Information on EC 1.3.5.6 - 9,9'-dicis-zeta-carotene desaturase

Word Map on EC 1.3.5.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.3.5.6
-
RECOMMENDED NAME
GeneOntology No.
9,9'-dicis-zeta-carotene desaturase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7,9,9'-tricis-neurosporene + a quinone = 7,9,7',9'-tetracis-lycopene + a quinol
show the reaction diagram
-
-
-
-
9,9'-dicis-zeta-carotene + 2 quinone = 7,9,7',9'-tetracis-lycopene + 2 quinol
show the reaction diagram
-
-
-
-
9,9'-dicis-zeta-carotene + a quinone = 7,9,9'-tricis-neurosporene + a quinol
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Carotenoid biosynthesis
-
-
Metabolic pathways
-
-
carotenoid biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
9,9'-dicis-zeta-corotene:quinone oxidoreductase
This enzyme is involved in carotenoid biosynthesis in plants and cyanobacteria.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
red-fleshed variant, single copy gene zds; yellow-fleshed variant, single copy gene zds
-
-
Manually annotated by BRENDA team
red-fleshed variant, single copy gene zds; yellow-fleshed variant, single copy gene zds
-
-
Manually annotated by BRENDA team
gene zds
-
-
Manually annotated by BRENDA team
gene zds
-
-
Manually annotated by BRENDA team
gene zds
UniProt
Manually annotated by BRENDA team
gene zds
UniProt
Manually annotated by BRENDA team
gene zds
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
contains two completely unrelated zeta-carotene desaturases CrtQa and CrtQb, encoded by genes crtQa and crtQb
-
-
Manually annotated by BRENDA team
gene crtI
-
-
Manually annotated by BRENDA team
gene crtI
-
-
Manually annotated by BRENDA team
cv. Ailsa Craig
-
-
Manually annotated by BRENDA team
gene zds
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
show the reaction diagram
9,9'-dicis-zeta-carotene + 2 quinone
7,9,7',9'-tetracis-lycopene + 2 quinol
show the reaction diagram
9,9'-dicis-zeta-carotene + a quinone
7,9,9'-tricis-neurosporene + a quinol
show the reaction diagram
neurosporene + a quinone
lycopene + a quinol
show the reaction diagram
-
-
-
-
?
neurosporene + decyl-plastoquinone
lycopene + decyl-plastoquinol
show the reaction diagram
-
-
-
-
?
neurosporene + decyl-ubiquinone
lycopene + decyl-ubiquinone
show the reaction diagram
-
-
-
-
?
phytoene + quinone
7,9,9'-tricis-neurosporene + quinol
show the reaction diagram
zeta-carotene + 2 AH2 + 2 O2
lycopene + 2 A + 4 H2O
show the reaction diagram
zeta-carotene + 2 decyl-plastoquinone
lycopene + 2 decyl-plastoquinol
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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 + a quinone
neurosporene + a quinol
show the reaction diagram
-
-
-
-
?
zeta-carotene + AH2 + O2
neurosporene + A + H2O
show the reaction diagram
-
-
-
?
zeta-carotene + decyl-plastoquinone
neurosporene + decyl-plastoquinol
show the reaction diagram
-
-
-
-
?
zeta-carotene + decyl-ubiquinone
neurosporene + decyl-ubiquinone
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
7,9,9'-tricis-neurosporene + a quinone
7,9,7',9'-tetracis-lycopene + a quinol
show the reaction diagram
9,9'-dicis-zeta-carotene + 2 quinone
7,9,7',9'-tetracis-lycopene + 2 quinol
show the reaction diagram
9,9'-dicis-zeta-carotene + a quinone
7,9,9'-tricis-neurosporene + a quinol
show the reaction diagram
neurosporene + a quinone
lycopene + a quinol
show the reaction diagram
-
-
-
-
?
phytoene + quinone
7,9,9'-tricis-neurosporene + quinol
show the reaction diagram
zeta-carotene + 2 AH2 + 2 O2
lycopene + 2 A + 4 H2O
show the reaction diagram
zeta-carotene + 2 quinone
lycopene + 2 quinol
show the reaction diagram
-
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 + a quinone
neurosporene + a quinol
show the reaction diagram
-
-
-
-
?
zeta-carotene + AH2 + O2
neurosporene + A + H2O
show the reaction diagram
Q2PPX8
-
-
-
?
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
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
tightly bound to zeta-carotene desaturase CrtQb
quinone
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0331 - 0.0658
7,9,9'-tricis-neurosporene
0.009
Neurosporene
-
pH 7.8, 28°C
0.0048 - 0.0171
phytoene
0.0084
zeta-carotene
-
pH 7.8, 28°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60000
-
x * 60000, SDS-PAGE
63700
-
x * 63700, aboout, sequence calculation
63900
x * 63900, about, sequence calculation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
F166I
-
random mutagenesis, a beneficial mutation that helps the conversion of product from neurosporene to lycopene
-
H12Q
-
random mutagenesis, the mutation has little effect on the enzyme activity
-
V68D
-
random mutagenesis, a beneficial mutation that helps the conversion of product from neurosporene to lycopene
-
D355G
-
naturally occuring mutation
D53G
-
naturally occuring mutation
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
T256M
-
naturally occuring mutation
V395A
-
naturally occuring mutation
Y44C
-
naturally occuring mutation
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
Show AA Sequence (610 entries)
Please use the Sequence Search for a specific query.