and Karkehabadi, Saeid and Samejima, Masahiro and Sandgren, Mats and Igarashi, Kiyohiko
(2022).
Comparison of glycoside hydrolase family 3 β-xylosidases from basidiomycetes and ascomycetes reveals evolutionarily distinct xylan degradation systems.
Journal of Biological Chemistry. 298
:3
, 101670
[Research article]
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Abstract
Xylan is the most common hemicellulose in plant cell walls, though the structure of xylan polymers differs between plant species. Here, to gain a better understanding of fungal xylan degradation systems, which can enhance enzymatic saccharification of plant cell walls in industrial processes, we conducted a comparative study of two glycoside hydrolase family 3 (GH3) β-xylosidases (Bxls), one from the basidiomycete Phanerochaete chrysosporium (PcBxl3), and the other from the ascomycete Trichoderma reesei (TrXyl3A). A comparison of the crystal structures of the two enzymes, both with saccharide bound at the catalytic center, provided insight into the basis of substrate binding at each subsite. PcBxl3 has a substrate-binding pocket at subsite -1, while TrXyl3A has an extra loop that contains additional binding subsites. Furthermore, kinetic experiments revealed that PcBxl3 degraded xylooligosaccharides faster than TrXyl3A, while the KM values of TrXyl3A were lower than those of PcBxl3. The relationship between substrate specificity and degree of polymerization of substrates suggested that PcBxl3 preferentially degrades xylobiose (X2), while TrXyl3A degrades longer xylooligosaccharides. Moreover, docking simulation supported the existence of extended positive subsites of TrXyl3A in the extra loop located at the N-terminus of the protein. Finally, phylogenetic analysis suggests that wood-decaying basidiomycetes use Bxls such as PcBxl3 that act efficiently on xylan structures from woody plants, whereas molds use instead Bxls that efficiently degrade xylan from grass. Our results provide added insights into fungal efficient xylan degradation systems.
Authors/Creators: | Kojima, Keisuke and Sunagawa, Naoki and Mikkelsen, Nils and Hansson, Henrik and Karkehabadi, Saeid and Samejima, Masahiro and Sandgren, Mats and Igarashi, Kiyohiko | ||||
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Title: | Comparison of glycoside hydrolase family 3 β-xylosidases from basidiomycetes and ascomycetes reveals evolutionarily distinct xylan degradation systems | ||||
Series Name/Journal: | Journal of Biological Chemistry | ||||
Year of publishing : | 2022 | ||||
Volume: | 298 | ||||
Number: | 3 | ||||
Article number: | 101670 | ||||
Number of Pages: | 14 | ||||
ISSN: | 0021-9258 | ||||
Language: | English | ||||
Publication Type: | Research article | ||||
Article category: | Scientific peer reviewed | ||||
Version: | Published version | ||||
Copyright: | Creative Commons: Attribution 4.0 | ||||
Full Text Status: | Public | ||||
Subjects: | (A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Biochemistry and Molecular Biology | ||||
Keywords: | glycoside hydrolase family 3, β-xylosidase, xylan, Phanerochaete chrysosporium, Trichoderma reesei | ||||
URN:NBN: | urn:nbn:se:slu:epsilon-p-116296 | ||||
Permanent URL: | http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-p-116296 | ||||
Additional ID: |
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ID Code: | 27275 | ||||
Faculty: | NJ - Fakulteten för naturresurser och jordbruksvetenskap | ||||
Department: | (NL, NJ) > Department of Molecular Sciences (NL, NJ) > Dept. of Molecular Biology (until 131231) | ||||
Deposited By: | SLUpub Connector | ||||
Deposited On: | 08 Mar 2022 10:25 | ||||
Metadata Last Modified: | 08 Mar 2022 10:31 |
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