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ENZYME entry: EC 1.3.99.27
Accepted Name |
1-hydroxycarotenoid 3,4-desaturase.
|
Alternative Name(s) |
1-hydroxycarotenoid 3,4-dehydrogenase. |
carotenoid 3,4-dehydrogenase. |
hydroxyneurosporene desaturase. |
Reaction catalysed |
A + rhodopin <=> (3E)-3,4-didehydrorhodopin + AH2 |
Comment(s) |
- 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-gamma-carotene is lower.
- The enzyme from the marine bacterium strain P99-3 shows high activity
with the monocyclic carotenoid 1'-hydroxy-1',2'-dihydro-gamma-
carotene.
- The enzyme from Rhodobacter sphaeroides utilizes molecular oxygen as
the electron acceptor in vitro.
- However, oxygen is unlikely to be the natural electron acceptor under
anaerobic conditions.
|
Cross-references |
BRENDA | 1.3.99.27 |
EC2PDB | 1.3.99.27 |
ExplorEnz | 1.3.99.27 |
PRIAM enzyme-specific profiles | 1.3.99.27 |
KEGG Ligand Database for Enzyme Nomenclature | 1.3.99.27 |
IUBMB Enzyme Nomenclature | 1.3.99.27 |
IntEnz | 1.3.99.27 |
MEDLINE | Find literature relating to 1.3.99.27 |
MetaCyc | 1.3.99.27 |
Rhea expert-curated reactions | 1.3.99.27 |
UniProtKB/Swiss-Prot |
|
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