| All-trans-8'-apo-beta-carotenal 15,15'-oxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.14.99.41 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
All-trans-8'-apo-beta-carotenal 15,15'-oxygenase (EC 1.14.99.41, Diox1, ACO, 8'-apo-beta-carotenal 15,15'-oxygenase) is an enzyme with systematic name all-trans-8'-apo-beta-carotenal:oxygen 15,15'-oxidoreductase (bond-cleaving).[1][2] This enzyme catalyses the following chemical reaction
- all-trans-8'-apo-beta-carotenal + O2 all-trans-retinal + (2E,4E,6E)-2,6-dimethylocta-2,4,6-trienedial
All-trans-8'-apo-beta-carotenal 15,15'-oxygenase contains an Fe2+-4His arrangement.
References
- ↑ Ruch S, Beyer P, Ernst H, Al-Babili S (February 2005). "Retinal biosynthesis in Eubacteria: in vitro characterization of a novel carotenoid oxygenase from Synechocystis sp. PCC 6803". Molecular Microbiology. 55 (4): 1015–24. doi:10.1111/j.1365-2958.2004.04460.x. PMID 15686550.
- ↑ Kloer DP, Ruch S, Al-Babili S, Beyer P, Schulz GE (April 2005). "The structure of a retinal-forming carotenoid oxygenase". Science. 308 (5719): 267–9. doi:10.1126/science.1108965. PMID 15821095.
External links
- All-trans-8'-apo-beta-carotenal+15,15'-oxygenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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