EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.5.1.150 | 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 |
Dietzia sp. CQ4 |
dihydroisopentenyldehydrorhodopin + diphosphate |
- |
? |
2.5.1.150 | 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 |
- |
? |
2.5.1.150 | 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 |
- |
? |
2.5.1.150 | 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 |
Dietzia sp. CQ4 |
dihydrobisanhydrobacterioruberin + diphosphate |
- |
? |
2.5.1.150 | 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 |
- |
? |
2.5.1.150 | 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 |
- |
? |