| Texto completo | |
| Autor(es): |
Tamaki, Fabio K.
;
Souza, Diorge P.
;
Souza, Valquiria P.
;
Ikegami, Cecilia M.
;
Farah, Chuck S.
;
Marana, Sandro R.
Número total de Autores: 6
|
| Tipo de documento: | Artigo Científico |
| Fonte: | PLoS One; v. 11, n. 12 DEC 9 2016. |
| Citações Web of Science: | 1 |
| Resumo | |
The active site residues in GH1 beta-glycosidases are compartmentalized into 3 functional regions, involved in catalysis or binding of glycone and aglycone motifs from substrate. However, it still remains unclear how residues outside the active site modulate the enzymatic activity. To tackle this question, we solved the crystal structure of the GH1 beta-glycosidase from Spodoptera frugiperda (Sf beta gly) to systematically map its residue contact network and correlate effects of mutations within and outside the active site. External mutations neighbouring the functional residues involved in catalysis and glycone-binding are deleterious, whereas mutations neighbouring the aglycone-binding site are less detrimental or even beneficial. The large dataset of new and previously characterized Sfpgly mutants supports that external perturbations are coherently transmitted to active site residues possibly through contacts and specifically disturb functional regions they interact to, reproducing the effects observed for direct mutations of functional residues. This allowed us to suggest that positions related to the aglycone-binding site are preferential targets for introduction of mutations aiming to further improve the hydrolytic activity of beta-glycosidases. (AU) | |
| Processo FAPESP: | 08/55914-9 - (bioen/pronex FAPESP) Development of beta-glycosidases designed to improve the efficiency of noncomplexed cellulase systems |
| Beneficiário: | Sandro Roberto Marana |
| Modalidade de apoio: | Auxílio à Pesquisa - Programa BIOEN - Temático |
| Processo FAPESP: | 14/19439-5 - Redes estruturais e propriedades funcionais em enzimas |
| Beneficiário: | Sandro Roberto Marana |
| Modalidade de apoio: | Auxílio à Pesquisa - Regular |