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1-hydroxylycopene + acceptor
1-hydroxy-3',4'-didehydrolycopene + reduced acceptor
-
Substrates: -
Products: -
?
1-hydroxyneurosporene + acceptor
1-hydroxylycopene + reduced acceptor
-
Substrates: -
Products: -
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
all-trans-lycopene + 1 acceptor
all-trans-3,4-didehydrolycopene + 1 reduced acceptor
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
all-trans-neurosporene + 2 acceptor
all-trans-3,4-didehydrolycopene + 2 reduced acceptor
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
all-trans-phytofluene + 4 acceptor
all-trans-3,4-didehydrolycopene + 4 reduced acceptor
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
all-trans-zeta-carotene + 3 acceptor
all-trans-3,4-didehydrolycopene + 3 reduced acceptor
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
additional information
?
-
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
Substrates: -
Products: -
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
Substrates: the enzyme is involved in the carotenoid biosynthesis pathway to beta-carotene and torulene
Products: -
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
Substrates: -
Products: -
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
Substrates: a decisive reaction for the formation of monocyclic or bicyclic products is the desaturation sequence to lycopene and further on to 3,4-didehydrolycopene. In the nontransformed strain, cyclization of lycopene, which directs the metabolic flux towards astaxanthin, is the dominating reaction. When the gene encoding phytoene desaturase is overexpressed, the five-step desaturation to 3,4-didehydrolycopene is intensified, resulting in an accumulation of torulene and 3-hydroxy-3'-4'-didehydro-beta-psi-caroten-4-one as subsequent products
Products: -
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
Substrates: -
Products: -
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
Substrates: a decisive reaction for the formation of monocyclic or bicyclic products is the desaturation sequence to lycopene and further on to 3,4-didehydrolycopene. In the nontransformed strain, cyclization of lycopene, which directs the metabolic flux towards astaxanthin, is the dominating reaction. When the gene encoding phytoene desaturase is overexpressed, the five-step desaturation to 3,4-didehydrolycopene is intensified, resulting in an accumulation of torulene and 3-hydroxy-3'-4'-didehydro-beta-psi-caroten-4-one as subsequent products
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + 1 acceptor
all-trans-3,4-didehydrolycopene + 1 reduced acceptor
-
Substrates: -
Products: -
?
all-trans-lycopene + 1 acceptor
all-trans-3,4-didehydrolycopene + 1 reduced acceptor
-
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + 2 acceptor
all-trans-3,4-didehydrolycopene + 2 reduced acceptor
-
Substrates: -
Products: -
?
all-trans-neurosporene + 2 acceptor
all-trans-3,4-didehydrolycopene + 2 reduced acceptor
-
Substrates: -
Products: -
?
all-trans-neurosporene + 2 acceptor
all-trans-3,4-didehydrolycopene + 2 reduced acceptor
-
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + 4 acceptor
all-trans-3,4-didehydrolycopene + 4 reduced acceptor
-
Substrates: -
Products: -
?
all-trans-phytofluene + 4 acceptor
all-trans-3,4-didehydrolycopene + 4 reduced acceptor
-
Substrates: -
Products: -
?
all-trans-phytofluene + 4 acceptor
all-trans-3,4-didehydrolycopene + 4 reduced acceptor
-
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + 3 acceptor
all-trans-3,4-didehydrolycopene + 3 reduced acceptor
-
Substrates: -
Products: -
?
all-trans-zeta-carotene + 3 acceptor
all-trans-3,4-didehydrolycopene + 3 reduced acceptor
-
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: gamma-carotene and 1,1'-dihydroxylycopene are not accepted as substrate
Products: -
?
additional information
?
-
Substrates: catalyzes both enzymatic conversion of phytoene to lycopene (fourth step product) and 3,4-didehydrolycopene (fifth step product), reactions of EC 1.3.99.30 and EC 1.3.99.31, respectively
Products: -
?
additional information
?
-
Substrates: catalyzes both enzymatic conversion of phytoene to lycopene (fourth step product) and 3,4-didehydrolycopene (fifth step product), reactions of EC 1.3.99.30 and EC 1.3.99.31, respectively
Products: -
?
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15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
Substrates: the enzyme is involved in the carotenoid biosynthesis pathway to beta-carotene and torulene
Products: -
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
Substrates: a decisive reaction for the formation of monocyclic or bicyclic products is the desaturation sequence to lycopene and further on to 3,4-didehydrolycopene. In the nontransformed strain, cyclization of lycopene, which directs the metabolic flux towards astaxanthin, is the dominating reaction. When the gene encoding phytoene desaturase is overexpressed, the five-step desaturation to 3,4-didehydrolycopene is intensified, resulting in an accumulation of torulene and 3-hydroxy-3'-4'-didehydro-beta-psi-caroten-4-one as subsequent products
Products: -
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
Substrates: a decisive reaction for the formation of monocyclic or bicyclic products is the desaturation sequence to lycopene and further on to 3,4-didehydrolycopene. In the nontransformed strain, cyclization of lycopene, which directs the metabolic flux towards astaxanthin, is the dominating reaction. When the gene encoding phytoene desaturase is overexpressed, the five-step desaturation to 3,4-didehydrolycopene is intensified, resulting in an accumulation of torulene and 3-hydroxy-3'-4'-didehydro-beta-psi-caroten-4-one as subsequent products
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
15-cis-phytoene + acceptor
all-trans-phytofluene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-phytofluene + acceptor
all-trans-zeta-carotene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
all-trans-zeta-carotene + acceptor
all-trans-neurosporene + reduced acceptor
Substrates: -
Products: -
?
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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.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
-
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
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. Pantoea ananatis CrtI produces lycopene in vivo, but also tetradehydrolycopene in vitro
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. Blakeslea trispora CrtI produces lycopene in vivo and in vitro (see also EC 1.3.99.31), but also didehydrolycopene 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. Pantoea ananatis CrtI produces lycopene in vivo, but also tetradehydrolycopene in vitro
-
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. Pantoea ananatis CrtI produces lycopene in vivo, but also tetradehydrolycopene in vitro
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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. Pantoea ananatis CrtI produces lycopene in vivo, but also tetradehydrolycopene in vitro
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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. Pantoea ananatis CrtI produces lycopene in vivo, but also tetradehydrolycopene in vitro
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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. Pantoea ananatis CrtI produces lycopene in vivo, but also tetradehydrolycopene in vitro
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physiological function
the expression product of crtI is essential for phytoene conversion to lycopene and 3,4-didehydrolycopene
physiological function
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the expression product of crtI is essential for phytoene conversion to lycopene and 3,4-didehydrolycopene
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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
-
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
-
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
-
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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Estrada, A.F.; Maier, D.; Scherzinger, D.; Avalos, J.; Al-Babili, S.
Novel apocarotenoid intermediates in Neurospora crassa mutants imply a new biosynthetic reaction sequence leading to neurosporaxanthin formation
Fungal Genet. Biol.
45
1497-1505
2008
Neurospora crassa
brenda
Verdoes, J.C.; Sandmann, G.; Visser, H.; Diaz, M.; van Mossel, M.; van Ooyen, A.J.
Metabolic engineering of the carotenoid biosynthetic pathway in the yeast Xanthophyllomyces dendrorhous (Phaffia rhodozyma)
Appl. Environ. Microbiol.
69
3728-3738
2003
Phaffia rhodozyma, Phaffia rhodozyma CBS 6938
brenda
Hausmann, A.; Sandmann, G.
A single five-step desaturase is involved in the carotenoid biosynthesis pathway to beta-carotene and torulene in Neurospora crassa
Fungal Genet. Biol.
30
147-153
2000
Neurospora crassa
brenda
Li, C.; Zhang, N.; Song, J.; Wei, N.; Li, B.; Zou, H.; Han, X.
A single desaturase gene from red yeast Sporidiobolus pararoseus is responsible for both four- and five-step dehydrogenation of phytoene
Gene
590
169-176
2016
Sporidiobolus pararoseus (A0A0K0QVD9), Sporidiobolus pararoseus CGMCC 2.5280 (A0A0K0QVD9)
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
Blakeslea trispora (Q67GI0), Neurospora crassa (P21334), Neurospora crassa 74-OR23-1A (P21334), Neurospora crassa ATCC 24698 (P21334), Neurospora crassa CBS 708.71 (P21334), Neurospora crassa DSM 1257 (P21334), Neurospora crassa FGSC 987 (P21334)
brenda