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Enzyme Nomenclature
Information on EC 1.3.5.6 - 9,9'-dicis-zeta-carotene desaturase
Word Map on EC 1.3.5.6
- 1.3.5.6
-
carotenoid
- lycopene
-
virus-induced
-
desaturation
- beta-carotene
-
carotenogenic
-
rattle
- benthamiana
- norflurazon
-
bleach
- zeaxanthin
- astaxanthin
-
geranylgeranyl
- pluvialis
- neurosporene
-
carotenogenesis
-
beta-cyclase
-
ketolase
- chromoplasts
- dendrorhous
- protoporphyrinogen
-
phytofluene
- uredovora
-
ketocarotenoids
-
photo-bleaching
-
epsilon-cyclase
-
chelatase
- haematococcus
-
xanthophyl
-
xanthophyllomyces
- violaxanthin
-
agroinfiltration
-
provitamin
- diphenylamine
-
immutans
-
apocarotenoids
- fluridone
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
1.3.5.6
-
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RECOMMENDED NAME
GeneOntology No.
9,9'-dicis-zeta-carotene desaturase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
7,9,9'-tricis-neurosporene + a quinone = 7,9,7',9'-tetracis-lycopene + a quinol
-
-
-
-
9,9'-dicis-zeta-carotene + 2 quinone = 7,9,7',9'-tetracis-lycopene + 2 quinol
-
-
-
-
9,9'-dicis-zeta-carotene + a quinone = 7,9,9'-tricis-neurosporene + a quinol
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
9,9'-dicis-zeta-corotene:quinone oxidoreductase
This enzyme is involved in carotenoid biosynthesis in plants and cyanobacteria.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
red-fleshed variant, single copy gene zds; yellow-fleshed variant, single copy gene zds
-
-
red-fleshed variant, single copy gene zds; yellow-fleshed variant, single copy gene zds
-
-
contains two completely unrelated zeta-carotene desaturases CrtQa and CrtQb, encoded by genes crtQa and crtQb
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
approximately 10% of known phytoene desaturases, as in Rhodobacter, produce neurosporene, whereas the rest produce lycopene. These two types of enzymes, although similar in function, have relatively low similarity, below 60%, in terms of nucleotide or amino acid sequence. Phytoene desaturase encoded by gene crtI is a neurosporene-producing enzyme
metabolism
physiological function
additional information
metabolism
-
the expression of zeta-carotene desaturase paralleles plastid terminal oxidase (PTOX, quinol:oxygen oxidoreductase) and zeta-carotene desaturase. The three genes are expressed when carotinoid biosynthesis is enhanced during fruit ripening
metabolism
-
the expression of zeta-carotene desaturase paralleles plastid terminal oxidase (PTOX, quinol:oxygen oxidoreductase) and zeta-carotene desaturase. The three genes are expressed when carotinoid biosynthesis is enhanced during fruit ripening. Tomato ghost mutant with impaired plastid terminal oxidase accumulate phytoene in leaves and fruits
metabolism
-
phytoene desaturase CrtI from Rubrivivax gelatinosus catalyzes simultaneously a three- and four-step desaturation producing both neurosporene and lycopene. These carotenes are intermediates for the synthesis of spheroidene and spirilloxanthin, respectively
metabolism
carotene desaturation, an essential step in the carotenoid biosynthesis pathway, is catalyzed by two carotene desaturases, phytoene desaturase, PDS, and zeta-carotene desaturase, ZDS
metabolism
the zeta-carotene desaturase is involved in the carotenogenic pathway, that is made up of three main parts: geranylgeranyl diphosphate biosynthesis, lycopene generation, and the formation of carotenoids with cyclohexene and their derivatives, overview
metabolism
-
the zeta-carotene desaturase is involved in the carotenogenic pathway, overview
metabolism
-
the enzyme is important in carotenoid biosynthesis pathway in citrus fruits, overview
metabolism
-
ZDS is a key enzyme in carotenogenesis serving downstream of zeta-carotene in the carotenoid biosynthetic pathway, overview
metabolism
-
ZDS is a key enzyme in carotenogenesis serving downstream of zeta-carotene in the carotenoid biosynthetic pathway, overview
-
metabolism
-
the zeta-carotene desaturase is involved in the carotenogenic pathway, overview
-
metabolism
-
the enzyme is important in carotenoid biosynthesis pathway in citrus fruits, overview
-
metabolism
-
the zeta-carotene desaturase is involved in the carotenogenic pathway, that is made up of three main parts: geranylgeranyl diphosphate biosynthesis, lycopene generation, and the formation of carotenoids with cyclohexene and their derivatives, overview
-
metabolism
-
phytoene desaturase CrtI from Rubrivivax gelatinosus catalyzes simultaneously a three- and four-step desaturation producing both neurosporene and lycopene. These carotenes are intermediates for the synthesis of spheroidene and spirilloxanthin, respectively
-
metabolism
-
carotene desaturation, an essential step in the carotenoid biosynthesis pathway, is catalyzed by two carotene desaturases, phytoene desaturase, PDS, and zeta-carotene desaturase, ZDS
-
physiological function
-
phytoene desaturase encoded by crtI catalyzes the desaturation of phytoene in the carotenoid biosynthesis pathway, approximately 10% of known phytoene desaturases, as in Rhodobacter, produce neurosporene, whereas the rest produce lycopene, mechanism controlling the product specificity, phytoene desaturase encoded by gene crtI is a neurosporene-producing enzyme, overview
physiological function
-
Zds is a key gene important in the regulation of carotenoid accumulation, including the early steps of the pathway, regulated during fruit maturation. Altered flow of carotenoid precursors during fruit maturation due to abscission agents is suggested by changes in phytoene desaturase and zeta-carotene desaturase gene expression. As fruit mature, increased phytoene desaturase (Pds) and zeta-carotene desaturase (Zds) gene expression result in increased downstream carotenoid content
physiological function
-
Zds is a key gene important in the regulation of carotenoid accumulation, including the early steps of the pathway, regulated during fruit maturation. Altered flow of carotenoid precursors during fruit maturation due to abscission agents is suggested by changes in phytoene desaturase and zeta-carotene desaturase gene expression. As fruit mature, increased phytoene desaturase (Pds) and zeta-carotene desaturase (Zds) gene expression result in increased downstream carotenoid content
-
additional information
-
Leu208, located in a highly hydrophobic membrane-integrated region, is important in substrate binding
additional information
-
the differential accumulation of carotenoids in red- and yellow-fleshed papaya varieties, being higher in the red-fleshed variant, might be partly explained by the transcriptional level of CpPDS, encoding phytoene desaturase, and CpZDS
additional information
-
the differential accumulation of carotenoids in red- and yellow-fleshed papaya varieties, being higher in the red-fleshed variant, might be partly explained by the transcriptional level of CpPDS, encoding phytoene desaturase, and CpZDS
-
additional information
-
Leu208, located in a highly hydrophobic membrane-integrated region, is important in substrate binding
-
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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
zeta-carotene + 2 decyl-plastoquinone
lycopene + 2 decyl-plastoquinol
-
zeta-carotene desaturase has no preference for certain isomers. The nature of the isomers formed during catalysis depends strictly on the isomeric composition of the substrate. Different lycopene isomers are formed, including substantial amounts of the all-trans form, together with 7,7',9,9'-tetracis prolycopene via the corresponding neurosporene isomers
-
-
?
zeta-carotene + 2 decyl-ubiquinone
lycopene + 2 decyl-ubiquinone
-
zeta-carotene desaturase has no preference for certain isomers. The nature of the isomers formed during catalysis depends strictly on the isomeric composition of the substrate. Different lycopene isomers are formed, including substantial amounts of the all-trans form, together with 7,7',9,9'-tetracis prolycopene via the corresponding neurosporene isomers
-
-
?
zeta-carotene + 2 quinone
lycopene + 2 quinol
-
zeta-carotene desaturase has no preference for certain isomers. The nature of the isomers formed during catalysis depends strictly on the isomeric composition of the substrate. Different lycopene isomers are formed, including substantial amounts of the all-trans form, together with 7,7',9,9'-tetracis prolycopene via the corresponding neurosporene isomers
-
-
?
zeta-carotene + decyl-plastoquinone
neurosporene + decyl-plastoquinol
-
-
-
-
?
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
-
-
-
?
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
-
-
-
?
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
-
-
-
?
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
catalyzed by zeta-carotene desaturase CrtQa, very poorly by CrtQb
-
-
?
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
mutant activity
-
-
?
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
-
-
-
?
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
-
-
-
?
9,9'-dicis-zeta-carotene + 2 quinone
7,9,7',9'-tetracis-lycopene + 2 quinol
-
the expression of zeta-carotene desaturase paralleles plastid terminal oxidase (PTOX, quinol:oxygen oxidoreductase) and zeta-carotene desaturase. The three genes are expressed when carotinoid biosynthesis is enhanced during fruit ripening
-
-
?
9,9'-dicis-zeta-carotene + 2 quinone
7,9,7',9'-tetracis-lycopene + 2 quinol
-
-
-
-
?
9,9'-dicis-zeta-carotene + 2 quinone
7,9,7',9'-tetracis-lycopene + 2 quinol
-
the expression of zeta-carotene desaturase paralleles plastid terminal oxidase (PTOX, quinol:oxygen oxidoreductase) and zeta-carotene desaturase. The three genes are expressed when carotinoid biosynthesis is enhanced during fruit ripening. Tomato ghost mutant with impaired plastid terminal oxidase accumulate phytoene in leaves and fruits
-
-
?
9,9'-dicis-zeta-carotene + a quinone
7,9,9'-tricis-neurosporene + a quinol
-
-
-
-
?
9,9'-dicis-zeta-carotene + a quinone
7,9,9'-tricis-neurosporene + a quinol
-
-
-
-
?
9,9'-dicis-zeta-carotene + a quinone
7,9,9'-tricis-neurosporene + a quinol
-
-
-
-
?
9,9'-dicis-zeta-carotene + a quinone
7,9,9'-tricis-neurosporene + a quinol
-
catalyzed by zeta-carotene desaturases CrtQa and CrtQb
-
-
?
phytoene + quinone
7,9,9'-tricis-neurosporene + quinol
-
via phytofluene and zeta-carotene
-
-
?
phytoene + quinone
7,9,9'-tricis-neurosporene + quinol
-
-
-
-
?
zeta-carotene + 2 AH2 + 2 O2
lycopene + 2 A + 4 H2O
-
-
-
?
additional information
?
-
-
the deduced protein possesses a dinucleotide-binding site at the N-terminus and a carotenoid-binding domain at the C-terminus
-
-
-
additional information
?
-
-
the deduced protein sequence possesses a dinucleotide-binding site at the N-terminus and a carotenoid-binding domain at the C-terminus
-
-
-
additional information
?
-
-
the deduced protein possesses a dinucleotide-binding site at the N-terminus and a carotenoid-binding domain at the C-terminus
-
-
-
additional information
?
-
-
the deduced protein sequence possesses a dinucleotide-binding site at the N-terminus and a carotenoid-binding domain at the C-terminus
-
-
-
additional information
?
-
-
strain PCC 7120 contains two completely unrelated zeta-carotene desaturases CrtQa and CrtQb, which differ in their preferred utilization of zeta-carotene Z isomers. CrtQa converts zeta-carotene isomers that are poorly metabolized by CrtQb and CrtQa still possesses the Z to E isomerase function of the ancestral desaturase CrtI. CrtQb is an enzyme with one molecule of tightly bound FAD and acts as a dehydrogenase transferring hydrogen to oxidized plastoquinone. CrtQb yields only trace amounts of 7,9-Z neurosporene and 7,9,7',9'-Z lycopene
-
-
-
additional information
?
-
-
zeta-carotene desaturase CrtQb converts (9Z)-zeta-carotene efficiently into (7Z,9Z)-neurosporene but stops at this stage without substantial lycopene formation. (all-E)-zeta-carotene cannot be converted by CrtQb. Similarly to (9Z)-zeta-carotene, the (all-E)-isomer is efficiently converted by CrtQa, substrate specificities, overview
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
zeta-carotene + 2 quinone
lycopene + 2 quinol
-
zeta-carotene desaturase has no preference for certain isomers. The nature of the isomers formed during catalysis depends strictly on the isomeric composition of the substrate. Different lycopene isomers are formed, including substantial amounts of the all-trans form, together with 7,7',9,9'-tetracis prolycopene via the corresponding neurosporene isomers
-
-
?
additional information
?
-
-
strain PCC 7120 contains two completely unrelated zeta-carotene desaturases CrtQa and CrtQb, which differ in their preferred utilization of zeta-carotene Z isomers. CrtQa converts zeta-carotene isomers that are poorly metabolized by CrtQb and CrtQa still possesses the Z to E isomerase function of the ancestral desaturase CrtI. CrtQb is an enzyme with one molecule of tightly bound FAD and acts as a dehydrogenase transferring hydrogen to oxidized plastoquinone. CrtQb yields only trace amounts of 7,9-Z neurosporene and 7,9,7',9'-Z lycopene
-
-
-
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
-
-
-
?
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
-
-
-
?
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
-
-
-
?
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
catalyzed by zeta-carotene desaturase CrtQa, very poorly by CrtQb
-
-
?
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
-
-
-
?
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
-
-
-
-
?
9,9'-dicis-zeta-carotene + 2 quinone
7,9,7',9'-tetracis-lycopene + 2 quinol
-
the expression of zeta-carotene desaturase paralleles plastid terminal oxidase (PTOX, quinol:oxygen oxidoreductase) and zeta-carotene desaturase. The three genes are expressed when carotinoid biosynthesis is enhanced during fruit ripening
-
-
?
9,9'-dicis-zeta-carotene + 2 quinone
7,9,7',9'-tetracis-lycopene + 2 quinol
-
-
-
-
?
9,9'-dicis-zeta-carotene + 2 quinone
7,9,7',9'-tetracis-lycopene + 2 quinol
-
the expression of zeta-carotene desaturase paralleles plastid terminal oxidase (PTOX, quinol:oxygen oxidoreductase) and zeta-carotene desaturase. The three genes are expressed when carotinoid biosynthesis is enhanced during fruit ripening. Tomato ghost mutant with impaired plastid terminal oxidase accumulate phytoene in leaves and fruits
-
-
?
9,9'-dicis-zeta-carotene + a quinone
7,9,9'-tricis-neurosporene + a quinol
-
-
-
-
?
9,9'-dicis-zeta-carotene + a quinone
7,9,9'-tricis-neurosporene + a quinol
-
-
-
-
?
9,9'-dicis-zeta-carotene + a quinone
7,9,9'-tricis-neurosporene + a quinol
-
-
-
-
?
9,9'-dicis-zeta-carotene + a quinone
7,9,9'-tricis-neurosporene + a quinol
-
catalyzed by zeta-carotene desaturases CrtQa and CrtQb
-
-
?
phytoene + quinone
7,9,9'-tricis-neurosporene + quinol
-
via phytofluene and zeta-carotene
-
-
?
phytoene + quinone
7,9,9'-tricis-neurosporene + quinol
-
-
-
-
?
zeta-carotene + 2 AH2 + 2 O2
lycopene + 2 A + 4 H2O
E0AE54
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
addition of the dinucleotides FAD, NADP+ or NAD+ alone or the latter in combination with ATP results in a negligible increase in zeta-carotene desaturase activity
-
quinone
-
the expression of zeta-carotene desaturase paralleles plastid terminal oxidase (PTOX, quinol:oxygen oxidoreductase) and zeta-carotene desaturase. The three genes are expressed when carotinoid biosynthesis is enhanced during fruit ripening. Tomato ghost mutant with impaired plastid terminal oxidase accumulate phytoene in leaves and fruits
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
decyl-plastoquinone
-
enhances zeta-carotene desaturase activity significantly and increases the ratio of lycopene to neurosporene among the reaction products. Quinones other than decyl-plastoquinone and decyl-ubiquinone do not stimulate
decyl-ubiquinone
-
enhances zeta-carotene desaturase activity significantly and increases the ratio of lycopene to neurosporene among the reaction products. Quinones other than decyl-plastoquinone and decyl-ubiquinone do not stimulate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0331
7,9,9'-tricis-neurosporene
-
pH 8.0, 28°C, recombinant wild-type enzyme
0.0417
7,9,9'-tricis-neurosporene
-
pH 8.0, 28°C, recombinant mutant L208P
0.0658
7,9,9'-tricis-neurosporene
-
pH 8.0, 28°C, recombinant mutant L208F
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
semi-quantitative RT-PCR tissue expression analysis
additional information
-
semi-quantitative RT-PCR tissue expression analysis
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
Zds is a nonsecretory and nonmembraneous protein
-
additional information
-
Zds is a nonsecretory and nonmembraneous protein
-
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
the deduced protein possesses a dinucleotide-binding site at the N-terminus and a carotenoid-binding domain at the C-terminus; the deduced protein sequence possesses a dinucleotide-binding site at the N-terminus and a carotenoid-binding domain at the C-terminus
additional information
-
the deduced protein possesses a dinucleotide-binding site at the N-terminus and a carotenoid-binding domain at the C-terminus; the deduced protein sequence possesses a dinucleotide-binding site at the N-terminus and a carotenoid-binding domain at the C-terminus
-
additional information
three-dimensional structure of Zds, comparative modeling, overview
additional information
-
three-dimensional structure of Zds, comparative modeling, overview
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crtI gene, construction of different mutation libraries used for screening for mutants which synthesize almost exclusively either neurosporene or lycopene, cloning n Escherichia coli strain DH5alpha
-
expression in Escherichia coli
gene crtQa, expressionin Escherichia coli, gene crtQb, expression of CrtQB in Escherichia coli strain JM101
-
gene ZDS, cotransformation of the Citrus unshiu carotinoid biosynthetic genes geranylgeranyl diphosphate synthase, i.e. GGPS, phytoene desaturase, i.e. PDS, zeta-carotene desaturase, i.e. ZDS, beta-carotene hydroxylase, i.e. CHX, and phytoene synthase, i.e. PSY, into Actinidia deliciosa var. deliciosa, kiwi, fruits using the micro-cross section technique for the Agrobacterium tumefaciens transfection system, method evaluation, overview
gene zds, DNA and amino acid sequence determination and analysis, a single copy gene located on chromosome LG3
-
gene zds, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene zds, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, suncloning in Escherichia coli strain DH5alpha
-
gene zds, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, semi-quantitative RT-PCR expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
5-chloro-3-methyl-4-nitro-1H-pyrazole induces Zds expression from early to midmaturation stages, overview
the expression of zeta-carotene desaturase paralles plastid terminal oxidase (PTOX, quinol:oxygen oxidoreductase) and zeta-carotene desaturase. The three genes are expressed when carotinoid biosynthesis is enhanced during fruit ripening
-
the expression of zeta-carotene desaturase paralles plastid terminal oxidase (PTOX, quinol:oxygen oxidoreductase) and zeta-carotene desaturase. The three genes are expressed when carotinoid biosynthesis is enhanced during fruit ripening. Tomato ghost mutant with impaired plastid terminal oxidase accumulate phytoene in leaves and fruits
-
the zds gene expression is upregulated in response to light
5-chloro-3-methyl-4-nitro-1H-pyrazole induces Zds expression from early to midmaturation stages, overview
-
5-chloro-3-methyl-4-nitro-1H-pyrazole induces Zds expression from early to midmaturation stages, overview
-
-
the zds gene expression is upregulated in response to light
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E508G
-
random mutagenesis, the mutation has little effect on the enzyme activity
F166I
-
random mutagenesis, a beneficial mutation that helps the conversion of product from neurosporene to lycopene
F220S
-
random mutagenesis, the mutation has little effect on the enzyme activity
H12Q
-
random mutagenesis, the mutation has little effect on the enzyme activity
L148H
-
random mutagenesis, the beneficial mutation is highly increasing the production of lycopene to over 80%
M402T
-
random mutagenesis, the mutation reduces the lycopene production rate
V68D
-
random mutagenesis, a beneficial mutation that helps the conversion of product from neurosporene to lycopene
L153P
-
naturally occuring mutation, which influences the secondary structure of the enzyme
L208F
-
naturally occuring mutation, which influences the secondary structure of the enzyme
L208P
-
naturally occuring mutation, which influences the secondary structure of the enzyme
L278P
-
naturally occuring mutation, which influences the secondary structure of the enzyme
L424P
-
naturally occuring mutation, which influences the secondary structure of the enzyme
P134L
-
naturally occuring mutation, which influences the secondary structure of the enzyme
L153P
-
naturally occuring mutation, which influences the secondary structure of the enzyme
-
L208F
-
naturally occuring mutation, which influences the secondary structure of the enzyme
-
L208P
-
naturally occuring mutation, which influences the secondary structure of the enzyme
-
P134L
-
naturally occuring mutation, which influences the secondary structure of the enzyme
-
additional information
additional information
ZDS is not a major target gene to increase carotenoid contents in kiwifruit, overview
additional information
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alteration of product specificity of Rhodobacter sphaeroides phytoene desaturase by directed evolution combining random mutagenesis and site-directed mutagenesis, DNA sequence determinations. Beneficial mutations increase the percent of lycopene production to 90%; introduction of stop mutations, M1, M2 and M3
additional information
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in mutant EP21, zeta-carotene and phytofluene, which are both early intermediates of the desaturation pathway and which are absent in the wild-type, are the main carotene products
additional information
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in mutant EP21, zeta-carotene and phytofluene, which are both early intermediates of the desaturation pathway and which are absent in the wild-type, are the main carotene products
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