Information on EC 1.7.1.B2 - aromatic nitroreductase [NAD(P)H]

for references in articles please use BRENDA:EC1.7.1.B2
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.7.1.B2
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
aromatic nitroreductase [NAD(P)H]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an aromatic amine + 3 NAD(P)+ + 2 H2O = an aromatic nitrate + 3 NAD(P)H + 3 H+
show the reaction diagram
in vivo the reaction is obseverved in the opposite direction from that shown in the equation; (overall reaction)
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an aromatic amine + NAD(P)+ + H2O = an aromatic hydroxylamine + NAD(P)H + H+
show the reaction diagram
(1a)
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an aromatic hydroxylamine + NAD(P)+ = an aromatic nitric oxide + NAD(P)H + H+
show the reaction diagram
(1b)
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an aromatic nitric oxide + NAD(P)+ + H2O = an aromatic nitrate + NAD(P)H + H+
show the reaction diagram
(1c)
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SYSTEMATIC NAME
IUBMB Comments
aromatic nitrate:NAD(P)H oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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nitroreductases are a family of flavoproteins that catalyze the NAD(P)H-dependent reduction of nitro groups to hydroxyamino and/or amino groups on vari-ous nitro-substituted compounds
physiological function
additional information
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the enzyme crystal structure of NfsB, PDB ID 1DS7, is used for molecular ligand docking studies
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4,6-trinitrotoluene + NADH + H+
4-hydroxyamino-2,6-dinitrotoluene + NAD+ + H2O
show the reaction diagram
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?
2,4,6-trinitrotoluene + NADPH + H+
4-hydroxyamino-2,6-dinitrotoluene + NADP+ + H2O
show the reaction diagram
2-amino-4,6-dinitrotoluene + NADH + H+
4-hydroxyamino-2-aminotoluene + NAD+ + H2O
show the reaction diagram
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?
4-amino-2,6-dinitrotoluene + NADH + H+
2-hydroxyamino-4-aminotoluene + NAD+ + H2O
show the reaction diagram
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?
5-(aziridin-1-yl)-2,4-dinitrobenzamide + NAD(P)H + H+
? + NAD(P)+
show the reaction diagram
nitro-CBI-5-[(dimethylamino)ethoxy]indole + NAD(P)H + H+
? + NAD(P)+
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,4,6-trinitrotoluene + NADH + H+
4-hydroxyamino-2,6-dinitrotoluene + NAD+ + H2O
show the reaction diagram
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?
2,4,6-trinitrotoluene + NADPH + H+
4-hydroxyamino-2,6-dinitrotoluene + NADP+ + H2O
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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NfsB is capable of utilizing bothNADH and NADPH as cofactor
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0023 - 0.0997
2,4,6-trinitrotoluene
0.0398 - 1.495
2-amino-4,6-dinitrotoluene
0.172 - 1.168
4-amino-2,6-dinitrotoluene
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additional information
additional information
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Michaelis-Menten steady-state kinetics of recombinant His6-tagged wild-type and mutant enzymes
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.51 - 62.87
2,4,6-trinitrotoluene
1.03 - 69.26
2-amino-4,6-dinitrotoluene
0.76 - 14.01
4-amino-2,6-dinitrotoluene
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
290 - 5389
2,4,6-trinitrotoluene
26 - 206
2-amino-4,6-dinitrotoluene
4 - 31
4-amino-2,6-dinitrotoluene
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant N-terminally His6-tagged enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 95% purity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene nfsB, recombinant expression of wild-type and mutant N-terminally His6-tagged enzymes in Escherichia coli strain BL21(DE3)
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gene nfsB, recombinant overexpression in Escherichia coli reporter strain SOS-R2, which contains a lacZ reporter gene under control of the SOS responsive promoter sfiA, functional nitroreductase NfsB expression in human HCT-116 cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F123A
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site-directed mutagenesis, residue F123 is located in helix alpha6 constituting the substrate entry site, the mutant enzyme kinetics are altered compared to the wild-type enzyme
F124A
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site-directed mutagenesis, residue F124 is located in helix alpha6 constituting the substrate entry site, the mutant enzyme kinetics are altered compared to the wild-type enzyme
F124N
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site-directed mutagenesis, residue F124 is located in helix alpha6 constituting the substrate entry site, the mutant enzyme kinetics are altered compared to the wild-type enzyme
F124W
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site-directed mutagenesis, residue F124 is located in helix alpha6 constituting the substrate entry site, the mutant enzyme kinetics are altered compared to the wild-type enzyme
N71S
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site-directed mutagenesis, active site residue mutation, the mutant shows increased activity with prodrug 5-[aziridin-1-yl]-2,4-dinitrobenzamide (CB1954) and nitrofurazone compared to the wild-type enzyme
T41L
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site-directed mutagenesis, active site residue mutation, the mutant shows increased activity with prodrug 5-[aziridin-1-yl]-2,4-dinitrobenzamide (CB1954) and nitrofurazone compared to the wild-type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
Pseudomonas aeruginosa NfsB and nitro-CBI-DEI is a promising enzyme/prodrug combination for gene directed enzyme prodrug therapy