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Your query returned 1 entry. Printable version
EC | 2.5.1.150 | ||||||
Accepted name: | lycopene elongase/hydratase (dihydrobisanhydrobacterioruberin-forming) | ||||||
Reaction: | (1) prenyl diphosphate + all-trans-lycopene + H2O = dihydroisopentenyldehydrorhodopin + diphosphate (2) prenyl diphosphate + isopentenyldehydrorhodopin + H2O = dihydrobisanhydrobacterioruberin + diphosphate |
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For diagram of C50-Carotenoid biosynthesis, click here and for diagram of bacterioruberin biosynthesis, click here | |||||||
Glossary: | dihydrobisanhydrobacterioruberin = (2S,2S′)-2,2′-bis(3-methylbut-2-en-1-yl)-3,3′,4,4′-tetradehydro-1,1′,2,2′-tetrahydro-ψ,ψ-carotene-1,1′-diol = (3S,4E,6E,8E,10E,12E,14E,16E,18E,20E,22E,24E,26E,30R)-2,6,10,14,19,23,27,31-octamethyl-3,30-bis(3-methylbut-2-en-1-yl)dotriaconta-4,6,8,10,12,14,16,18,20,22,24,26-dodecaene-2,31-diol | ||||||
Other name(s): | lbtA (gene name); lyeJ (gene name); dimethylallyl-diphosphate:all-trans-lycopene dimethylallyltransferase (hydrating, dihydrobisanhydrobacterioruberin-forming) | ||||||
Systematic name: | prenyl-diphosphate:all-trans-lycopene prenyltransferase (hydrating, dihydrobisanhydrobacterioruberin-forming) | ||||||
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). | ||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||
References: |
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