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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Impact of cellulose properties on enzymatic degradation by bacterial GH48 enzymes: Structural and mechanistic insights from processive Bacillus licheniformis Cel48B cellulase

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Araujo, Evandro A. [1, 2] ; Dias, Artur Hermano Sampaio [3, 4] ; Kadowaki, Marco A. S. [1] ; Piyadov, Vasily [1] ; Pellegrini, Vanessa O. A. [1] ; Urio, Mateus B. [5] ; Ramos, Luiz P. [5] ; Skaf, Munir S. ; Polikarpov, Igor [1]
Total Authors: 9
[1] Univ Sao Paulo, Sao Carlos Inst Phys, BR-13560970 Sao Carlos, SP - Brazil
[2] Brazilian Ctr Res Energy & Mat, Brazilian Synchrotron Light Lab LNLS, BR-13083970 Campinas, SP - Brazil
[3] Univ Campinas UNICAMP, Inst Chem, BR-13084862 Campinas, SP - Brazil
[4] Univ Campinas UNICAMP, Ctr Comp Engn & Sci, BR-13084862 Campinas, SP - Brazil
[5] Fed Univ Parana UFPR, Grad Programs Bioenergy Chem & Chem Engn, BR-81531980 Curitiba, Parana - Brazil
Total Affiliations: 5
Document type: Journal article
Source: Carbohydrate Polymers; v. 264, JUL 15 2021.
Web of Science Citations: 0

Processive cellulases are highly efficient molecular engines involved in the cellulose breakdown process. However, the mechanism that processive bacterial enzymes utilize to recruit and retain cellulose strands in the catalytic site remains poorly understood. Here, integrated enzymatic assays, protein crystallography and computational approaches were combined to study the enzymatic properties of the processive BlCel48B cellulase from Bacillus licheniformis. Hydrolytic efficiency, substrate binding affinity, cleavage patterns, and the apparent processivity of bacterial BlCel48B are significantly impacted by the cellulose size and its surface morphology. BlCel48B crystallographic structure was solved with ligands spanning -5 to -2 and +1 to +2 subsites. Statistical coupling analysis and molecular dynamics show that co-evolved residues on active site are critical for stabilizing ligands in the catalytic tunnel. Our results provide mechanistic insights into BlCel48B molecular-level determinants of activity, substrate binding, and processivity on insoluble cellulose, thus shedding light on structure-activity correlations of GH48 family members in general. (AU)

FAPESP's process: 14/00769-5 - Structural studies of glycoside hydrolyses in solution using small-angle scattering (SAS) techniques
Grantee:Vasilii Piiadov
Support type: Scholarships in Brazil - Doctorate (Direct)
FAPESP's process: 15/13684-0 - Structural and functional studies of enzymes that participate in complex carbohydrates synthesis and degradation
Grantee:Igor Polikarpov
Support type: Research Projects - Thematic Grants
FAPESP's process: 13/08293-7 - CCES - Center for Computational Engineering and Sciences
Grantee:Munir Salomao Skaf
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 19/17350-0 - Molecular modeling of carbohydrate-modifying enzymes
Grantee:Artur Hermano Sampaio Dias
Support type: Scholarships in Brazil - Doctorate