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

for references in articles please use BRENDA:EC1.14.14.8
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)


The expected taxonomic range for this enzyme is: Geobacillus thermodenitrificans

top print hide
EC NUMBER
COMMENTARY hide
1.14.14.8
-
top print hide
RECOMMENDED NAME
GeneOntology No.
anthranilate 3-monooxygenase (FAD)
-
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
anthranilate + FADH2 + O2 = 3-hydroxyanthranilate + FAD + H2O
show the reaction diagram
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
anthranilate degradation IV (aerobic)
-
-
tryptophan metabolism
-
-
Tryptophan metabolism
-
-
top print hide
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.
top
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
top print hide
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
-
62.79% relative activity
-
-
?
2-hydroxyphenylacetate + FADH2 + O2
? + FAD + H2O
show the reaction diagram
4-hydroxyphenylacetate + FADH2 + O2
?
show the reaction diagram
-
42.7% relative activity
-
-
?
4-hydroxyphenylacetate + FADH2 + O2
? + FAD + H2O
show the reaction diagram
anthranilate + FADH2 + O2
3-hydroxyanthranilate + FAD
show the reaction diagram
-
highest activity
-
-
?
anthranilate + FADH2 + O2
3-hydroxyanthranilate + FAD + H2O
show the reaction diagram
salicylate + FADH2 + O2
?
show the reaction diagram
-
49% relative activity
-
-
?
salicylate + FADH2 + O2
? + FAD + H2O
show the reaction diagram
additional information
?
-
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FADH2
-
; FADH2-utilizing monooxygenase, no reaction with FMNH2
additional information
-
no cofactor: FMNH2
-
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
151.3
-
substrate anthranilate, pH 9.0, 60°C
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
-
; assay at, highest activity
top print hide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
; assay at, highest activity
top print hide
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
-
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli; expression in Escherichia coli
-
top print hide
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription level increases highly when anthranilate is used as the sole carbon source
top
top
top
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)