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Information on EC 1.14.12.23 - nitroarene dioxygenase
for references in articles please use BRENDA:EC1.14.12.23
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor
1.14.12.23 nitroarene dioxygenase
IUBMB Comments
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 α3β3 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+.
The enzyme appears in viruses and cellular organisms
- 1.14.12.23
- naphthalene
- nitrite
- 2-nitrotoluene
-
dinitrotoluenes
- comamonas
- 3-methylcatechol
-
nitroaromatic
-
regiospecificity
- oxygenases
-
archetypal
- 2,6-dinitrotoluene
-
rieske
- anthranilate
-
burkholderia
-
1,2-dioxygenase
- acidovorax
-
three-component
-
chlorocatechol
-
ring-hydroxylating
-
ralstonia
-
dioxygenation
- 2-amino-4,6-dinitrotoluene
- 3,4-dichloronitrobenzene
- diaphorobacter
- ferredoxin
-
nonheme
showSynonyms
2ntdo, nitroarene dioxygenase, mntab, nbzac, nbzad, cnbaa, cnbab, cnbac, cnbad, mntac, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cnbA
-
-
-
-
naphthalene dioxygenase
nbzAc
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nitrobenzene + NADH + O2 = catechol + nitrite + NAD+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
1-chloro-2-nitrobenzene degradation, 2,6-dinitrotoluene degradation, 2-nitrotoluene degradation, nitrobenzene degradation II
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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+.
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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
1,3-dinitrobenzene + NADH + O2
4-nitrocatechol + nitrite + NAD+
Substrates: -
Products: 100% yield. 89% of the activity with ntrobenzene
Products: 100% yield. 89% of the activity with ntrobenzene
?
2,4-dinitrotoluene + NADH + O2
4-methyl-5-nitrocatechol + nitrite + NAD+
Substrates: -
Products: products are 4-methyl-5-nitrocatechol + 25% 4-methyl-3-nitrocatechol
Products: products are 4-methyl-5-nitrocatechol + 25% 4-methyl-3-nitrocatechol
?
2-nitrotoluene + NADH + O2
4-methylcatechol + nitrite + NAD+
Substrates: -
Products: 100% yield. 221% of the activity with ntrobenzene
Products: 100% yield. 221% of the activity with ntrobenzene
?
3-nitrotoluene + NADH + O2
3-methylcatechol + 4-methylcatechol + nitrite + NAD+
M9PTH9; M9PW10; M9PSS0; M9PV03
Substrates: -
Products: products are 54% 3-methylcatechol, 39% 4-methylcatechol, 7% 3-nitrobenzyl alcohol
Products: products are 54% 3-methylcatechol, 39% 4-methylcatechol, 7% 3-nitrobenzyl alcohol
?
naphthalene + NADH + O2
1,2-dihydronaphthalene cis-1,2-diol + NAD+
Substrates: -
Products: 100% yield. 59% of the activity with ntrobenzene
Products: 100% yield. 59% of the activity with ntrobenzene
?
naphthalene + NADH + O2
cis-1,2-dihydroxy-1,2-dihydronaphthalene + NAD+
Substrates: -
Products: about 60% (-)-cis-1,2-dihydroxy-1,2-dihydronaphthalene
Products: about 60% (-)-cis-1,2-dihydroxy-1,2-dihydronaphthalene
?
naphthalene + O2
cis-1,2-dihydroxy-1,2-dihydronaphthalene
-
Substrates: -
Products: formation of 0.75 nmol 3-methylcatechol per mg protein
Products: formation of 0.75 nmol 3-methylcatechol per mg protein
?
2,3-dinitrotoluene + NADH + O2
4-methyl-3-nitrocatechol + nitrite + NAD+
-
Substrates: no substrate for wild-type, but substrate of mutant F350T
Products: -
Products: -
?
2,3-dinitrotoluene + NADH + O2
4-methyl-3-nitrocatechol + nitrite + NAD+
-
Substrates: no substrate for wild-type, but substrate of mutant F350T
Products: -
Products: -
?
2,6-dinitrotoluene + NADH + O2
3-methyl-4-nitrocatechol + nitrite + NAD+
Substrates: -
Products: -
Products: -
?
2,6-dinitrotoluene + NADH + O2
3-methyl-4-nitrocatechol + nitrite + NAD+
M9PTH9; M9PW10; M9PSS0; M9PV03
Substrates: -
Products: 84% of the activity with 3-nitrotoluene
Products: 84% of the activity with 3-nitrotoluene
?
2,6-dinitrotoluene + NADH + O2
3-methyl-4-nitrocatechol + nitrite + NAD+
-
Substrates: no substrate for wild-type, but substrate of mutant F350T
Products: -
Products: -
?
2,6-dinitrotoluene + NADH + O2
3-methyl-4-nitrocatechol + nitrite + NAD+
-
Substrates: no substrate for wild-type, but substrate of mutant F350T
Products: -
Products: -
?
2-amino-4,6-dinitrotoluene + NADH + O2
3-amino-4-methyl-5-nitrocatechol + nitrite + NAD+
-
Substrates: no substrate for wild-type, but substrate of mutant F350T
Products: plus 2-amino-4,6-dinitrobenzyl alcohol
Products: plus 2-amino-4,6-dinitrobenzyl alcohol
?
2-amino-4,6-dinitrotoluene + NADH + O2
3-amino-4-methyl-5-nitrocatechol + nitrite + NAD+
-
Substrates: no substrate for wild-type, but substrate of mutant F350T
Products: plus 2-amino-4,6-dinitrobenzyl alcohol
Products: plus 2-amino-4,6-dinitrobenzyl alcohol
?
2-chloronitrobenzene + NADH + O2
3-chlorocatechol + nitrite + NAD+
M9PTH9; M9PW10; M9PSS0; M9PV03
Substrates: -
Products: 80% of the activity with 3-nitrotoluene
Products: 80% of the activity with 3-nitrotoluene
?
2-chloronitrobenzene + NADH + O2
3-chlorocatechol + nitrite + NAD+
Pseudomonas stutzeri ZWLR2-1
F4Y9I5; F4Y9I4; F4Y9J0; F4Y9J1
Substrates: -
Products: -
Products: -
?
2-nitrotoluene + NADH + O2
3-methylcatechol + nitrite + NAD+
-
Substrates: -
Products: -
Products: -
?
2-nitrotoluene + NADH + O2
3-methylcatechol + nitrite + NAD+
-
Substrates: -
Products: -
Products: -
?
2-nitrotoluene + NADH + O2
3-methylcatechol + nitrite + NAD+
Substrates: -
Products: 55% yield, plus 45% 2-nitrobenzyl alcohol. 59% of the activity with ntrobenzene
Products: 55% yield, plus 45% 2-nitrobenzyl alcohol. 59% of the activity with ntrobenzene
?
2-nitrotoluene + NADH + O2
3-methylcatechol + nitrite + NAD+
M9PTH9; M9PW10; M9PSS0; M9PV03
Substrates: -
Products: 71% of the activity with 3-nitrotoluene. Products are 91% 3-methylcatechol, 9% 3-nitrobenzyl alcohol
Products: 71% of the activity with 3-nitrotoluene. Products are 91% 3-methylcatechol, 9% 3-nitrobenzyl alcohol
?
2-nitrotoluene + NADH + O2
3-methylcatechol + nitrite + NAD+
-
Substrates: -
Products: formation of 10 nmol 3-methylcatechol per mg protein plus 1.06 nmol 2-nitrobenzyl alcohol
Products: formation of 10 nmol 3-methylcatechol per mg protein plus 1.06 nmol 2-nitrobenzyl alcohol
?
3-nitrotoluene + NADH + O2
3-methylcatechol + nitrite + NAD+
-
Substrates: -
Products: products are 72% 3-methylcatechol, 25% 4-methylcatechol and 4% 3-nitrobenzyl alcohol
Products: products are 72% 3-methylcatechol, 25% 4-methylcatechol and 4% 3-nitrobenzyl alcohol
?
3-nitrotoluene + NADH + O2
3-methylcatechol + nitrite + NAD+
-
Substrates: -
Products: products are 72% 3-methylcatechol, 25% 4-methylcatechol and 4% 3-nitrobenzyl alcohol
Products: products are 72% 3-methylcatechol, 25% 4-methylcatechol and 4% 3-nitrobenzyl alcohol
?
3-nitrotoluene + NADH + O2
4-methylcatechol + nitrite + NAD+
-
Substrates: -
Products: sole product
Products: sole product
?
3-nitrotoluene + NADH + O2
4-methylcatechol + nitrite + NAD+
-
Substrates: -
Products: sole product
Products: sole product
?
3-nitrotoluene + NADH + O2
4-methylcatechol + nitrite + NAD+
-
Substrates: -
Products: formation of 0.06 nmol 4-methylcatechol per mg protein plus 0.03 nmol 3-nitrobenzyl alcohol
Products: formation of 0.06 nmol 4-methylcatechol per mg protein plus 0.03 nmol 3-nitrobenzyl alcohol
?
4-nitrotoluene + NADH + O2
4-methylcatechol + nitrite + NAD+
-
Substrates: -
Products: -
Products: -
?
4-nitrotoluene + NADH + O2
4-methylcatechol + nitrite + NAD+
-
Substrates: -
Products: -
Products: -
?
4-nitrotoluene + NADH + O2
4-methylcatechol + nitrite + NAD+
Substrates: -
Products: 85% yield, plus 15% 4-nitrobenzyl alcohol. 42% of the activity with ntrobenzene
Products: 85% yield, plus 15% 4-nitrobenzyl alcohol. 42% of the activity with ntrobenzene
?
nitrobenzene + NADH + O2
catechol + nitrite + NAD+
-
Substrates: -
Products: -
Products: -
?
nitrobenzene + NADH + O2
catechol + nitrite + NAD+
-
Substrates: -
Products: reaction of EC 1.14.12.23
Products: reaction of EC 1.14.12.23
?
nitrobenzene + NADH + O2
catechol + nitrite + NAD+
Substrates: -
Products: -
Products: -
?
nitrobenzene + NADH + O2
catechol + nitrite + NAD+
Substrates: -
Products: 100% yield
Products: 100% yield
?
nitrobenzene + NADH + O2
catechol + nitrite + NAD+
M9PTH9; M9PW10; M9PSS0; M9PV03
Substrates: -
Products: 78% of the activity with 3-nitrotoluene
Products: 78% of the activity with 3-nitrotoluene
?
additional information
?
-
-
Substrates: all three mononitrotoluene isomers serve as substrates for 2-nitrotoluene dioxygenase, but strain JS42 is unable to grow on 3- or 4-nitrotoluene
Products: -
Products: -
?
additional information
?
-
-
Substrates: all three mononitrotoluene isomers serve as substrates for 2-nitrotoluene dioxygenase, but strain JS42 is unable to grow on 3- or 4-nitrotoluene
Products: -
Products: -
?
additional information
?
-
Substrates: a nitro-substituted position is generally the preferred, but not exclusive, oxidation site. All of the nitrotoluene and dinitrotoluene isomers tested are transformed. Oxidation at the 3,4 position of the ring, with respect to the methyl substituent, appears to be favored. The nitro substituent appears to contribute significantly to specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: a nitro-substituted position is generally the preferred, but not exclusive, oxidation site. All of the nitrotoluene and dinitrotoluene isomers tested are transformed. Oxidation at the 3,4 position of the ring, with respect to the methyl substituent, appears to be favored. The nitro substituent appears to contribute significantly to specificity
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: 2,4-dinitrotoluene
Products: -
Products: -
?
additional information
?
-
-
Substrates: wild-type enzyme catalyzes dioxygenation of naphthalen, reaction of EC 1.14.12.12
Products: -
Products: -
?
additional information
?
-
-
Substrates: wild-type enzyme catalyzes dioxygenation of naphthalen, reaction of EC 1.14.12.12
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
0.5 mol of NADH is required to reduce each alphabeta heterodimer of oxygenase
[2Fe-2S]-center
-
presence of a Rieske [2Fe-2S] cluster in the oxygenase component
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
M9PTH9 i.e. ferredoxin reductase subunit MntAa, M9PW10 i.e. oxygenase alpha subunit MntAc, M9PSS0 i.e. ferredoxin subunit MntAb, M9PV03 i.e. oxygenase beta subunit MntAd
M9PTH9; M9PW10; M9PSS0; M9PV03
UniProt
brenda
Pseudomonas stutzeri ZWLR2-1
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; F4Y9I4; F4Y9J0; F4Y9J1
UniProt
brenda
P95561 i.e.subunit nbzAa, reductase NBDR, Q8RTL5 i.e. ferredoxin, subunit nbzAb, Q8RTL4 i.e. oxygenase alpha-subunit nbzAc, NBDO, Q8RTL3 i.e. oxygenase beta-subunit nbzAd, NBDO
UniProt
brenda
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.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
Acidovorax sp. strain JS42 uses 2-nitrotoluene as a sole source of carbon and energy. The first enzyme of the degradation pathway, 2-nitrotoluene 2,3-dioxygenase, adds both atoms of molecular oxygen to 2-nitrotoluene, forming nitrite and 3-methylcatechol
physiological function
Pseudomonas stutzeri ZWLR2-1
F4Y9I5; F4Y9I4; F4Y9J0; 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
physiological function
-
Acidovorax sp. strain JS42 uses 2-nitrotoluene as a sole source of carbon and energy. The first enzyme of the degradation pathway, 2-nitrotoluene 2,3-dioxygenase, adds both atoms of molecular oxygen to 2-nitrotoluene, forming nitrite and 3-methylcatechol
-
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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). Q8RTL3_9BURK
194
0
23086
TrEMBL
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25300
-
3 * 51200, alpha-subunit, 3 * 25300, beta-subunit, SDS-PAGE of oxygenase component
25500
-
3 * 50400, alpha-subunit, 3 * 25500, beta-subunit, SDS-PAGE of oxygenase component
50400
-
3 * 50400, alpha-subunit, 3 * 25500, beta-subunit, SDS-PAGE of oxygenase component
51200
-
3 * 51200, alpha-subunit, 3 * 25300, beta-subunit, SDS-PAGE of oxygenase component
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
hexamer
-
3 * 50400, alpha-subunit, 3 * 25500, beta-subunit, SDS-PAGE of oxygenase component
hexamer
-
3 * 51200, alpha-subunit, 3 * 25300, beta-subunit, SDS-PAGE of oxygenase component
hexamer
-
3 * 50400, alpha-subunit, 3 * 25500, beta-subunit, SDS-PAGE of oxygenase component
-
hexamer
-
3 * 51200, alpha-subunit, 3 * 25300, beta-subunit, SDS-PAGE of oxygenase component
-
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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
-
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A405G
-
synthesizes 17% 3-methylcatechol, 83% 4-methylcatechol from substrate 3-nitrotoluene
I204A
-
synthesizes 2% 3-methylcatechol, 97% 4-methylcatechol and 1% 3-nitrobenzyl alcohol from substrate 3-nitrotoluene
I204T
-
synthesizes 5% 3-methylcatechol, 93% 4-methylcatechol and 2% 3-nitrobenzyl alcohol from substrate 3-nitrotoluene
I204V
-
synthesizes 13% 3-methylcatechol, 83% 4-methylcatechol and 5% 3-nitrobenzyl alcohol from substrate 3-nitrotoluene
A405G
-
synthesizes 17% 3-methylcatechol, 83% 4-methylcatechol from substrate 3-nitrotoluene
-
I204A
-
synthesizes 2% 3-methylcatechol, 97% 4-methylcatechol and 1% 3-nitrobenzyl alcohol from substrate 3-nitrotoluene
-
I204T
-
synthesizes 5% 3-methylcatechol, 93% 4-methylcatechol and 2% 3-nitrobenzyl alcohol from substrate 3-nitrotoluene
-
I204V
-
synthesizes 13% 3-methylcatechol, 83% 4-methylcatechol and 5% 3-nitrobenzyl alcohol from substrate 3-nitrotoluene
-
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
F350T
-
contrary to wild-type, mutant produces 3-methyl-4-nitrocatechol from 2,6-dinitrotoluene and 3-amino-4-methyl-5-nitrocatechol and 2-amino-4,6-dinitrobenzyl alcohol from 2-amino-4,6-dinitrotoluene, and mutant releases nitrite from 2,3-dinitrotoluene sixfold faster than wild-type
F350T/G407S
-
double mutant increases the rate of oxidation of 2,3-dinitrotoluene, 2,6-dinitrotoluene , and 2-amino-4,6-dinitrotoluene threefold relative to variant F350T
G50S/L225R/A269T
-
mutant displays increased rate of 4-amino-2-nitrotoluene oxidation and additionally produces oxidation product 4-amino-2-nitrocresol (enhanced 11fold relative to wild-type) as well as 4-amino-2-nitrobenzyl alcohol
L225R
-
12fold faster generation of 4-amino-2-nitrocresol and production of 4-amino-2-nitrobenzyl alcohol from 4-amino-2-nitrotoluene as well as 24fold faster generation of nitrite and 15fold faster generation of 2,3-dinitrobenzyl alcohol from 2,3-dinitrotoluene
F350T
-
contrary to wild-type, mutant produces 3-methyl-4-nitrocatechol from 2,6-dinitrotoluene and 3-amino-4-methyl-5-nitrocatechol and 2-amino-4,6-dinitrobenzyl alcohol from 2-amino-4,6-dinitrotoluene, and mutant releases nitrite from 2,3-dinitrotoluene sixfold faster than wild-type
-
F350T/G407S
-
double mutant increases the rate of oxidation of 2,3-dinitrotoluene, 2,6-dinitrotoluene , and 2-amino-4,6-dinitrotoluene threefold relative to variant F350T
-
G50S/L225R/A269T
-
mutant displays increased rate of 4-amino-2-nitrotoluene oxidation and additionally produces oxidation product 4-amino-2-nitrocresol (enhanced 11fold relative to wild-type) as well as 4-amino-2-nitrobenzyl alcohol
-
L225R
-
12fold faster generation of 4-amino-2-nitrocresol and production of 4-amino-2-nitrobenzyl alcohol from 4-amino-2-nitrotoluene as well as 24fold faster generation of nitrite and 15fold faster generation of 2,3-dinitrobenzyl alcohol from 2,3-dinitrotoluene
-
additional information
additional information
M9PTH9; M9PW10; M9PSS0; M9PV03
individual expression of each subunit and separate purification. The active recombinant enzyme can be reconstituted in vitro by mixing all three purified subunits
additional information
-
construction of hybrid dioxygenases with the genes encoding 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 and 2,4-dinitrotoluene dioxygenase from Burkholderia sp. strain DNT. The C-terminal region of the large subunit of the oxygenase component is responsible for the enzyme specificity differences observed between 2-nitrotoluene 2,3-dioxygenase and 2,4-dinitrotoluene dioxygenase
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lessner, D.; Johnson, G.; Parales, R.; Spain, J.; Gibson, D.
Molecular characterization and substrate specificity of nitrobenzene dioxygenase from Comamonas sp. strain JS765
Appl. Environ. Microbiol.
68
634-641
2002
Comamonas sp. (P95561 and Q8RTL5 and Q8RTL4 and Q8RTL3), Comamonas sp.
brenda
Parales, R.; Huang, R.; Yu, C.; Parales, J.; Lee, F.; Lessner, D.; Ivkovic-Jensen, M.; Liu, W.; Friemann, R.; Ramaswamy, S.; Gibson, D.
Purification, characterization, and crystallization of the components of the nitrobenzene and 2-nitrotoluene dioxygenase enzyme systems
Appl. Environ. Microbiol.
71
3806-3814
2005
Acidovorax sp., Acidovorax sp. JS42
brenda
Ju, K.S.; Parales, R.E.
Control of substrate specificity by active-site residues in nitrobenzene dioxygenase
Appl. Environ. Microbiol.
72
1817-1824
2006
Comamonas sp. (Q8RTL4)
brenda
Liu, H.; Wang, S.J.; Zhang, J.J.; Dai, H.; Tang, H.; Zhou, N.Y.
Patchwork assembly of nag-like nitroarene dioxygenase genes and the 3-chlorocatechol degradation cluster for evolution of the 2-chloronitrobenzene catabolism pathway in Pseudomonas stutzeri ZWLR2-1
Appl. Environ. Microbiol.
77
4547-4552
2011
Pseudomonas stutzeri ZWLR2-1 (F4Y9I5 and F4Y9I4 and F4Y9J0 and F4Y9J1)
brenda
Mahan, K.M.; Penrod, J.T.; Ju, K.S.; Al Kass, N.; Tan, W.A.; Truong, R.; Parales, J.V.; Parales, R.E.
Selection for growth on 3-nitrotoluene by 2-nitrotoluene-utilizing Acidovorax sp. strain JS42 identifies nitroarene dioxygenases with altered specificities
Appl. Environ. Microbiol.
81
309-319
2015
Acidovorax sp., Acidovorax sp. JS42
brenda
Singh, D.; Kumari, A.; Ramaswamy, S.; Ramanathan, G.
Expression, purification and substrate specificities of 3-nitrotoluene dioxygenase from Diaphorobacter sp. strain DS2
Biochem. Biophys. Res. Commun.
445
36-42
2014
Diaphorobacter sp. DS2 (M9PTH9 and M9PW10 and M9PSS0 and M9PV03)
brenda
Parales, J.; Parales, R.; Resnick, S.; Gibson, D.
Enzyme specificity of 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 is determined by the C-terminal region of the alpha-subunit of the oxygenase component
J. Bacteriol.
180
1194-1199
1998
Pseudomonas sp.
brenda
Keenan, B.G.; Leungsakul, T.; Smets, B.F.; Mori, M.A.; Henderson, D.E.; Wood, T.K.
Protein engineering of the archetypal nitroarene dioxygenase of Ralstonia sp. strain U2 for activity on aminonitrotoluenes and dinitrotoluenes through alpha-subunit residues leucine 225, phenylalanine 350, and glycine 407
J. Bacteriol.
187
3302-3310
2005
Ralstonia sp., Ralstonia sp. U2
brenda
Friemann, R.; Ivkovic-Jensen, M.M.; Lessner, D.J.; Yu, C.L.; Gibson, D.T.; Parales, R.E.; Eklund, H.; Ramaswamy, S.
Structural insight into the dioxygenation of nitroarene compounds: the crystal structure of nitrobenzene dioxygenase
J. Mol. Biol.
348
1139-1151
2005
Comamonas sp. (Q8RTL3), Comamonas sp. JS7650 (Q8RTL3)
brenda
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Release 2023.1 (January 2023)
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