Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,2-epoxyphytoene + acceptor
1,2-epoxyneurosporene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + 3 acceptor
all-trans-neurosporene + 3 reduced acceptor
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
15-cis-phytoene + FAD
all-trans-phytofluene + FADH2
all-trans-neurosporene + acceptor
lycopene + reduced acceptor
all-trans-neurosporene + FAD
lycopene + FADH2
all-trans-phytofluene + 2 acceptor
all-trans-neurosporene + 2 reduced acceptor
-
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
all-trans-phytofluene + FAD
all-trans-zeta-carotene + FADH2
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
all-trans-zeta-carotene + FAD
all-trans-neurosporene + FADH2
-
-
-
-
?
phytoene + acceptor
neurosporene + reduced acceptor
-
-
-
-
?
additional information
?
-
15-cis-phytoene + 3 acceptor
all-trans-neurosporene + 3 reduced acceptor
-
the enzyme is involved in carotenoid biosynthesis
-
-
?
15-cis-phytoene + 3 acceptor
all-trans-neurosporene + 3 reduced acceptor
-
-
formation of all-trans-neurosporene and two cis-isomers
-
?
15-cis-phytoene + 3 acceptor
all-trans-neurosporene + 3 reduced acceptor
-
involved in carotenoid biosynthesis
-
-
?
15-cis-phytoene + 3 acceptor
all-trans-neurosporene + 3 reduced acceptor
-
intermediates are phytofluene and zeta-carotene. The proportion of all-trans versus cis isomers is about 20% for phytofluene, 46% for zeta-carotene, and 72% for neurosporene
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + FAD
all-trans-phytofluene + FADH2
-
-
-
-
?
15-cis-phytoene + FAD
all-trans-phytofluene + FADH2
-
-
-
-
?
all-trans-neurosporene + acceptor
lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + FAD
lycopene + FADH2
-
-
-
-
?
all-trans-neurosporene + FAD
lycopene + FADH2
-
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
additional information
?
-
at higher concentrations, phytoene is the preferred substrate for CrtI, and neurosporene is produced as the major desaturation product. At lower phytoene concentrations, neurosporene can be further desaturated by CrtI to produce lycopene, EC 1.3.99.31
-
-
?
additional information
?
-
at higher concentrations, phytoene is the preferred substrate for CrtI, and neurosporene is produced as the major desaturation product. At lower phytoene concentrations, neurosporene can be further desaturated by CrtI to produce lycopene, EC 1.3.99.31
-
-
?
additional information
?
-
-
C30-diapophytoene is not a substrate
-
-
?
additional information
?
-
-
the phytoene desaturase CrtI from Rubrivivax gelatinosus catalyzes simultaneously a three- and four-step desaturation producing both neurosporene and lycopene, determination of kinetic with the L208 modified desaturase and the specificities for phytoene and neurosporene as substrates, overview
-
-
?
additional information
?
-
-
the phytoene desaturase CrtI from Rubrivivax gelatinosus catalyzes simultaneously a three- and four-step desaturation producing both neurosporene and lycopene, determination of kinetic with the L208 modified desaturase and the specificities for phytoene and neurosporene as substrates, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
15-cis-phytoene + 3 acceptor
all-trans-neurosporene + 3 reduced acceptor
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
15-cis-phytoene + FAD
all-trans-phytofluene + FADH2
all-trans-neurosporene + acceptor
lycopene + reduced acceptor
all-trans-neurosporene + FAD
lycopene + FADH2
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
all-trans-phytofluene + FAD
all-trans-zeta-carotene + FADH2
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
all-trans-zeta-carotene + FAD
all-trans-neurosporene + FADH2
-
-
-
-
?
additional information
?
-
15-cis-phytoene + 3 acceptor
all-trans-neurosporene + 3 reduced acceptor
-
the enzyme is involved in carotenoid biosynthesis
-
-
?
15-cis-phytoene + 3 acceptor
all-trans-neurosporene + 3 reduced acceptor
-
involved in carotenoid biosynthesis
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + FAD
all-trans-phytofluene + FADH2
-
-
-
-
?
15-cis-phytoene + FAD
all-trans-phytofluene + FADH2
-
-
-
-
?
all-trans-neurosporene + acceptor
lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + FAD
lycopene + FADH2
-
-
-
-
?
all-trans-neurosporene + FAD
lycopene + FADH2
-
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
-
-
-
-
?
additional information
?
-
at higher concentrations, phytoene is the preferred substrate for CrtI, and neurosporene is produced as the major desaturation product. At lower phytoene concentrations, neurosporene can be further desaturated by CrtI to produce lycopene, EC 1.3.99.31
-
-
?
additional information
?
-
at higher concentrations, phytoene is the preferred substrate for CrtI, and neurosporene is produced as the major desaturation product. At lower phytoene concentrations, neurosporene can be further desaturated by CrtI to produce lycopene, EC 1.3.99.31
-
-
?
additional information
?
-
-
the phytoene desaturase CrtI from Rubrivivax gelatinosus catalyzes simultaneously a three- and four-step desaturation producing both neurosporene and lycopene, determination of kinetic with the L208 modified desaturase and the specificities for phytoene and neurosporene as substrates, overview
-
-
?
additional information
?
-
-
the phytoene desaturase CrtI from Rubrivivax gelatinosus catalyzes simultaneously a three- and four-step desaturation producing both neurosporene and lycopene, determination of kinetic with the L208 modified desaturase and the specificities for phytoene and neurosporene as substrates, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG -CrtBPAG
evolution
-
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG-CrtBPAG
evolution
-
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG-CrtBPAG
evolution
-
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG-CrtBPAG
evolution
-
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG-CrtBPAG
evolution
-
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG-CrtBPAG
evolution
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
evolution
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
evolution
-
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
-
evolution
-
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
-
evolution
-
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG-CrtBPAG
-
evolution
-
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG-CrtBPAG
-
evolution
-
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG-CrtBPAG
-
evolution
-
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG-CrtBPAG
-
evolution
-
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG -CrtBPAG
-
evolution
-
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
-
evolution
-
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
-
evolution
-
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
-
evolution
-
homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG-CrtBPAG
-
evolution
-
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
-
evolution
-
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
-
evolution
-
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
-
evolution
-
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
-
evolution
-
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
-
evolution
-
the enzyme belongs to the CrtI family of enzymes, analysis of the phylogenetic tree of a subset of phytoene desaturases from the CrtI family, overview. Recombinant expression of eight codon optimized CrtI enzymes from different clades in a bacterial system reveals that three CrtI enzymes can catalyse up to six desaturations, forming tetradehydrolycopene. Existence of characteristic patterns of desaturated molecules associated with various CrtI clades. Variations in the reaction rates and binding constants can explain the various carotene patterns observed. Relationship between genetic and functional evolution of certain CrtI enzymes, overview
-
metabolism
-
the enzyme is a pathway branch point enzyme in the carotenoid pathway
metabolism
-
the enzyme is a pathway branch point enzyme in the carotenoid pathway
metabolism
-
the enzyme is a pathway branch point enzyme in the carotenoid pathway
metabolism
-
the enzyme is a pathway branch point enzyme in the carotenoid pathway
metabolism
-
the enzyme is a pathway branch point enzyme in the carotenoid pathway
metabolism
the enzyme is a pathway branch point enzyme in the carotenoid pathway. Carotenoid pathways of Pantoea agglomerans wild-type and reconstructed pathways in Escherichia coli, overview
metabolism
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. Rhodobacter capsulatus strain SB1003 also produces lycopene in vitro (cf. EC 1.3.99.31)
metabolism
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. CrtI from Rhodobacter sphaeroides produced neurosporene in vitro and in vivo
metabolism
-
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. Rhodobacter capsulatus strain SB1003 also produces lycopene in vitro (cf. EC 1.3.99.31)
-
metabolism
-
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. CrtI from Rhodobacter sphaeroides produced neurosporene in vitro and in vivo
-
metabolism
-
the enzyme is a pathway branch point enzyme in the carotenoid pathway
-
metabolism
-
the enzyme is a pathway branch point enzyme in the carotenoid pathway
-
metabolism
-
the enzyme is a pathway branch point enzyme in the carotenoid pathway
-
metabolism
-
the enzyme is a pathway branch point enzyme in the carotenoid pathway
-
metabolism
-
the enzyme is a pathway branch point enzyme in the carotenoid pathway. Carotenoid pathways of Pantoea agglomerans wild-type and reconstructed pathways in Escherichia coli, overview
-
metabolism
-
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. CrtI from Rhodobacter sphaeroides produced neurosporene in vitro and in vivo
-
metabolism
-
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. CrtI from Rhodobacter sphaeroides produced neurosporene in vitro and in vivo
-
metabolism
-
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. Rhodobacter capsulatus strain SB1003 also produces lycopene in vitro (cf. EC 1.3.99.31)
-
metabolism
-
the enzyme is a pathway branch point enzyme in the carotenoid pathway
-
metabolism
-
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. CrtI from Rhodobacter sphaeroides produced neurosporene in vitro and in vivo
-
metabolism
-
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. CrtI from Rhodobacter sphaeroides produced neurosporene in vitro and in vivo
-
metabolism
-
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. CrtI from Rhodobacter sphaeroides produced neurosporene in vitro and in vivo
-
metabolism
-
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. Rhodobacter capsulatus strain SB1003 also produces lycopene in vitro (cf. EC 1.3.99.31)
-
metabolism
-
carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. CrtI from Rhodobacter sphaeroides produced neurosporene in vitro and in vivo
-
metabolism
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carotenoid biosynthesis starts with the symmetrical condensation of two geranylgeranyl diphosphate molecules, forming phytoene. A series of successive desaturation reactions convert phytoene into phytofluene, zeta-carotene, neurosporene, lycopene. These desaturation reactions can be accomplished by a single enzyme (poly-trans pathway) or through a cascade of different enzymes (poly-cis pathway). In algae and plants, four different enzymes are necessary to form the final product (all-trans-lycopene). The phytoene and the zeta-carotene desaturases (PDS and ZDS, respectively) add double bonds in the cis-conformation. ZISO (zeta-carotene isomerase) and CRTISO (prolycopene isomerase) convert the cis-carotenes into di-cis-zeta-carotene and all-trans-lycopene, respectively. By contrast to other phytoene desaturases, CrtI are versatile enzymes classified into four enzymatic subgroups (EC 1.3.99.28, EC 1.3.99.29, EC 1.3.99.30, and EC 1.3.99.31) based on the last product they presumably produce (from zeta-carotene to didehydrolycopene). Carotene diversity can be further expanded in later steps with the addition of one or two rings by lycopene cyclases, thereby producing an extensive variety of symmetrical or asymmetrical cyclised carotenes, such as beta-zeacarotene, dehydro-beta-carotene, gamma-carotene, beta-carotene, and the fungi-specific torulene. When expressed in heterologous hosts, CrtI enzymes exhibit distinct desaturation patterns, CrtI enzyme activities may depend on the experimental conditions and thus be inconsistent with the patterns generated in the natural host. CrtI from Rhodobacter sphaeroides produced neurosporene in vitro and in vivo
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physiological function
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involved in carotenoid biosynthesis
physiological function
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involved in carotenoid biosynthesis
physiological function
involved in carotenoid biosynthesis
additional information
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Leu208 is exchanged in the neurosporene or lycopene-forming desaturase
additional information
Rhodobacter azotoformans cntains a carotenogenesis gene cluster with an unusual organization and a phytoene desaturase catalyzing both three- and four-step desaturations. CrtI from Rhodobacter azotoformans CGMCC 6086 can produce three-step desaturated neurosporene and four-step desaturated lycopene as major products, see also EC 1.3.99.31, together with small amounts of five-step desaturated 3,4-didehydrolycopene, EC 1.3.99.30
additional information
comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
additional information
comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
additional information
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Leu208 is exchanged in the neurosporene or lycopene-forming desaturase
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additional information
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comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
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additional information
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comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
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additional information
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comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
-
additional information
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comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
-
additional information
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comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
-
additional information
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comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
-
additional information
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comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
-
additional information
-
Rhodobacter azotoformans cntains a carotenogenesis gene cluster with an unusual organization and a phytoene desaturase catalyzing both three- and four-step desaturations. CrtI from Rhodobacter azotoformans CGMCC 6086 can produce three-step desaturated neurosporene and four-step desaturated lycopene as major products, see also EC 1.3.99.31, together with small amounts of five-step desaturated 3,4-didehydrolycopene, EC 1.3.99.30
-
additional information
-
comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
-
additional information
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comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
-
additional information
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comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
-
additional information
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comparison of the natural evolution and kinetic properties of selected CrtI enzymes expressed and assayed under standardised conditions. Potentially all CrtI enzymes can catalyse desaturation reactions that progress beyond the already observed end-products and the pattern of products formed originates from variations in the reaction rates rather than affinity constants
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F166I
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mutation changes the product of phytoene desaturation from neurosporene to lycopene
H12Q
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mutation has little effect on the product formation
M402T
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mutation has a negative effect on percent lycopene production
V68D
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mutation changes the product of phytoene desaturation from neurosporene to lycopene
L153P/L278P
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site-directed mutagenesis, the mutant shows altered secondary structure and substrate desaturation level with increased lycopene production compared to the wild-type enzyme
L208F
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site-directed mutagenesis, the mutant shows altered secondary structure and substrate desaturation level with increased lycopene production compared to the wild-type enzyme
L208P
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site-directed mutagenesis, the mutant shows altered secondary structure compared to the wild-type enzyme
T256M/D355G/L424P
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site-directed mutagenesis, the mutant shows altered secondary structure and substrate desaturation level with increased lycopene production compared to the wild-type enzyme
Y44C/D53G/P134L/V395A
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site-directed mutagenesis, the mutant shows altered secondary structure and substrate desaturation level with increased lycopene production compared to the wild-type enzyme
additional information
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functional complementation of heterogeneous phytoene desaturases (CrtIs) from 5 carotenogenic microorganisms, overview
additional information
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functional complementation of heterogeneous phytoene desaturases (CrtIs) from 5 carotenogenic microorganisms, overview
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additional information
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directed evolution is used to change the product of Rhodobacter sphaeroides phytoene desaturase (crtI gene product), a neurosporene-producing enzyme, to lycopene. Two generations of random mutagenesis are performed, from which three positive mutants are isolated and sequenced. Site-directed mutagenesis is used to determine the effect of each amino acid change
additional information
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functional complementation of heterogeneous phytoene desaturases (CrtIs) from 5 carotenogenic microorganisms, overview
additional information
competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
additional information
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competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
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additional information
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competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
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additional information
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competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
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additional information
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competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
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additional information
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competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
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additional information
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functional complementation of heterogeneous phytoene desaturases (CrtIs) from 5 carotenogenic microorganisms, overview
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additional information
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competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
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additional information
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competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
-
additional information
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competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
-
additional information
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functional complementation of heterogeneous phytoene desaturases (CrtIs) from 5 carotenogenic microorganisms, overview
additional information
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functional complementation of heterogeneous phytoene desaturases (CrtIs) from 5 carotenogenic microorganisms, overview
-
additional information
functional complementation of heterogeneous phytoene desaturases (CrtIs) from 5 carotenogenic microorganisms, overview
additional information
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functional complementation of heterogeneous phytoene desaturases (CrtIs) from 5 carotenogenic microorganisms, overview
-
additional information
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functional complementation of heterogeneous phytoene desaturases (CrtIs) from 5 carotenogenic microorganisms, overview
additional information
competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
additional information
-
competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
-
additional information
-
functional complementation of heterogeneous phytoene desaturases (CrtIs) from 5 carotenogenic microorganisms, overview
-
additional information
-
competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
-
additional information
-
competition between lycopene cyclase and the phytoene desaturases modified the distribution between carotene intermediates when expressed in yeast in the context of the full beta-carotene production pathway
-
additional information
-
functional complementation of heterogeneous phytoene desaturases (CrtIs) from 5 carotenogenic microorganisms, overview
additional information
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functional complementation of heterogeneous phytoene desaturases (CrtIs) from 5 carotenogenic microorganisms, overview
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expression in Escherichia coli
gene crtI, cloning and expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha
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gene crtI, cloning of the crt gene cluster crtCDEF, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene crtI, phylogenetic tree, co-expression with 5 other enzymes of the carotenoid pathway from Pantoea agglomerans, i.e. IPP isomerase, FPP synthase, GGPP synthase, phytoene synthase, lycopene cyclase, beta-carotene hydrolase, and zeaxanthin glucosyltransferase, in Escherichia coli, functional complementation by CrtI of Brevibacterium linens, CGI, CrtI of Corynebacterium glutamicum, RSI, CrtI of Rhodobacter sphaeroides RCI, CrtI of Rhodobacter capsulatus, and RBI, CrtI of Rhodopirellula baltica, and the homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG -CrtBPAG
gene crtI, sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
sequence comparisons and phylogenetic analysis, recombinant expression in Escherichia coli
the phytoene desaturase gene, from Rhodobacter capsulatus is functionally complemented with a gene construct from Erwinia uredovora which encodes all enzymes responsible for formation of 15-cis phytoene in Escherichia coli
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expression in Escherichia coli
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expression in Escherichia coli
gene crtI, phylogenetic tree, co-expression with 5 other enzymes of the carotenoid pathway from Pantoea agglomerans, i.e. IPP isomerase, FPP synthase, GGPP synthase, phytoene synthase, lycopene cyclase, beta-carotene hydrolase, and zeaxanthin glucosyltransferase, in Escherichia coli, functional complementation by CrtI of Brevibacterium linens, CGI, CrtI of Corynebacterium glutamicum, RSI, CrtI of Rhodobacter sphaeroides RCI, CrtI of Rhodobacter capsulatus, and RBI, CrtI of Rhodopirellula baltica, and the homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG -CrtBPAG
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gene crtI, phylogenetic tree, co-expression with 5 other enzymes of the carotenoid pathway from Pantoea agglomerans, i.e. IPP isomerase, FPP synthase, GGPP synthase, phytoene synthase, lycopene cyclase, beta-carotene hydrolase, and zeaxanthin glucosyltransferase, in Escherichia coli, functional complementation by CrtI of Brevibacterium linens, CGI, CrtI of Corynebacterium glutamicum, RSI, CrtI of Rhodobacter sphaeroides RCI, CrtI of Rhodobacter capsulatus, and RBI, CrtI of Rhodopirellula baltica, and the homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG -CrtBPAG
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gene crtI, phylogenetic tree, co-expression with 5 other enzymes of the carotenoid pathway from Pantoea agglomerans, i.e. IPP isomerase, FPP synthase, GGPP synthase, phytoene synthase, lycopene cyclase, beta-carotene hydrolase, and zeaxanthin glucosyltransferase, in Escherichia coli, functional complementation by CrtI of Brevibacterium linens, CGI, CrtI of Corynebacterium glutamicum, RSI, CrtI of Rhodobacter sphaeroides RCI, CrtI of Rhodobacter capsulatus, and RBI, CrtI of Rhodopirellula baltica, and the homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG -CrtBPAG
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gene crtI, phylogenetic tree, co-expression with 5 other enzymes of the carotenoid pathway from Pantoea agglomerans, i.e. IPP isomerase, FPP synthase, GGPP synthase, phytoene synthase, lycopene cyclase, beta-carotene hydrolase, and zeaxanthin glucosyltransferase, in Escherichia coli, functional complementation by CrtI of Brevibacterium linens, CGI, CrtI of Corynebacterium glutamicum, RSI, CrtI of Rhodobacter sphaeroides RCI, CrtI of Rhodobacter capsulatus, and RBI, CrtI of Rhodopirellula baltica, and the homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG -CrtBPAG
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gene crtI, phylogenetic tree, co-expression with 5 other enzymes of the carotenoid pathway from Pantoea agglomerans, i.e. IPP isomerase, FPP synthase, GGPP synthase, phytoene synthase, lycopene cyclase, beta-carotene hydrolase, and zeaxanthin glucosyltransferase, in Escherichia coli, functional complementation by CrtI of Brevibacterium linens, CGI, CrtI of Corynebacterium glutamicum, RSI, CrtI of Rhodobacter sphaeroides RCI, CrtI of Rhodobacter capsulatus, and RBI, CrtI of Rhodopirellula baltica, and the homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG -CrtBPAG
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gene crtI, phylogenetic tree, co-expression with 5 other enzymes of the carotenoid pathway from Pantoea agglomerans, i.e. IPP isomerase, FPP synthase, GGPP synthase, phytoene synthase, lycopene cyclase, beta-carotene hydrolase, and zeaxanthin glucosyltransferase, in Escherichia coli, functional complementation by CrtI of Brevibacterium linens, CGI, CrtI of Corynebacterium glutamicum, RSI, CrtI of Rhodobacter sphaeroides RCI, CrtI of Rhodobacter capsulatus, and RBI, CrtI of Rhodopirellula baltica, and the homologous complementation of CrtI from Pantoea agglomerans with the Pantoea agglomerans carotenogenic module expressing CrtEPAG -CrtBPAG
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Structural and kinetics properties of a mutated phytoene desaturase from Rubrivivax gelatinosus with modified product specificity
Arch. Biochem. Biophys.
505
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Rubrivivax gelatinosus, Rubrivivax gelatinosus CGMCC 6086
brenda
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Purification in an active state and properties of the 3-step phytoene desaturase from Rhodobacter capsulatus overexpressed in Escherichia coli
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Rhodobacter capsulatus
brenda
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Carotenoid biosynthesis in photosynthetic bacteria. Genetic characterization of the Rhodobacter capsulatus CrtI protein
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Rhodobacter capsulatus (P17054)
brenda
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Alteration of product specificity of Rhodobacter sphaeroides phytoene desaturase by directed evolution
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Cereibacter sphaeroides
brenda
Linden, H.; Misawa, N.; Chamovitz, D.; Pecker, I.; Hirschberg, J.; Sandmann, G.
Functional complementation in Escherichia coli of different phytoene desaturase genes and analysis of accumulated carotenes
Z. Naturforsch. C
46
1045-1051
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Rhodobacter capsulatus
brenda
Song, G.H.; Kim, S.H.; Choi, B.H.; Han, S.J.; Lee, P.C.
Heterologous carotenoid-biosynthetic enzymes: functional complementation and effects on carotenoid profiles in Escherichia coli
Appl. Environ. Microbiol.
79
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Corynebacterium glutamicum, Brevibacterium linens, Rhodobacter capsulatus, Cereibacter sphaeroides, Rhodopirellula baltica, Pantoea agglomerans (K7WPN7), Rhodopirellula baltica DSM 10527, Rhodobacter capsulatus KCTC 2583, Cereibacter sphaeroides KCTC 12085, Corynebacterium glutamicum KCTC 1445, Pantoea agglomerans KCTC 2479 (K7WPN7), Brevibacterium linens DSM 20426
brenda
Zhang, J.; Lu, L.; Yin, L.; Xie, S.; Xiao, M.
Carotenogenesis gene cluster and phytoene desaturase catalyzing both three- and four-step desaturations from Rhodobacter azotoformans
FEMS Microbiol. Lett.
333
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2012
Cereibacter azotoformans (G3FHJ1), Cereibacter azotoformans CGMCC 6086 (G3FHJ1)
brenda
Chi, S.C.; Mothersole, D.J.; Dilbeck, P.; Niedzwiedzki, D.M.; Zhang, H.; Qian, P.; Vasilev, C.; Grayson, K.J.; Jackson, P.J.; Martin, E.C.; Li, Y.; Holten, D.; Neil Hunter, C.
Assembly of functional photosystem complexes in Rhodobacter sphaeroides incorporating carotenoids from the spirilloxanthin pathway
Biochim. Biophys. Acta
1847
189-201
2015
Cereibacter sphaeroides (P54980), Cereibacter sphaeroides DSM 158 (P54980)
brenda
Ding, B.Y.; Niu, J.; Shang, F.; Yang, L.; Chang, T.Y.; Wang, J.J.
Characterization of the geranylgeranyl diphosphate synthase gene in Acyrthosiphon pisum (Hemiptera Aphididae) and its association with carotenoid biosynthesis
Front. Physiol.
10
1398
2019
Rhodobacter capsulatus (P17054), Cereibacter sphaeroides (P54980), Rhodobacter capsulatus NBRC 16581 (P17054), Cereibacter sphaeroides ATCC 17023 (P54980), Cereibacter sphaeroides JCM 6121 (P54980), Cereibacter sphaeroides CCUG 31486 (P54980), Rhodobacter capsulatus ATCC BAA-309 (P17054), Cereibacter sphaeroides LMG 2827 (P54980), Cereibacter sphaeroides NBRC 12203 (P54980), Cereibacter sphaeroides ATH 2.4.1. (P54980), Rhodobacter capsulatus SB1003 (P17054), Cereibacter sphaeroides DSM 158 (P54980), Cereibacter sphaeroides NCIMB 8253 (P54980)
brenda