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Bases estructurales y computacionales para el reordenamiento esquelético dramático en la biosíntesis de Anditomin

Yu Nakashima¹, Takaaki Mitsuhashi¹, Yudai Matsuda^1,2

¹Graduate School of Pharmaceutical Sciences , The University of Tokyo , 7-3-1 Hongo , Bunkyo-ku , Tokyo 113-0033 , Japan.

Journal of the American Chemical Society

|July 5, 2018

Resumen

AndA, una enzima dependiente del hierro (II) /α-cetoglutarato, construye complejas estructuras de anillo puente. La cristalografía de rayos X y los estudios computacionales revelan residuos clave y cambios conformacionales que permiten esta transformación química única.

Área de la Ciencia:

Enzimología
Biología estructural
Química orgánica

Sus antecedentes:

AndA es crucial para sintetizar anditomin, una molécula con un complejo sistema de anillos puenteados.
La caracterización anterior de AndA dejó su mecanismo catalítico para la reconstrucción estructural drástica poco claro.

Objetivo del estudio:

Para aclarar el mecanismo por el cual AndA cataliza la formación del sistema de anillo puente en anditomin.
Identificar los residuos de aminoácidos clave y los cambios conformacionales involucrados en la actividad catalítica de AndA.

Principales métodos:

Se utilizó la cristalografía de rayos X para determinar las estructuras de AndA en su forma apo y compleja con Fe ((II), αKG y sustratos.
Se realizaron experimentos de mutagénesis dirigidos al sitio para evaluar el papel de los residuos de aminoácidos identificados.
Se emplearon cálculos computacionales para validar el mecanismo de reacción propuesto.

Principales resultados:

Tres estructuras cristalinas revelaron la conformación de la enzima en presencia de cofactores y sustratos.
Se identificaron residuos de aminoácidos clave esenciales para la catálisis a través de análisis estructurales y mutacionales.
Los estudios computacionales confirmaron la vía de reacción y destacaron la necesidad de cambios conformacionales.

Conclusiones:

El estudio proporciona información estructural y mecanicista detallada sobre la función de AndA.
Los residuos identificados y la dinámica conformacional son críticos para la actividad catalítica única de la enzima.
Este trabajo avanza en la comprensión de la biosíntesis de productos naturales complejos.

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