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Una proteína de diirón autogenera un enlace cruzado valina-fenilalanina

Richard B Cooley¹, Timothy W Rhoads, Daniel J Arp

¹Department of Biochemistry and Biophysics, 2011 Agriculture and Life Sciences Building, Oregon State University, Corvallis, OR 97331, USA.

Science (New York, N.Y.)

|May 21, 2011

Resumen

Los investigadores descubrieron un nuevo enlace cruzado carbono-carbono entre cadenas laterales de proteínas no funcionalizadas. Este vínculo único valina-fenilalanina, estabilizado por un centro de diirón, revela nuevas posibilidades de modificación posttraducional.

Área de la Ciencia:

La bioquímica es la bioquímica.
Química de las proteínas química de las proteínas.
Enzimología Enzimología.

Sus antecedentes:

Los enlaces cruzados covalentes internos en las proteínas generalmente requieren grupos funcionalizados.
Los átomos de oxígeno, nitrógeno o azufre suelen estar involucrados en facilitar la formación de enlaces cruzados.

Objetivo del estudio:

Para informar sobre el descubrimiento de un nuevo tipo de enlace cruzado de proteínas.
Para caracterizar un enlace cruzado carbono-carbono entre cadenas laterales de aminoácidos no funcionalizados.

Principales métodos:

Mecanismos de enlace cruzado de proteínas investigados.
Se analizó la formación de un enlace cruzado valina-fenilalanina.
Estudió el papel de un centro de diirón con puente de carboxilato en la reacción.

Principales resultados:

Se identificó un enlace directo carbono-carbono entre las cadenas laterales de valina y fenilalanina.
Se demostró que la formación de enlaces cruzados es dependiente del oxígeno.
Se demostró que el centro de diirón cataliza y estabiliza este enlace cruzado único.

Conclusiones:

Este hallazgo representa una nueva clase de modificaciones posttraduccionales.
Los centros de diirón exhiben un nuevo potencial catalítico más allá de las funciones conocidas.
El descubrimiento desafía los paradigmas existentes de enlace cruzado de proteínas.

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