Information on EC 1.21.3.8 - cannabidiolic acid synthase

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The expected taxonomic range for this enzyme is: Cannabis sativa

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EC NUMBER
COMMENTARY hide
1.21.3.8
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RECOMMENDED NAME
GeneOntology No.
cannabidiolic acid synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cannabigerolate + O2 = cannabidiolate + H2O2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cannabinoid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
cannabigerolate:oxygen oxidoreductase (cyclizing, cannabidiolate-forming)
Binds FAD covalently. Part of the cannabinoids biosynthetic pathway of the plant Cannabis sativa. The enzyme can also convert cannabinerolate to cannabidiolate with lower efficiency.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
cannabigerolate + O2
cannabidiolate + H2O2
show the reaction diagram
cannabinerolate + O2
cannabidiolate + H2O2
show the reaction diagram
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-
-
-
?
additional information
?
-
-
the enzyme does not require molecular oxygen for the production of cannabidiolate in the presence or absence of NADPH
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
the enzyme has a covalently bound flavin
additional information
-
the enzyme does not require any coenzyme like NAD+, NADP+, FAD, and FMN
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme does not require metal ions
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Hg2+
-
complete inhibition at 2 mM
additional information
-
EDTA has little influence on the enzyme activity at concentrations up to 5 mM
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.137
cannabigerolate
-
in 100 mM sodium citrate buffer (pH 5.0), at 30°C
0.206
cannabinerolate
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in 100 mM sodium citrate buffer (pH 5.0), at 30°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
cannabigerolate
-
in 100 mM sodium citrate buffer (pH 5.0), at 30°C
0.03
cannabinerolate
-
in 100 mM sodium citrate buffer (pH 5.0), at 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.175
-
enzyme from supernatant, in 100 mM sodium citrate buffer (pH 5.0), at 30°C
9
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after 519fold purification, in 100 mM sodium citrate buffer (pH 5.0), at 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 6
-
half-maximal activities at pH values around 4.0 and 6.0
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
-
isoelectric focusing
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58863
x * 58863, deduced from amino acid sequence
62000
x * 62000, SDS-PAGE
74000
-
1 * 74000, SDS-PAGE
75000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 58863, deduced from amino acid sequence; x * 62000, SDS-PAGE
monomer
-
1 * 74000, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 40% (v/v) glycerol, ineffective storage conditions for enzyme stabilization
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4°C, purified enzyme in 10 mM sodium phosphate buffer (pH 7.0), 3 mM beta-mercaptoethanol, 2 weeks, 10-20% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-cellulose column chromatography, phenyl-Sepharose CL-4B column chromatography, and hydroxylapatite column chromatography
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hydroxylapatite column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Sf9 insect cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H114A
inactive
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LINKS TO OTHER DATABASES (specific for EC-Number 1.21.3.8)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)