Home About Browse Search
Svenska


Comparison of glycoside hydrolase family 3 β-xylosidases from basidiomycetes and ascomycetes reveals evolutionarily distinct xylan degradation systems

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]

[img] PDF
3MB

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
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:
Type of IDID
DOI10.1016/j.jbc.2022.101670
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

Repository Staff Only: item control page

Downloads

Downloads per year (since September 2012)

View more statistics

Downloads
Hits