Information on EC 1.14.13.14 - trans-cinnamate 2-monooxygenase

for references in articles please use BRENDA:EC1.14.13.14
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The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
1.14.13.14
-
top print hide
RECOMMENDED NAME
GeneOntology No.
trans-cinnamate 2-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
trans-cinnamate + NADPH + H+ + O2 = 2-hydroxycinnamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
coumarin biosynthesis (via 2-coumarate)
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Phenylalanine metabolism
-
-
Phenylpropanoid biosynthesis
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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-
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SYSTEMATIC NAME
IUBMB Comments
trans-cinnamate,NADPH:oxygen oxidoreductase (2-hydroxylating)
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CAS REGISTRY NUMBER
COMMENTARY hide
53126-56-0
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cucumber
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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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
trans-cinnamate + NADPH + O2
2-hydroxycinnamate + NADP+ + H2O
show the reaction diagram
top print hide
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
trans-cinnamate + NADPH + O2
2-hydroxycinnamate + NADP+ + H2O
show the reaction diagram
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
less effective than NADPH
NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KCN
-
70% inhibition at 10 mM
Triton X-100
-
concentration higher than 0.5% deactivates the enzyme
additional information
-
UV-light treatment for 200 min leads to 30% inhibition
-
top print hide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glucose 6-phosphate
-
400% activation at 4 mM
sulfonic acid
-
700% activation at 0.003%
Triton X-100
-
700% activation at 0.025%
additional information
-
white light treatment for 200 min leads to 50% activation
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0004
-
supernatant activity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
predominantly, chloroplast membrane
Manually annotated by BRENDA team
-
lamellar, 50% of the hydroxylase activity
Manually annotated by BRENDA team
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.13.14)
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)