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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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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.8 anthranilate 3-monooxygenase (FAD)
IUBMB Comments
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.
The enzyme appears in viruses and cellular organisms
showSynonyms
gtng_3160, fadh2-utilizing monooxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FADH2-utilizing monooxygenase
GTNG_3160
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
anthranilate + FADH2 + O2 = 3-hydroxyanthranilate + FAD + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
anthranilate degradation IV (aerobic)
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-hydroxyphenylacetate + FADH2 + O2
?
-
Substrates: 62.79% relative activity
Products: -
Products: -
?
4-hydroxyphenylacetate + FADH2 + O2
?
-
Substrates: 42.7% relative activity
Products: -
Products: -
?
anthranilate + FADH2 + O2
3-hydroxyanthranilate + FAD
-
Substrates: highest activity
Products: -
Products: -
?
salicylate + FADH2 + O2
?
-
Substrates: 49% relative activity
Products: -
Products: -
?
2-hydroxyphenylacetate + FADH2 + O2
? + FAD + H2O
-
Substrates: 67.8% of the activity with anthranilate
Products: -
Products: -
?
2-hydroxyphenylacetate + FADH2 + O2
? + FAD + H2O
-
Substrates: 67.8% of the activity with anthranilate
Products: -
Products: -
?
4-hydroxyphenylacetate + FADH2 + O2
? + FAD + H2O
-
Substrates: 42.7% of the activity with anthranilate
Products: -
Products: -
?
4-hydroxyphenylacetate + FADH2 + O2
? + FAD + H2O
-
Substrates: 42.7% of the activity with anthranilate
Products: -
Products: -
?
anthranilate + FADH2 + O2
3-hydroxyanthranilate + FAD + H2O
-
Substrates: -
Products: -
Products: -
?
anthranilate + FADH2 + O2
3-hydroxyanthranilate + FAD + H2O
-
Substrates: -
Products: -
Products: -
?
salicylate + FADH2 + O2
? + FAD + H2O
-
Substrates: 49.6% of the activity with anthranilate
Products: -
Products: -
?
salicylate + FADH2 + O2
? + FAD + H2O
-
Substrates: 49.6% of the activity with anthranilate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: kynurenine, phenol, 2-nitrobenzylic acid, chlorobenzene, naphthalene, naphthol, toluene or ethylbenzene
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: kynurenine, phenol, 2-nitrobenzylic acid, chlorobenzene, naphthalene, naphthol, toluene or ethylbenzene
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FADH2
-
FADH2-utilizing monooxygenase, no reaction with FMNH2
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HPAH_GEOTN
Geobacillus thermodenitrificans (strain NG80-2)
494
0
56164
Swiss-Prot
-
A0A2S6STT7_9PROT
483
0
54360
TrEMBL
-
A0A644UMQ4_9ZZZZ
503
0
55335
TrEMBL
other Location (Reliability: 3)
A0A2S6U561_9PROT
435
0
48300
TrEMBL
-
A0A1C0TYW9_9GAMM
481
0
54852
TrEMBL
-
A0A2S6R4A3_9PROT
496
0
55825
TrEMBL
-
A0A347WBL2_9PROT
483
0
54450
TrEMBL
-
A0A6J5GAL9_9BURK
493
0
55548
TrEMBL
-
A0A2S6QHF1_9PROT
504
0
56623
TrEMBL
-
A0A2S6Q7L0_9PROT
496
0
56280
TrEMBL
-
A0A2S6QDC8_9PROT
496
0
55481
TrEMBL
-
A0A2S6S4Q3_9PROT
483
0
54537
TrEMBL
-
A0A2P5VL78_9PROT
488
0
54968
TrEMBL
-
A0A2S6TDN4_9PROT
502
0
56492
TrEMBL
-
A0A2S6TZS8_9PROT
497
0
56298
TrEMBL
-
A0A2S6R535_9PROT
317
0
35304
TrEMBL
-
A0A2S6ULV6_9PROT
508
0
57310
TrEMBL
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription level increases highly when anthranilate is used as the sole carbon source
transcription level increases highly when anthranilate is used as the sole carbon source
-
transcription level increases highly when anthranilate is used as the sole carbon source
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, X.; Dong, Y.; Li, X.; Ren, Y.; Li, Y.; Wang, W.; Wang, L.; Feng, L.
Characterization of the anthranilate degradation pathway in Geobacillus thermodenitrificans NG80-2
Microbiology
156
589-595
2010
Geobacillus thermodenitrificans, Geobacillus thermodenitrificans NG80-2
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.14.8)
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Release 2023.1 (January 2023)
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