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: pdf
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
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