Information on EC 1.14.16.3 - anthranilate 3-monooxygenase

for references in articles please use BRENDA:EC1.14.16.3
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The expected taxonomic range for this enzyme is: Tecoma stans

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EC NUMBER
COMMENTARY hide
1.14.16.3
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RECOMMENDED NAME
GeneOntology No.
anthranilate 3-monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
anthranilate + tetrahydrobiopterin + O2 = 3-hydroxyanthranilate + dihydrobiopterin + H2O
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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redox reaction
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-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Tryptophan metabolism
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SYSTEMATIC NAME
IUBMB Comments
anthranilate,tetrahydrobiopterin:oxygen oxidoreductase (3-hydroxylating)
Requires Fe2+.
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CAS REGISTRY NUMBER
COMMENTARY hide
37256-79-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
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
anthranilate + tetrahydrofolic acid + O2
3-hydroxyanthranilate + dihydrofolic acid + H2O2
show the reaction diagram
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specific for anthranilate, the optimum concentration is 0.5 mM, tetrahydrofolic acid is the most active electron donor when tested alone
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?
additional information
?
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phenylalanine, benzoic acid, acetanilide, tryptophan, kynurenine and cinnamic acid do not serve as substrates
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
tetrahydrofolic acid
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absolute requirement
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
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activator, required for the reaction
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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74.2% inhibition at 0.5 mM
2,2'-dipyridyl
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97.4% inhibition, reversed by Fe3+
2,3-Dimercaptopropanol
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Ag+
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100% inhibition at 0.5 mM
aminopterin
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100% inhibition at 0.5 mM, 78.4% inhibition at 0.2 mM
anthranilic acid
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above 1 mM
Co2+
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62.4% inhibition at 0.5 mM
Cu2+
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77% inhibition at 0.5 mM
cysteine
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91.9% inhibition at 0.5 mM
EDTA
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64.6% inhibition
glutathione
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86.8% inhibition at 0.5 mM
Hg2+
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97% inhibition at 0.5 mM
iodoacetate
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57% inhibition at 0.5 mM
p-chloromercuribenzoate
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slight at 0.5 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
increases activity
NADPH
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increases activity
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.549
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-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.6 - 6.2
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about 50% of activity maximum at pH 3.6 and pH 6.2
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20�C, 1 month stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using fractional precipitation with acetone and adsorption on DEAE-cellulose
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.16.3)
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)