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Regulación alostérica dependiente del sustrato en el citocromo P450cam (CYP101A1)

Alec H Follmer¹, Mavish Mahomed², David B Goodin²

¹Departments of Molecular Biology and Biochemistry, Pharmaceutical Sciences, and Chemistry , University of California , Irvine , California 92697-3900 , United States.

Journal of the American Chemical Society

|October 31, 2018

Resumen

El citocromo P450cam tiene un segundo sitio de sustrato. La unión de una segunda molécula de sustrato a este sitio alostérico abre canales para la entrada del sustrato y la salida del producto, revelando la cooperatividad.

Área de la Ciencia:

La bioquímica
Biología molecular
Enzimología

Sus antecedentes:

El citocromo P450cam es una enzima bien estudiada.
La evidencia sugiere un segundo sitio de unión al sustrato, pero su papel no está claro.
La comprensión del transporte de sustrato/producto a través de los canales activos del sitio es crucial.

Objetivo del estudio:

Investigar la localización y la relevancia biológica de un segundo sitio de unión al sustrato en el citocromo P450cam.
Elucidar los mecanismos de unión del sustrato y la salida del producto.
Explorar el potencial de cooperación entre los diferentes sitios de enlace.

Principales métodos:

Se emplearon simulaciones de dinámica molecular.
Análisis de las vías de unión y de salida del sustrato y del producto.
Investigación de la dinámica del canal y de las interacciones en el sitio alostérico.

Principales resultados:

Se identificó un sitio alostérico remoto que influye en la unión al sustrato y la salida del producto.
La unión de una segunda molécula de sustrato al sitio alostérico abre el canal 1.
Se prepara un nuevo canal de salida (canal 2) que facilita la entrada en el sustrato y la salida del producto.
Se demostró la cooperación entre el sitio activo y el sitio alostérico.

Conclusiones:

El estudio revela una interacción dinámica entre un sitio alostérico y el sitio activo del citocromo P450cam.
Esta interacción controla la actividad enzimática mediante la regulación del acceso al sustrato y la liberación del producto.
Los hallazgos concilian las observaciones experimentales anteriores con respecto a la función de la cámara P450.

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