Trichoderma reesei cellobiohydrolase Cel6A is an inverting glycosidase. Structural studies have established that the tunnel-shaped active site of Cel6A contains two aspartic acids, D221 and D175, that are close to the glycosidic oxygen of the scissile bond and at hydrogen-bonding distance from each other. Here, site-directed mutagenesis, X-ray crystallography, and enzyme kinetic studies have been used to confirm the role of residue D221 as the catalytic acid. D175 is shown to affect protonation of D221 and to contribute to the electrostatic stabilization of the partial positive charge in the transition state. Structural and modeling studies suggest that the single-displacement mechanism of Cel6A may not directly involve a catalytic base. Th...
Aiming to contribute toward the characterization of new, biotechnologically relevant cellulolytic en...
AbstractCellobiohydrolase I from Trichoderma reesei catalyzes the hydrolysis of methyl β-D-cellotrio...
Aiming to contribute toward the characterization of new, biotechnologically relevant cellulolytic en...
Trichoderma reesei cellobiohydrolase Cel6A is an inverting glycosidase. Structural studies have est...
Trichoderma reesei cellobiohydrolase II (CBHII) is an exoglucanase cleaving primarily cellobiose uni...
Trichoderma reesei cellobiohydrolase II (CBHII) is an exoglucanase cleaving primarily cellobiose uni...
Background: Cel6A is one of the two cellobiohydrolases produced by Trichoderma reesei. The catalytic...
Background: Cel6A is one of the two cellobiohydrolases produced by Trichoderma reesei. The catalytic...
Trichoderma reesei cellobiohydrolase II (CBH11) is an exoglucanase cleaving primarily cellobiose uni...
AbstractBackground: Cel6A is one of the two cellobiohydrolases produced by Trichoderma reesei. The c...
The crystal structures of Family 7 glycohydrolases suggest that a histidine residue near the acid/ba...
The crystal structures of Family 7 glycohydrolases suggest that a histidine residue near the acid/ba...
The crystal structures of Family 7 glycohydrolases suggest that a histidine residue near the acid/ba...
The roles of the residues in the catalytic trio Glu212-Asp214-Glu217 in cellobiohydrolase I (CBHI) f...
The roles of the residues in the catalytic trio Glu212-Asp214-Glu217 in cellobiohydrolase I (CBHI) f...
Aiming to contribute toward the characterization of new, biotechnologically relevant cellulolytic en...
AbstractCellobiohydrolase I from Trichoderma reesei catalyzes the hydrolysis of methyl β-D-cellotrio...
Aiming to contribute toward the characterization of new, biotechnologically relevant cellulolytic en...
Trichoderma reesei cellobiohydrolase Cel6A is an inverting glycosidase. Structural studies have est...
Trichoderma reesei cellobiohydrolase II (CBHII) is an exoglucanase cleaving primarily cellobiose uni...
Trichoderma reesei cellobiohydrolase II (CBHII) is an exoglucanase cleaving primarily cellobiose uni...
Background: Cel6A is one of the two cellobiohydrolases produced by Trichoderma reesei. The catalytic...
Background: Cel6A is one of the two cellobiohydrolases produced by Trichoderma reesei. The catalytic...
Trichoderma reesei cellobiohydrolase II (CBH11) is an exoglucanase cleaving primarily cellobiose uni...
AbstractBackground: Cel6A is one of the two cellobiohydrolases produced by Trichoderma reesei. The c...
The crystal structures of Family 7 glycohydrolases suggest that a histidine residue near the acid/ba...
The crystal structures of Family 7 glycohydrolases suggest that a histidine residue near the acid/ba...
The crystal structures of Family 7 glycohydrolases suggest that a histidine residue near the acid/ba...
The roles of the residues in the catalytic trio Glu212-Asp214-Glu217 in cellobiohydrolase I (CBHI) f...
The roles of the residues in the catalytic trio Glu212-Asp214-Glu217 in cellobiohydrolase I (CBHI) f...
Aiming to contribute toward the characterization of new, biotechnologically relevant cellulolytic en...
AbstractCellobiohydrolase I from Trichoderma reesei catalyzes the hydrolysis of methyl β-D-cellotrio...
Aiming to contribute toward the characterization of new, biotechnologically relevant cellulolytic en...