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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: pdf
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
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