EC number:1.3.99.27

Enzyme

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     1. Oxidoreductases
        1.3 Acting on the CH-CH group of donors
            1.3.99 With unknown physiological acceptors
ID:1.3.99.27
Description:1-hydroxycarotenoid 3,4-desaturase.
Alternative Name: Hydroxyneurosporene desaturase.
Carotenoid 3,4-dehydrogenase.
1-hydroxycarotenoid 3,4-dehydrogenase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.3.99.27
BRENDA Enzyme Link: BRENDA 1.3.99.27
KEGG Enzyme Link: KEGG1.3.99.27
BioCyc Enzyme Link: BioCyc 1.3.99.27
ExPASy Enzyme Link: ExPASy1.3.99.27
EC2PDB Enzyme Link: EC2PDB 1.3.99.27
ExplorEnz Enzyme Link: ExplorEnz 1.3.99.27
PRIAM enzyme-specific profiles Link: PRIAM 1.3.99.27
IntEnz Enzyme Link: IntEnz 1.3.99.27
MEDLINE Enzyme Link: MEDLINE 1.3.99.27

EC number:1.3.99.27

MSA:

1.3.99.27;
Phylogenetic Tree:

1.3.99.27;
Uniprot:
M-CSA:
RHEA:30919 A + rhodopin = (3E)-3,4-didehydrorhodopin + AH2
RULE(radius=1) [*:1]-[CH2;+0:2]-[CH2;+0:3]-[*:4]>>[*:1]-[CH;+0:2]=[CH;+0:3]-[*:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Purification and biochemical characterization of a hydroxyneurosporene desaturase involved in the biosynthetic pathway of the carotenoid spheroidene in Rhodobacter sphaeroides.Albrecht M, Ruther A, Sandmann G1997 Dec9393712
1-Hydroxy monocyclic carotenoid 3,4-dehydrogenase from a marine bacterium that produces myxol.Teramoto M, Rählert N, Misawa N, Sandmann G2004 Jul 1615251462
Substrate specificity of the expressed carotenoid 3,4-desaturase from Rubrivivax gelatinosus reveals the detailed reaction sequence to spheroidene and spirilloxanthin.Steiger S, Astier C, Sandmann G2000 Jul 1510880364