1-Hydroxycarotenoid 3,4-desaturase
1-hydroxycarotenoid 3,4-desaturase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 1.3.99.27 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
|
1-Hydroxycarotenoid 3,4-desaturase (EC 1.3.99.27, CrtD, hydroxyneurosporene desaturase, carotenoid 3,4-dehydrogenase, 1-hydroxy-carotenoid 3,4-dehydrogenase) is an enzyme with systematic name 1-hydroxy-1,2-dihydrolycopene:acceptor oxidoreductase.[1][2][3] This enzyme catalyses the following chemical reaction
- 1-hydroxy-1,2-dihydrolycopene + acceptor 1-hydroxy-3,4-didehydro-1,2-dihydrolycopene + reduced acceptor
The enzymes from Rubrivivax gelatinosus and Rhodobacter sphaeroides acts primarily on acyclic carotenoids.
References
- ↑ Teramoto, M.; Rahlert, N.; Misawa, N.; Sandmann, G. (2004). "1-Hydroxy monocyclic carotenoid 3,4-dehydrogenase from a marine bacterium that produces myxol". FEBS Lett. 570 (1-3): 184–188. doi:10.1016/j.febslet.2004.05.085. PMID 15251462.
- ↑ Steiger, S.; Astier, C.; Sandmann, G. (2000). "Substrate specificity of the expressed carotenoid 3,4-desaturase from Rubrivivax gelatinosus reveals the detailed reaction sequence to spheroidene and spirilloxanthin". Biochem. J. 349 (Pt 2): 635–640. doi:10.1042/0264-6021:3490635. PMC 1221188. PMID 10880364.
- ↑ Albrecht, M.; Ruther, A.; Sandmann, G. (1997). "Purification and biochemical characterization of a hydroxyneurosporene desaturase involved in the biosynthetic pathway of the carotenoid spheroidene in Rhodobacter sphaeroides". J. Bacteriol. 179 (23): 7462–7467. PMC 179698. PMID 9393712.
External links
- 1-hydroxycarotenoid 3,4-desaturase at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia - version of the 5/16/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.