Molecular mechanism of cellulose depolymerization by the two-domain BlCel9A enzyme from the glycoside hydrolase family 9
Carbohydrate-active enzymes from the glycoside hydrolase family 9 (GH9) play a key role in
processing lignocellulosic biomass. Although the structural features of some GH9 enzymes
are known, the molecular mechanisms that drive their interactions with cellulosic substrates
remain unclear. To investigate the molecular mechanisms that the two-domain Bacillus
licheniformis Bl Cel9A enzyme utilizes to depolymerize cellulosic substrates, we used a
combination of biochemical assays, X-ray crystallography, small-angle X-ray scattering, and …
processing lignocellulosic biomass. Although the structural features of some GH9 enzymes
are known, the molecular mechanisms that drive their interactions with cellulosic substrates
remain unclear. To investigate the molecular mechanisms that the two-domain Bacillus
licheniformis Bl Cel9A enzyme utilizes to depolymerize cellulosic substrates, we used a
combination of biochemical assays, X-ray crystallography, small-angle X-ray scattering, and …
[引用][C] Molecular mechanism of cellulose depolymerization by the two-domain BlCel9A enzyme from the glycoside hydrolase family
CCM Capetti, VOA Pellegrini, MCE Santo… - Carbohydrate …, 2024 - repositorio.usp.br
USP affiliated authors: CURVELO, ANTONIO APRIGIO DA SILVA-IQSC; GUIMARÃES,
FRANCISCO EDUARDO GONTIJO-IFSC; AZEVÊDO, EDUARDO RIBEIRO DE-IFSC;
POLIKARPOV, IGOR-IFSC; CAPETTI, CAIO CESAR DE MELLO-IFSC; PELLEGRINI,
VANESSA DE OLIVEIRA ARNOLDI-IFSC; SANTO, MELISSA CRISTINA DO ESPIRITO-IFSC;
CORTEZ, ANELYSE ABREU-IFSC; FALVO, MAURÍCIO-IFSC
FRANCISCO EDUARDO GONTIJO-IFSC; AZEVÊDO, EDUARDO RIBEIRO DE-IFSC;
POLIKARPOV, IGOR-IFSC; CAPETTI, CAIO CESAR DE MELLO-IFSC; PELLEGRINI,
VANESSA DE OLIVEIRA ARNOLDI-IFSC; SANTO, MELISSA CRISTINA DO ESPIRITO-IFSC;
CORTEZ, ANELYSE ABREU-IFSC; FALVO, MAURÍCIO-IFSC
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