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Enzyme Nomenclature
Information on EC 1.3.99.30 - phytoene desaturase (3,4-didehydrolycopene-forming)
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EC Tree
1.3.99.30 phytoene desaturase (3,4-didehydrolycopene-forming)IUBMB Comments
This enzyme is involved in carotenoid biosynthesis and catalyses up to five desaturation steps (cf. EC 1.3.99.28 [phytoene desaturase (neurosporene-forming)], EC 1.3.99.29 [phytoene desaturase (zeta-carotene-forming)] and EC 1.3.99.31 [phytoene desaturase (lycopene-forming)]).
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The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Al-1
CrtI
PDS
phytoene desaturase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
overall reaction
-
15-cis-phytoene + 5 acceptor = all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
15-cis-phytoene:acceptor oxidoreductase (3,4-didehydrolycopene-forming)
This enzyme is involved in carotenoid biosynthesis and catalyses up to five desaturation steps (cf. EC 1.3.99.28 [phytoene desaturase (neurosporene-forming)], EC 1.3.99.29 [phytoene desaturase (zeta-carotene-forming)] and EC 1.3.99.31 [phytoene desaturase (lycopene-forming)]).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-hydroxylycopene + acceptor
1-hydroxy-3',4'-didehydrolycopene + reduced acceptor
-
-
-
-
?
1-hydroxyneurosporene + acceptor
1-hydroxylycopene + reduced acceptor
-
-
-
-
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
-
-
-
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
the enzyme is involved in the carotenoid biosynthesis pathway to beta-carotene and torulene
-
-
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
-
-
-
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
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
-
-
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
-
-
-
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
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
-
-
?
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
-
-
-
?
all-trans-lycopene + 1 acceptor
all-trans-3,4-didehydrolycopene + 1 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-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
-
-
-
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
-
-
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
-
-
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
-
-
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
-
-
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + 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 + 2 acceptor
all-trans-3,4-didehydrolycopene + 2 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-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
all-trans-lycopene + 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 + 4 acceptor
all-trans-3,4-didehydrolycopene + 4 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-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 + 3 acceptor
all-trans-3,4-didehydrolycopene + 3 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
-
-
-
?
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
?
-
-
gamma-carotene and 1,1'-dihydroxylycopene are not accepted as substrate
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
the enzyme is involved in the carotenoid biosynthesis pathway to beta-carotene and torulene
-
-
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
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
-
-
?
15-cis-phytoene + 5 acceptor
all-trans-3,4-didehydrolycopene + 5 reduced acceptor
-
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
-
-
?
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
-
-
-
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
-
-
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
-
-
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
-
-
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
-
-
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
-
-
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
-
-
?
all-trans-lycopene + acceptor
all-trans-3,4-didehydrolycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
all-trans-lycopene + reduced acceptor
-
-
-
?
all-trans-neurosporene + acceptor
all-trans-lycopene + 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
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
addition of FAD results in product formation close to that of the control without additions
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
more than 2fold stimulation of activity compared to control, assay with supernatant of Escherichia coli recombinantly expressing phytoene desaturase from Neurospora crassa
NADP+
-
stimulation is lower than with NAD+, assay with supernatant of Escherichia coli recombinantly expressing phytoene desaturase from Neurospora crassa
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
classical Michaelis-Menten kinetic model
-
additional information
additional information
classical Michaelis-Menten kinetic model
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme, catalyzes both reactions of EC 1.3.99.30 and EC 1.3.99.31
UniProt
brenda
bifunctional enzyme, catalyzes both reactions of EC 1.3.99.30 and EC 1.3.99.31
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
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
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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
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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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). CRTI_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
595
1
66367
Swiss-Prot
Mitochondrion (Reliability: 5)
CRTI_PHYB8
Phycomyces blakesleeanus (strain ATCC 8743b / DSM 1359 / FGSC 10004 / NBRC 33097 / NRRL 1555)
583
1
65984
Swiss-Prot
other Location (Reliability: 4)
CRTI_CERNC
621
1
69530
Swiss-Prot
Mitochondrion (Reliability: 3)
I6PE27_GERHY
249
0
28279
TrEMBL
other Location (Reliability: 5)
A0A3S5XGQ4_TRIFG
105
0
11594
TrEMBL
other Location (Reliability: 2)
A0A0K0QVD9_9BASI
560
1
62284
TrEMBL
other Location (Reliability: 1)
A0A0P0KMF9_PHARH
582
1
65057
TrEMBL
other Location (Reliability: 2)
A0A8K1X5W8_9BASI
552
1
61787
TrEMBL
Mitochondrion (Reliability: 5)
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