Information on EC 5.2.1.13 - prolycopene isomerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.2.1.13
-
RECOMMENDED NAME
GeneOntology No.
prolycopene isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
7,9,7',9'-tetracis-lycopene = all-trans-lycopene
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Carotenoid biosynthesis
-
-
Metabolic pathways
-
-
trans-lycopene biosynthesis II (plants)
-
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carotenoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
7,9,7',9'-tetracis-lycopene cis-trans-isomerase
Requires FADH2 [1]. The enzyme is involved in carotenoid biosynthesis.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
L. var. Nipponbare
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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
(5'Z)-gamma-carotene
(all-E)-gamma-carotene
show the reaction diagram
(5'Z)-rubixanthin
(all-E)-rubixanthin
show the reaction diagram
(5Z,9Z,5'Z,9'Z)-lycopene
(all-E)-lycopene
show the reaction diagram
7,9,7',9'-tetracis-lycopene
all-trans-lycopene
show the reaction diagram
-
-
-
?
7,9,7',9'-tetracis-lycopene
prolycopene
show the reaction diagram
-
-
all-trans-lycopene is the main lycopene species formed, accompanied by certain amounts of newly formed cis isomers
-
?
prolycopene
(all-E)-lycopene
show the reaction diagram
additional information
?
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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
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FADH2
-
requires the reduced cofactor for activity. The enzyme requires anaerobic conditions for activity. Km: 0.00055 mM
FMNH2
-
can substitute for FADH2, with about 60% loss effectivity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
the enzyme requires anaerobic conditions for activity
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 8
-
exhibits no pH-dependence in the range pH 5.8-8.0
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.24
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the transcript of Zmcrtiso1 increases throughout endosperm development to day 25 after pollination. Until 30 after pollination the level decreases
Manually annotated by BRENDA team
-
in wild-type fruit, the mRNA levels of CRTISO increase 10fold during the breaker stage of fruit ripening. Expression of CRTISO in fruit of the mutant tangerine(mic) is similar to that in the wild type
Manually annotated by BRENDA team
ZEBRA2 is predominantly expressed in mesophyll cells of mature leaves
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
63700
x * 63700, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 63700, calculated from sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene CoCRTISO1-ORa, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR analysis; gene CoCRTISO1-ORb, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR analysis; gene CoCRTISO1-Y, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR analysis; gene CoCRTISO2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR analysis; gene CoCRTISO3, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR analysis; gene CoCRTISO4, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, quantitative real-time PCR analysis
mutant enzyme tangerine3183
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in wild-type fruit, the mRNA levels of CRTISO increases 10fold during the breaker stage of fruit ripening. Expression of CRTISO in fruit of the mutant tangerine(mic) is similar to that in the wild type
-
the transcript of Zmcrtiso1 increases throughout endosperm development to day 25 after pollination. Until 30 after pollination the levels decreases
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A412S
site-directed mutagenesis, the mutant shows substrate specificity like the wild-type enzyme
G450E
site-directed mutagenesis, the isozyme CoCRTISO1-ORb mutant is catalytically inactive
I370T
site-directed mutagenesis, the isozyme CoCRTISO1-ORa mutant is catalytically inactive
L581P
site-directed mutagenesis, the isozyme CoCRTISO1-ORa mutant is catalytically inactive
P584L
site-directed mutagenesis, the mutant shows substrate specificity like the wild-type enzyme
S412A
site-directed mutagenesis, the isozyme CoCRTISO1-ORb mutant is catalytically inactive