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Remodelación del sitio activo en el bifuncional fructosa-1,6-bisfosfato aldolasa/fosfatasa
Juan Du1, Rafael F Say, Wei Lü
1Lehrstuhl für Biochemie, Institut für organische Chemie und Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg, Germany.
Nature
|October 11, 2011
Resumen
Este estudio revela cómo la enzima bifuncional fructosa-1,6-bisfosfato (FBP) aldolasa/fosfatasa remodela su sitio activo para catalizar dos reacciones claves de la gluconeogénesis. Las instantáneas estructurales muestran movimientos secuenciales de unión y bucle de Mg2+ que permiten esta enzima ancestral.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología Estructural Biología estructural.
- Enzimología Enzimología.
Sus antecedentes:
- La fructosa-1,6-bisfosfato (FBP) aldolasa/fosfatasa es una enzima bifuncional crucial en la gluconeogénesis.
- Cataliza la condensación de aldol y las reacciones de hidrólisis, esenciales en las arqueas y algunas bacterias.
Objetivo del estudio:
- Para aclarar los mecanismos estructurales detrás de las funciones catalíticas duales de FBP aldolasa/fosfatasa.
- Para entender cómo funciona esta enzima ancestral a altas temperaturas.
Principales métodos:
- Se utilizó la cristalografía de rayos X para determinar las estructuras de la aldolasa/fosfatasa FBP de *Thermoproteus neutrophilus*.
- Las estructuras se resolvieron en estados libres de ligandos y se complexionaron con sustratos (DHAP, GAP) y producto (F6P).
- Los estudios de mutagenesis identificaron residuos clave para la actividad catalítica.
Principales resultados:
- Las instantáneas estructurales revelaron una remodelación significativa del sitio activo a través de movimientos de bucle, creando distintas funcionalidades catalíticas.
- Se demostró que la unión secuencial de cationes Mg2+ facilita ambos pasos de reacción.
- Se confirmó la naturaleza ancestral de la enzima y su optimización para altas temperaturas.
Conclusiones:
- El estudio resuelve la bifuncionalidad no canónica de FBP aldolasa/fosfatasa a través de reordenamientos estructurales dinámicos.
- Este trabajo proporciona información sobre la evolución de las vías metabólicas y la catálisis enzimática en organismos termófilos.
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