Information on EC 1.3.8.2 - 4,4'-diapophytoene desaturase (4,4'-diapolycopene-forming)

Word Map on EC 1.3.8.2
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 enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.8.2
-
RECOMMENDED NAME
GeneOntology No.
4,4'-diapophytoene desaturase (4,4'-diapolycopene-forming)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
15-cis-4,4'-diapophytoene + 4 FAD = all-trans-4,4'-diapolycopene + 4 FADH2
show the reaction diagram
overall reaction
-
-
-
15-cis-4,4'-diapophytoene + FAD = all-trans-4,4'-diapophytofluene + FADH2
show the reaction diagram
(1a)
-
-
-
all-trans-4,4'-diapo-zeta-carotene + FAD = all-trans-4,4'-diaponeurosporene + FADH2
show the reaction diagram
(1c)
-
-
-
all-trans-4,4'-diaponeurosporene + FAD = all-trans-4,4'-diapolycopene + FADH2
show the reaction diagram
(1d)
-
-
-
all-trans-4,4'-diapophytofluene + FAD = all-trans-4,4'-diapo-zeta-carotene + FADH2
show the reaction diagram
(1b)
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Carotenoid biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
15-cis-4,4'-diapophytoene:FAD oxidoreductase (4,4'-diapolycopene-forming)
The enzyme catalyses four successive dehydrogenations, resulting in production of 4,4'-diapolycopene. While the enzyme from Staphylococcus aureus was only shown to produce 4,4'-diaponeurosporene in vivo [4], it is able to catalyse the last reaction in vitro [5].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
dehydrosqualene synthase converts farnesyl diphosphate to dehydrosqualene, dehydrosqualene desaturase then converts dehydrosqualene to the yelllow carotenoid 4,4'-diaponeurosporene
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
15-cis-4,4'-diapophytoene + 3 FAD
all-trans-4,4'-diapolycopene + 3 FADH2
show the reaction diagram
-
-
-
?
15-cis-4,4'-diapophytoene + 3 FAD
all-trans-4,4'-diaponeurosporene + 3 FADH2
show the reaction diagram
15-cis-4,4'-diapophytoene + 4 FAD
all-trans-4,4'-diapolycopene + 4 FADH2
show the reaction diagram
15-cis-4,4'-diapophytoene + FAD
all-trans-4,4'-diapophytofluene + FADH2
show the reaction diagram
all-trans-4,4'-diapo-zeta-carotene + FAD
all-trans-4,4'-diaponeurosporene + FADH2
show the reaction diagram
all-trans-4,4'-diaponeurosporene + FAD
all-trans-4,4'-diapolycopene + FADH2
show the reaction diagram
all-trans-4,4'-diapophytofluene + FAD
all-trans-4,4'-diapo-zeta-carotene + FADH2
show the reaction diagram
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
15-cis-4,4'-diapophytoene + 3 FAD
all-trans-4,4'-diaponeurosporene + 3 FADH2
show the reaction diagram
-
the enzyme is involved in the C30 carotenoid pathway
-
-
?
15-cis-4,4'-diapophytoene + 4 FAD
all-trans-4,4'-diapolycopene + 4 FADH2
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Diphenylamine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.049
15-cis-4,4'-diapophytoene
-
pH and temperature not specified in the publication
0.04 - 0.245
all-trans-4,4'-diapo-zeta-carotene
0.01
all-trans-4,4'-diapophytofluene
-
pH and temperature not specified in the publication
0.039
FAD
-
pH 6.6, 30°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
Diphenylamine
Staphylococcus aureus
-
pH 6.6, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.005
-
pH and temperature not specified in the publication
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
it can be assumed that diapophytoene desaturase forms a complex in the membrane that keeps the substrate carotenoids bound until all three double bonds are introduced in the desaturation process
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
1 * 52000, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 52000, calculated from sequence
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
coexpression with dehydroqualene desarurase with dehydrosqualene synthase and induction of endogenous genes crtP and crtQ encoding mixed function oxidase and glycosyltransferase for production of glycosylated C30 carotenoic acid, overview; gene crtN, functional expression in Bacillus subtilis, coexpression with dehydroqualene synthase and induction of endogenous genes crtP and crtQ
-
expression in Escherichia coli
-
the carotenoid synthetic genes, crtM and crtN, derived from Staphylococcus aureus, are introduced into Bacillus subtilis, resulting in yellow pigmentation
-
Show AA Sequence (165 entries)
Please use the Sequence Search for a specific query.