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Literature summary for 2.5.1.150 extracted from

  • Yang, Y.; Yatsunami, R.; Ando, A.; Miyoko, N.; Fukui, T.; Takaichi, S.; Nakamura, S.
    Complete biosynthetic pathway of the C50 carotenoid bacterioruberin from lycopene in the extremely halophilic archaeon Haloarcula japonica (2015), J. Bacteriol., 197, 1614-1623 .
    View publication on PubMedView publication on EuropePMC
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethylallyl diphosphate + all-trans-lycopene + H2O Haloarcula japonica the enzyme is involved in the biosynthetic pathway of the C50 carotenoid bacterioruberin. The enzyme is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate dihydroisopentenyldehydrorhodopin + diphosphate
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 ?
dimethylallyl diphosphate + isopentenyldehydrorhodopin + H2O Haloarcula japonica the enzyme is involved in the biosynthetic pathway of the C50 carotenoid bacterioruberin. The enzyme is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate dihydrobisanhydrobacterioruberin + diphosphate
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 ?

Organism

Organism UniProt Comment Textmining
Haloarcula japonica A0A0A1GNW8
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylallyl diphosphate + all-trans-lycopene + H2O the enzyme is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate Haloarcula japonica dihydroisopentenyldehydrorhodopin + diphosphate
-
 ?
dimethylallyl diphosphate + all-trans-lycopene + H2O the enzyme is involved in the biosynthetic pathway of the C50 carotenoid bacterioruberin. The enzyme is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate Haloarcula japonica dihydroisopentenyldehydrorhodopin + diphosphate
-
 ?
dimethylallyl diphosphate + isopentenyldehydrorhodopin + H2O the enzyme is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate Haloarcula japonica dihydrobisanhydrobacterioruberin + diphosphate
-
 ?
dimethylallyl diphosphate + isopentenyldehydrorhodopin + H2O the enzyme is involved in the biosynthetic pathway of the C50 carotenoid bacterioruberin. The enzyme is bifunctional. It catalyses the elongation of the C40 carotenoid all-trans-lycopene by attaching an isoprene unit at C-2 as well as the hydroxylation of the previous end of the molecule. The enzyme acts at both ends of the substrate Haloarcula japonica dihydrobisanhydrobacterioruberin + diphosphate
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 ?

Synonyms

Synonyms Comment Organism
c0506
-
 Haloarcula japonica
lycopene elongase/1,2-hydratase bifunctional enzyme Haloarcula japonica
lyeJ
-
 Haloarcula japonica

General Information

General Information Comment Organism
metabolism the enzyme is involved in the biosynthetic pathway of the C50 carotenoid bacterioruberin Haloarcula japonica