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

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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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; assay at, highest activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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; assay at, highest activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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