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Information on EC 2.5.1.150 - lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming) and Organism(s) Haloarcula japonica and UniProt Accession M0L7V9

for references in articles please use BRENDA:EC2.5.1.150
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IUBMB Comments
The enzyme, characterized from the bacterium Dietzia sp. CQ4 and the halophilic archaea Halobacterium salinarum and Haloarcula japonica, 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, and combined with the action of EC 1.3.99.37, 1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase, it forms the C50 carotenoid dihydrobisanhydrobacterioruberin. cf. EC 2.5.1.149, lycopene elongase/hydratase (flavuxanthin-forming).
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Haloarcula japonica
UNIPROT: M0L7V9
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The taxonomic range for the selected organisms is: Haloarcula japonica
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
c0506, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
c0506
A0A0A1GNW8
-
lycopene elongase/1,2-hydratase
A0A0A1GNW8
bifunctional enzyme
lyeJ
A0A0A1GNW8
-
lbtA
-
-
-
-
lyeJ
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
dimethylallyl-diphosphate:all-trans-lycopene dimethylallyltransferase (hydrating, dihydrobisanhydrobacterioruberin-forming)
The enzyme, characterized from the bacterium Dietzia sp. CQ4 and the halophilic archaea Halobacterium salinarum and Haloarcula japonica, 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, and combined with the action of EC 1.3.99.37, 1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase, it forms the C50 carotenoid dihydrobisanhydrobacterioruberin. cf. EC 2.5.1.149, lycopene elongase/hydratase (flavuxanthin-forming).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + all-trans-lycopene + H2O
dihydroisopentenyldehydrorhodopin + diphosphate
show the reaction diagram
dimethylallyl diphosphate + isopentenyldehydrorhodopin + H2O
dihydrobisanhydrobacterioruberin + diphosphate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + all-trans-lycopene + H2O
dihydroisopentenyldehydrorhodopin + diphosphate
show the reaction diagram
A0A0A1GNW8
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
-
-
?
dimethylallyl diphosphate + isopentenyldehydrorhodopin + H2O
dihydrobisanhydrobacterioruberin + diphosphate
show the reaction diagram
A0A0A1GNW8
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
-
-
?
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
A0A0A1GNW8
the enzyme is involved in the biosynthetic pathway of the C50 carotenoid bacterioruberin
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
J. Bacteriol.
197
1614-1623
2015
Haloarcula japonica (A0A0A1GNW8), Haloarcula japonica
Manually annotated by BRENDA team