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The oxygenase CAO-1 of Neurospora crassa is a resveratrol cleavage enzyme.

Opened Access The oxygenase CAO-1 of Neurospora crassa is a resveratrol cleavage enzyme.


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Autor: Avalos Cordero, Francisco Javier
Díaz Sánchez, Violeta
Estrada Alejandro, F
Limón Mirón, María del Carmen
Al-Babili, Salim
Departamento: Universidad de Sevilla. Departamento de Genética
Fecha: 2013
Publicado en: Eukaryotic Cell, 12 (9), 1305-1314
Tipo de documento: Artículo
Resumen: The genome of the ascomycete Neurospora crassa encodes CAO-1 and CAO-2, two members of the carotenoid cleavage oxygenase family that target double bonds in different substrates. Previous studies demonstrated the role of CAO-2 in cleaving the C40 carotene torulene, a key step in the synthesis of the C35 apocarotenoid pigment neurosporaxanthin. In this work, we investigated the activity of CAO-1, assuming that it may provide retinal, the chromophore of the NOP-1 rhodopsin, by cleaving β-carotene. For this purpose, we tested CAO-1 activity with carotenoid substrates that were, however, not converted. In contrast and consistent with its sequence similarity to family members that act on stilbenes, CAO-1 cleaved the interphenyl Cα-Cβ double bond of resveratrol and its derivative piceatannol. CAO-1 did not convert five other similar stilbenes, indicating a requirement for a minimal number of unmodified hydroxyl groups in the stilbene background. Confirming its biological function in converti...
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