| EC |
1.3.99.27 |
| Accepted name: |
1-hydroxycarotenoid 3,4-desaturase |
| Reaction: |
1-hydroxy-1,2-dihydrolycopene + acceptor = 1-hydroxy-3,4-didehydro-1,2-dihydrolycopene + reduced acceptor |
| Other name(s): |
CrtD; hydroxyneurosporene desaturase; carotenoid 3,4-dehydrogenase; 1-hydroxy-carotenoid 3,4-dehydrogenase |
| Systematic name: |
1-hydroxy-1,2-dihydrolycopene:acceptor oxidoreductase |
| Comments: |
The enzymes from Rubrivivax gelatinosus and Rhodobacter sphaeroides prefer the acyclic carotenoids (e.g. 1-hydroxy-1,2-dihydroneurosporene, 1-hydroxy-1,2-dihydrolycopene) as substrates. The conversion rate for the 3,4-desaturation of the monocyclic 1′-hydroxy-1′,2′-dihydro-γ-carotene is lower [2,3]. The enzyme from the marine bacterium strain P99-3 shows high activity with the monocyclic carotenoid 1′-hydroxy-1′,2′-dihydro-γ-carotene [1]. The enzyme from Rhodobacter sphaeroides utilizes molecular oxygen as the electron acceptor in vitro [3]. However, oxygen is unlikely to be the natural electron acceptor under anaerobic conditions. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Teramoto, M., Rahlert, N., Misawa, N. and Sandmann, G. 1-Hydroxy monocyclic carotenoid 3,4-dehydrogenase from a marine bacterium that produces myxol. FEBS Lett. 570 (2004) 184–188. [DOI] [PMID: 15251462] |
| 2. |
Steiger, S., Astier, C. and Sandmann, G. Substrate specificity of the expressed carotenoid 3,4-desaturase from Rubrivivax gelatinosus reveals the detailed reaction sequence to spheroidene and spirilloxanthin. Biochem. J. 349 (2000) 635–640. [PMID: 10880364] |
| 3. |
Albrecht, M., Ruther, A. and Sandmann, G. Purification and biochemical characterization of a hydroxyneurosporene desaturase involved in the biosynthetic pathway of the carotenoid spheroidene in Rhodobacter sphaeroides. J. Bacteriol. 179 (1997) 7462–7467. [DOI] [PMID: 9393712] |
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| [EC 1.3.99.27 created 2011] |
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