Information on EC 1.14.14.8 - anthranilate 3-monooxygenase (FAD)

for references in articles please use BRENDA:EC1.14.14.8
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The expected taxonomic range for this enzyme is: Geobacillus thermodenitrificans

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EC NUMBER
COMMENTARY hide
1.14.14.8
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RECOMMENDED NAME
GeneOntology No.
anthranilate 3-monooxygenase (FAD)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
anthranilate + FADH2 + O2 = 3-hydroxyanthranilate + FAD + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
anthranilate degradation IV (aerobic)
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tryptophan metabolism
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Tryptophan metabolism
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SYSTEMATIC NAME
IUBMB Comments
anthranilate,FAD:oxygen oxidoreductase (3-hydroxylating)
This enzyme, isolated from the bacterium Geobacillus thermodenitrificans, participates in the pathway of tryptophan degradation. The enzyme is part of a system that also includes a bifunctional riboflavin kinase/FMN adenylyltransferase and an FAD reductase, which ensures ample supply of FAD to the monooxygenase.
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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
2-hydroxyphenylacetate + FADH2 + O2
?
show the reaction diagram
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62.79% relative activity
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?
2-hydroxyphenylacetate + FADH2 + O2
? + FAD + H2O
show the reaction diagram
4-hydroxyphenylacetate + FADH2 + O2
?
show the reaction diagram
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42.7% relative activity
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?
4-hydroxyphenylacetate + FADH2 + O2
? + FAD + H2O
show the reaction diagram
anthranilate + FADH2 + O2
3-hydroxyanthranilate + FAD
show the reaction diagram
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highest activity
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?
anthranilate + FADH2 + O2
3-hydroxyanthranilate + FAD + H2O
show the reaction diagram
salicylate + FADH2 + O2
?
show the reaction diagram
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49% relative activity
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?
salicylate + FADH2 + O2
? + FAD + H2O
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FADH2
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; FADH2-utilizing monooxygenase, no reaction with FMNH2
additional information
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no cofactor: FMNH2
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
151.3
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substrate anthranilate, pH 9.0, 60�C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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; assay at, highest activity
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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; assay at, highest activity
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli; expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription level increases highly when anthranilate is used as the sole carbon source
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.14.8)
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)