Advanced search
Start date
Betweenand
Related content
(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Unlocking the structural features for the xylobiohydrolase activity of an unusual GH11 member identified in a compost-derived consortium

Full text
Author(s):
Kadowaki, Marco A. S. [1, 2] ; Briganti, Lorenzo [1] ; Evangelista, Danilo E. [1, 3] ; Echevarria-Poza, Alberto [4] ; Tryfona, Theodora [4] ; Pellegrini, Vanessa O. A. [1] ; Nakayama, Darlan G. [1] ; Dupree, Paul [4] ; Polikarpov, Igor [1]
Total Authors: 9
Affiliation:
[1] Univ Sao Paulo, Inst Fis Sao Carlos, Grp Biotecnol Mol, Ave Trabalhador Sao Carlense 400, BR-13566590 Sao Carlos, SP - Brazil
[2] Univ Libre Bruxelles, Ecole Interfacultaire Bioingn EIB, PhotoBioCatalysis Biomass Transformat Lab BTL, Brussels - Belgium
[3] Superintendencia Policia Tecn Cient Sao Paulo, Inst Criminalist Andradina, Andradina, SP - Brazil
[4] Univ Cambridge, Dept Biochem, Cambridge - England
Total Affiliations: 4
Document type: Journal article
Source: Biotechnology and Bioengineering; v. 118, n. 10 JUL 2021.
Web of Science Citations: 1
Abstract

The heteropolysaccharide xylan is a valuable source of sustainable chemicals and materials from renewable biomass sources. A complete hydrolysis of this major hemicellulose component requires a diverse set of enzymes including endo-beta-1,4-xylanases, beta-xylosidases, acetylxylan esterases, alpha-l-arabinofuranosidases, and alpha-glucuronidases. Notably, the most studied xylanases from glycoside hydrolase family 11 (GH11) have exclusively been endo-beta-1,4- and beta-1,3-xylanases. However, a recent analysis of a metatranscriptome library from a microbial lignocellulose community revealed GH11 enzymes capable of releasing solely xylobiose from xylan. Although initial biochemical studies clearly indicated their xylobiohydrolase mode of action, the structural features that drive this new activity still remained unclear. It was also not clear whether the enzymes acted on the reducing or nonreducing end of the substrate. Here, we solved the crystal structure of MetXyn11 in the apo and xylobiose-bound forms. The structure of MetXyn11 revealed the molecular features that explain the observed pattern on xylooligosaccharides released by this nonreducing end xylobiohydrolase. (AU)

FAPESP's process: 15/13684-0 - Structural and functional studies of enzymes that participate in complex carbohydrates synthesis and degradation
Grantee:Igor Polikarpov
Support Opportunities: Research Projects - Thematic Grants