Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.12.23 - nitroarene dioxygenase

for references in articles please use BRENDA:EC1.14.12.23
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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 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+.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: Q8RTL4
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
2ntdo, nitroarene dioxygenase, mntab, nbzab, nbzac, nbzad, cnbaa, cnbab, cnbac, cnbad, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cnbA
-
-
-
-
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+.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-dinitrotoluene + NADH + O2
4-methyl-5-nitrocatechol + nitrite + NAD+
show the reaction diagram
-
products are 4-methyl-5-nitrocatechol + 25% 4-methyl-3-nitrocatechol
-
?
2,6-dinitrotoluene + NADH + O2
3-methyl-4-nitrocatechol + nitrite + NAD+
show the reaction diagram
-
-
-
?
naphthalene + NADH + O2
cis-1,2-dihydroxy-1,2-dihydronaphthalene + NAD+
show the reaction diagram
-
about 60% (-)-cis-1,2-dihydroxy-1,2-dihydronaphthalene
-
?
nitrobenzene + NADH + O2
catechol + nitrite + NAD+
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012 - 0.851
2,6-dinitrotoluene
0.0077 - 1.78
nitrobenzene
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
oxygenase alpha-subunit
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8RTL4_9BURK
447
0
49557
TrEMBL
-
PROTEIN VARIANTS
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team