Information on EC 1.14.12.23 - nitroarene dioxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.12.23
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RECOMMENDED NAME
GeneOntology No.
nitroarene dioxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
nitrobenzene + NADH + O2 = catechol + nitrite + NAD+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1-chloro-2-nitrobenzene degradation
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2,6-dinitrotoluene degradation
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2-nitrotoluene degradation
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nitrobenzene degradation II
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Aminobenzoate degradation
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
nitrobenzene,NADH:oxygen oxidoreductase (1,2-hydroxylating, denitrifying)
This enzyme is a member of the naphthalene family of bacterial Rieske non-heme iron dioxygenases. It comprises a multicomponent system, containing a Rieske [2Fe-2S] ferredoxin, an NADH-dependent flavoprotein reductase (EC 1.18.1.3, ferredoxin---NAD+ reductase), and an alpha3beta3 oxygenase. The enzyme forms of a cis-dihydroxylated product that spontaneously rearranges to form a catechol with accompanying release of nitrite. It can typically act on many different nitroaromatic compounds, including chlorinated species. Enzymes found in different strains may have different substrate preferences. Requires Fe2+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
beta-subunit of oxidase
UniProt
Manually annotated by BRENDA team
F4Y9I5 i.e. ferredoxin reductase cnbAa, F4Y9I4 i.e. ferredoxin cnbAb, F4Y9J0 i.e. 2-chloronitrobenzene dioxygenase alpha subunit cnbAc, F4Y9J1 i.e. 2-chloronitrobenzene dioxygenase beta subunit cnbAd
F4Y9I5 and F4Y9I4 and F4Y9J0 and F4Y9J1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
F4Y9I5 and F4Y9I4 and F4Y9J0 and F4Y9J1
Escherichia coli cells expressing dioxygenase genes cnbAaAbAcAd convert 2-chloronitrobenzene to 3-chlorocatechol with concomitant nitrite release. The cnbCDEF gene cluster, homologous to a 3-chlorocatechol degradation cluster in Sphingomonas sp. strain TFD44, probably contains all of the genes necessary for the conversion of 3-chlorocatechol to 3-oxoadipate
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-dinitrobenzene + NADH + O2
4-nitrocatechol + nitrite + NAD+
show the reaction diagram
P95561 and Q8RTL5 and Q8RTL4 and Q8RTL3
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100% yield. 89% of the activity with ntrobenzene
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?
2,4-dinitrotoluene nitrobenzene + NADH + O2
4-methyl-5-nitrocatechol + 4-methyl-3-nitrocatechol + nitrite + NAD+
show the reaction diagram
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products are 4-methyl-5-nitrocatechol + 25% 4-methyl-3-nitrocatechol
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?
2,6-dinitrotoluene + NADH + O2
3-methyl-4-nitrocatechol + nitrite + NAD+
show the reaction diagram
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?
2-chloronitrobenzene + NADH + O2
3-chlorocatechol + nitrite + NAD+
show the reaction diagram
F4Y9I5 and F4Y9I4 and F4Y9J0 and F4Y9J1
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?
2-nitrotoluene + NADH + O2
3-methylcatechol + nitrite + NAD+
show the reaction diagram
2-nitrotoluene + NADH + O2
4-methylcatechol + nitrite + NAD+
show the reaction diagram
P95561 and Q8RTL5 and Q8RTL4 and Q8RTL3
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100% yield. 221% of the activity with ntrobenzene
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?
3-nitrotoluene + NADH + O2
4-methylcatechol + nitrite + NAD+
show the reaction diagram
4-nitrotoluene + NADH + O2
4-methylcatechol + nitrite + NAD+
show the reaction diagram
naphthalene + NADH + O2
cis-1,2-dihydroxy-1,2-dihydronaphthalene + NAD+
show the reaction diagram
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about 60% (-)-cis-1,2-dihydroxy-1,2-dihydronaphthalene
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?
naphthalene + NADH + O2
naphthalene cis-1,2-diol + nitrite + NAD+
show the reaction diagram
P95561 and Q8RTL5 and Q8RTL4 and Q8RTL3
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100% yield. 59% of the activity with ntrobenzene
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?
nitrobenzene + NADH + O2
catechol + nitrite + NAD+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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0.5 mol of NADH is required to reduce each alphabeta heterodimer of oxygenase
[2Fe-2S]-center
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
active site of alpha subunit contains a mononuclear iron atom
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012 - 0.851
2,6-dinitrotoluene
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0.0137
2-nitrotoluene
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pH 6.8, 30C
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0.0042
3-nitrotoluene
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pH 6.8, 30C
0.0045 - 1.78
nitrobenzene
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16
2-nitrotoluene
Acidovorax sp.
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pH 6.8, 30C
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0.27
3-nitrotoluene
Acidovorax sp.
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pH 6.8, 30C
0.3
nitrobenzene
Acidovorax sp.
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pH 6.8, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12
2-nitrotoluene
Acidovorax sp.
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pH 6.8, 30C
206831
65
3-nitrotoluene
Acidovorax sp.
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pH 6.8, 30C
136150
67
nitrobenzene
Acidovorax sp.
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pH 6.8, 30C
21873
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
215900
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dynamic light scattering, oxygenase component
216000
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gel filtration, oxygenase component
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
oxygenase component, to 1.2 A resolution, hexagonal space group P63 with cell dimensions a = b = 121.6 A and c = 84.4 A
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native enzyme and in complex with nitrobenzene and 3-nitrotoluene, to 1.2 A, 1.55 A and 1.5 A resolution, respectively. Enzyme shows a mushroom-shaped alpha3beta3 hexamer. The catalytic subunit contains a Rieske iron-sulfur center and an active-site mononuclear iron atom. The substrate pocket contains an asparagine residue that forms a hydrogen bond to the nitro-group of the substrate, and orients the substrate in relation to the active-site mononuclear iron atom
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F293H
mutation in alpha-subunit of oxygenase, residue is important for determining regiospecificity with nitroarene substrates and enantiospecificity with naphthalene
F293I
mutation in alpha-subunit of oxygenase, residue is important for determining regiospecificity with nitroarene substrates and enantiospecificity with naphthalene
F293Q
mutation in alpha-subunit of oxygenase, residue is important for determining regiospecificity with nitroarene substrates and enantiospecificity with naphthalene. Mutant is 2.5 times faster than wild-type at oxidizing 2,6-dinitrotoluene while retaining a similar Km for the substrate
I350F
mutation in alpha-subunit of oxygenase, residue is important for determining regiospecificity with nitroarene substrates and enantiospecificity with naphthalene. Most mononitrotoluene oxidation products formed by the N258V mutant are nitrobenzyl alcohols rather than catechols
I350T
mutation in alpha-subunit of oxygenase, residue is important for determining regiospecificity with nitroarene substrates and enantiospecificity with naphthalene
N258V
mutation in alpha-subunit of oxygenase, residue is important for determining regiospecificity with nitroarene substrates and enantiospecificity with naphthalene. Up to 99% of the mononitrotoluene oxidation products formed by the N258V mutant are nitrobenzyl alcohols rather than catechols