1.3.99.27: 1-hydroxycarotenoid 3,4-desaturase

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For detailed information about 1-hydroxycarotenoid 3,4-desaturase, go to the full flat file.

Reaction

Synonyms

1-HO carotenoid 3,4-dehydrogenase, 1-hydroxy monocyclic carotenoid 3,4-dehydrogenase, acyclic carotenoid 3,4-desaturase, CrtD, DDD_2394, hydroxyneurosporene desaturase, P99-3 CrtD

ECTree

     1 Oxidoreductases

         1.3 Acting on the CH-CH group of donors

             1.3.99 With unknown physiological acceptors

                1.3.99.27 1-hydroxycarotenoid 3,4-desaturase

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Results	in table
102	AA Sequence
1	Application
4	Cloned(Commentary)
2	Cofactor
1	Crystallization (Commentary)
13	General Information
4	KM Value [mM]
2	Molecular Weight [Da]
9	Natural Substrates/ Products (Substrates)
15	Organism
5	Pathway
2	pH Optimum
1	Purification (Commentary)
1	Reaction
14	Reference
25	Substrates and Products (Substrate)
2	Subunits
26	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]

Cofactor

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Cofactor on EC 1.3.99.27 - 1-hydroxycarotenoid 3,4-desaturase

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

FAD

Nonlabens dokdonensis

L7WC64

the FAD-binding site is located at the G-x-G-x-x-G nucleotide-binding motif, comprising residues Gly8-Ala9-Gly10-Ile11-Gly12-Gly13

742415

additional information

Cereibacter sphaeroides

-

NAD+, NADP+, and flavin adenine dinucleotide have no influence on enzymatic activity. When O2 is depleted less than 10% of the specific activity is retained. It is rather unlikely that molecular oxygen is the genuine cofactor for hydroxyneurosporene desaturation reactions in Rhodobacter cells when they reach their maximum carotenoid content under anaerobic conditions. Consequently, another, as-yet-unknown electron acceptor may exist in Rhodobacter species that replaces molecular oxygen during anaerobic growth

712271

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