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
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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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Metals Ions
Metals Ions on EC 1.14.12.12 - naphthalene 1,2-dioxygenase
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Fe2+
Iron
additional information
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no significant activation by the addition of Fe2+, Fe3+, Zn2+, Mg2+ or Cu2+
Fe2+
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alpha subunit of terminal oxygenase ISPNAP contains a Rieske [2Fe-2S] center in one domain and a mono-nuclear iron in the catalytic domain
Fe2+
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component A, i.e. NADH-ferredoxinNAP reductase, of the multienzyme system is an iron-containing flavoprotein containing 1.8 g-atoms Fe2+ and 2 g-atoms sulfur
Fe2+
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component B, the terminal oxygenase ISPNAP is an iron-sulfur protein, oxidized ISPNAP binds naphthalene without conformational changes that affect its FeS-chromophores, ISPNAP contains 6 g-atom Fe2+ and 4 g-atom acid-labile sulfur per mol enzyme, the enzyme complex is not stimulated by exogenous Fe2+
Fe2+
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terminal dioxygenase ISPNAR may be a Rieske-type iron-sulfur protein containing 2.4 g-atoms of iron and 2.1 g-atoms of sulfur per alpha,beta subunit
Fe2+
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the iron content of the oxygenase component ht-PhnI varies between 1.73 and 2.55 Fe atoms per pair of subunits depending on preparation, preincubation of ht-PhnI with ferrous ions under reducing conditions prior to enzyme assay results in a marginal increase of activity, the iron content of the ferredoxin component ht-PhnA3 is estimated to be 1.5 mol/mol of ferredoxin
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in the presence of the aromatic substrate indole, nitric oxide is bound end-on to the active-site mononuclear iron of NDO
Iron
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a molecular oxygen species is bound to the mononuclear iron in a side-on fashion
Iron
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the catalytic ferrous site is primed for the O2 reaction when substrate is bound in the active site in the presence of the reduced Rieske site. These structural changes ensure that two electrons and the substrate are present before the binding and activation of O2, which avoids the uncontrolled formation and release of reactive oxygen species