Por favor, use este identificador para citar o enlazar este ítem:
http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2849| Título : | Susceptibility to proteolysis of triosephosphate isomerase from two pathogenic parasites: Characterization of an enzyme with an intact and a nicked monomer |
| Creador: | Reyes Vivas, Horacio |
| Nivel de acceso: | Open access |
| Palabras clave : | Triosa-fosfato isomerasa - metabolismo Trypanosoma brucei brucei - enzimología Trypanosoma cruzi - enzimología Trypanosoma cruzi - patogenicidad Triose-Phosphate Isomerase - metabolism Trypanosoma brucei brucei - enzymology Trypanosoma cruzi - enzymology especifidad flexibilidad estructural inactivación por hidrólisis limitada estabilidad estructural de proteínas subtilisin structuralflexibility asym-metricaldimers inactivation by limited hydrolysis protein structural stability |
| Descripción : | The susceptibility to subtilisin of homodimeric triosephosphate isomerase from Trypanosoma brucei (TbTIM) and Trypanosoma cruzi (TcTIM) was studied. Their amino sequence and 3D structure are markedly similar. In 36 h of incubation at a molar ratio of 4 TIM per subtilisin, TcTIM underwent extensive hydrolysis, loss of activity, and large structural alterations. Under the same conditions, only about 50% of the monomers of TbTIM were cleaved in two sites. The higher sensitivity of TcTIM to subtilisin is probably due to a higher intrinsic flexibility. We isolated and characterized TbTIM that had been exposed to subtilisin. It exhibited the molecular mass of the dimer, albeit it was formed by one intact and one nicked monomer. Its kcat with glyceraldehyde 3-phosphate was half that of native TbTIM, with no change in Km. The intrinsic fluorescence of nicked TbTIM was red-shifted by 5 nm. The association between subunits was not affected. The TbTIM data suggest that there are structural differences in the two monomers or that alterations of one subunit change the characteristics of the other subunit. In comparison to the action of subtilisin on TIMs from other species, the trypanosomal enzymes appear to be unique. © 2002 Wiley-Liss, Inc. |
| Colaborador(es) u otros Autores: | Martínez Martínez E Mendoza Hernández G López Velázquez G Pérez Montfort R Tuena de Gómez-Puyou M Gómez-Puyou A. |
| Fecha de publicación : | 2002 |
| Tipo de publicación: | Artículo |
| Formato: | |
| Identificador del Recurso : | 10.1002/prot.10179 |
| Fuente: | Proteins: Structure, Function and Genetics 48(3):580 - 590 |
| URI : | http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2849 |
| Idioma: | eng |
| Aparece en las colecciones: | Artículos |
Ficheros en este ítem:
No hay ficheros asociados a este ítem.
Los ítems de DSpace están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.