Structural highlights
Function
CAO1_NEUCR Dioxygenase that cleaves the interphenyl C-alpha-C-beta double bond of resveratrol to yield 3,5-dihydroxybenzaldehyde and 4-hydroxybenzaldehyde (PubMed:23893079, PubMed:28493664). Cleaves also piceatannol, a compound that differs from resveratrol only in the occurrence of an additional hydroxyl group, which leads to the production of 3,4-dihydroxybenzaldehyde and 3,5-hydroxybenzaldehyde (PubMed:23893079 PubMed:28493664). Is not able to cleave trans-stilbene, 4-monohydroxy-trans-stilbene, 3,5-dihydroxy-trans-stilbene (pinosylvin), trismethoxy-resveratrol, and 3,3',5-trihydroxy-4'-methoxystilbene-3-O-beta-D-glucoside (PubMed:23893079). Is not involved in carotenoid metabolism (PubMed:23893079).[1] [2]
References
- ↑ Díaz-Sánchez V, Estrada AF, Limón MC, Al-Babili S, Avalos J. The oxygenase CAO-1 of Neurospora crassa is a resveratrol cleavage enzyme. Eukaryot Cell. 2013 Sep;12(9):1305-14. PMID:23893079 doi:10.1128/EC.00084-13
- ↑ Sui X, Weitz AC, Farquhar ER, Badiee M, Banerjee S, von Lintig J, Tochtrop GP, Palczewski K, Hendrich MP, Kiser PD. Structure and Spectroscopy of Alkene-Cleaving Dioxygenases Containing an Atypically Coordinated Non-Heme Iron Center. Biochemistry. 2017 Jun 6;56(22):2836-2852. doi: 10.1021/acs.biochem.7b00251. Epub, 2017 May 19. PMID:28493664 doi:http://dx.doi.org/10.1021/acs.biochem.7b00251