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http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2628| Título : | Mutations of glucose-6-phosphate dehydrogenase durham, Santa-Maria and A+ variants are associated with loss functional and structural stability of the protein |
| Creador: | Gómez Manzo, Saúl |
| Nivel de acceso: | Open access |
| Palabras clave : | Catálisis Activación Enzimática Expresión Génica Variación Genética Glucosafosfato Deshidrogenasa - química Glucosafosfato Deshidrogenasa - genética Glucosafosfato Deshidrogenasa - metabolismo Humanos Cinética Modelos Moleculares Conformación Molecular Mutación Estabilidad Proteica Proteínas Recombinantes Relación Estructura-Actividad Termodinámica Catalysis Enzyme Activation Gene Expression Genetic Variation Glucosephosphate Dehydrogenase - chemistry Glucosephosphate Dehydrogenase - genetics Glucosephosphate Dehydrogenase - metabolism Humans Kinetics Models, Molecular Molecular Conformation Mutation Protein Stability Recombinant Proteins Structure-Activity Relationship Thermodynamics Deficiencia de G6PD G6PD-variantes Propiedades cinéticas Expresión recombinante estabilidad G6PD deficiency G6PD-variants kinetic-properties recombinant expression stability |
| Descripción : | Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the most common enzymopathy in the world. More than 160 mutations causing the disease have been identified, but only 10% of these variants have been studied at biochemical and biophysical levels. In this study we report on the functional and structural characterization of three naturally occurring variants corresponding to different classes of disease severity: Class I G6PD Durham, Class II G6PD Santa Maria, and Class III G6PD A+. The results showed that the G6PD Durham (severe deficiency), and the G6PD Santa Maria and A+ (less severe deficiency) (Class I, II and III, respectively) affect the catalytic efficiency of these enzymes, are more sensitive to temperature denaturing, and affect the stability of the overall protein when compared to the wild type WT-G6PD. In the variants, the exposure of more and buried hydrophobic pockets was induced and monitored with 8-Anilinonaphthalene-1-sulfonic acid (ANS) fluorescence, directly affecting the compaction of structure at different levels and probably reducing the stability of the protein. The degree of functional and structural perturbation by each variant correlates with the clinical severity reported in different patients. © 2015 by the authors; licensee MDPI, Basel, Switzerland. |
| Colaborador(es) u otros Autores: | Marcial-Quino Jaime Vanoye-Carlo America Enríquez-Flores Sergio De La Mora-De La Mora Ignacio González-Valdez Abigail García-Torres Itzhel Martínez-Rosas Víctor Sierra-Palacios Edgar Lazcano-Pérez Fernando Rodríguez-Bustamante Eduardo Arreguin-Espinosa Roberto |
| Fecha de publicación : | 2015 |
| Tipo de publicación: | Artículo |
| Formato: | |
| Identificador del Recurso : | 10.3390/ijms161226124 |
| Fuente: | International Journal of Molecular Sciences 16(12):28657 - 28668 |
| URI : | http://repositorio.pediatria.gob.mx:8180/handle/20.500.12103/2628 |
| Idioma: | eng |
| Aparece en las colecciones: | Artículos |
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