| Texto completo | |
| Autor(es): Mostrar menos - |
Teune, Michelle
;
Vieira, Plinio S.
;
Doehler, Thorben
;
Palm, Gottfried J.
;
Dutschei, Theresa
;
Bartosik, Daniel
;
Berndt, Leona
;
Persinoti, Gabriela F.
;
Maass, Sandra
;
Becher, Doerte
;
Schweder, Thomas
;
Murakami, Mario T.
;
Lammers, Michael
;
Bornscheuer, Uwe T.
Número total de Autores: 14
|
| Tipo de documento: | Artigo Científico |
| Fonte: | NATURE COMMUNICATIONS; v. 16, n. 1, p. 13-pg., 2025-07-31. |
| Resumo | |
Carbohydrate esterases modify polysaccharides by removing different ester moieties thereby affecting their physicochemical properties and their accessibility by glycoside hydrolases. We determined the full-length structures of two members (Fl8CE20_II and PpCE20_II) from the carbohydrate esterase family 20 (CE20) by X-ray crystallography that feature an ancillary domain, inserted into the catalytic SGNH-hydrolase domain. Detailed structural analysis identifies a so far undescribed catalytic triad architecture which lacks the typical aspartate for polarization of the histidine but instead reveals a precisely coordinated water molecule mediating contact between the His and Asp. This coordinated water in the Ser-His-(H2O-Asp/Asn) motif, as further confirmed by mutational studies and by determination of kinetic constants, is crucial for catalytic activity. We therefore term this active site architecture a water-mediated catalytic triad. (AU) | |
| Processo FAPESP: | 16/06509-0 - Entendimento do sistema enzimático envolvido na degradação e utilização de xiloglicanas do fitopatógeno Xanthomonas axonopodis pv. citri |
| Beneficiário: | Plínio Salmazo Vieira |
| Modalidade de apoio: | Bolsas no Brasil - Pós-Doutorado |
| Processo FAPESP: | 21/04891-3 - Mecanismos enzimáticos do microbioma de herbívoros aquáticos para a despolimerização e metabolismo de carboidratos complexos |
| Beneficiário: | Mário Tyago Murakami |
| Modalidade de apoio: | Auxílio à Pesquisa - Temático |