1.14.12.12: naphthalene 1,2-dioxygenase
This is an abbreviated version!
For detailed information about naphthalene 1,2-dioxygenase, go to the full flat file.
Word Map on EC 1.14.12.12
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1.14.12.12
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putida
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polycyclic
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bioremediation
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rieske
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toluene
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phenanthrene
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dioxygenation
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naphthalene-degrading
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ring-hydroxylating
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dihydroxylation
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indigo
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pah-degrading
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hydrocarbon-degrading
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dihydrodiols
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cis-dihydrodiols
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rieske-type
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oil-contaminated
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cis-dihydroxylation
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parales
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2-nitrotoluene
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pah-contaminated
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acenaphthene
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cis-diols
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side-on
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alpha3beta3
-
indene
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synthesis
- 1.14.12.12
- putida
-
polycyclic
-
bioremediation
-
rieske
- toluene
- phenanthrene
-
dioxygenation
-
naphthalene-degrading
-
ring-hydroxylating
-
dihydroxylation
- indigo
-
pah-degrading
-
hydrocarbon-degrading
- dihydrodiols
- cis-dihydrodiols
-
rieske-type
-
oil-contaminated
-
cis-dihydroxylation
-
parales
- 2-nitrotoluene
-
pah-contaminated
- acenaphthene
-
cis-diols
-
side-on
-
alpha3beta3
- indene
- synthesis
Reaction
Synonyms
NAG, NAHA, nahAc, naphthalene 1,2-dioxygenase, naphthalene dioxygenase, naphthalene oxygenase, NDO, oxygenase, naphthalene di-
ECTree
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Cofactor
Cofactor on EC 1.14.12.12 - naphthalene 1,2-dioxygenase
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FAD
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component A, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD
FAD
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addition enhances ferredoxinNAP reductase activity with all in vitro electron-acceptors, e.g. cytochrome c, 2,6-dichlorophenolindophenol, Nitroblue tetrazolium and ferricyanide
FMN
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requirement, ferredoxinNAP reductase is a flavoprotein, enzyme can use both FAD and FMN but exhibits slightly higher affinity for FAD, addition stimulates dioxygenase activity by 53% of FAD-stimulation
NADH
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requirement, the oxygenase accepts two electrons from NADH, the reduction requires component A and C as mediators