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Enzyme Nomenclature
Information on EC 1.7.1.14 - nitric oxide reductase [NAD(P)+, nitrous oxide-forming]
Word Map on EC 1.7.1.14
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.7.1.14
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RECOMMENDED NAME
GeneOntology No.
nitric oxide reductase [NAD(P)+, nitrous oxide-forming]
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N2O + NAD(P)+ + H2O = 2 NO + NAD(P)H + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
nitrous oxide:NAD(P) oxidoreductase
A heme-thiolate protein (P-450). The enzyme from Fusarium oxysporum utilizes only NADH, but the isozyme from Trichosporon cutaneum utilizes both NADH and NADPH. The electron transfer from NAD(P)H to heme occurs directly, not requiring flavin or other redox cofactors.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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isozyme P450nor2 acts as the electron sink under anaerobic, denitrifying conditions to regenerate NADP+ for the pentose phosphate cycle
physiological function
physiological function
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P450nor has an important role in protecting the fungus from NO inhibition of mitochondria especially when dioxygen becomes limiting
physiological function
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P450nor is involved in fungal denitrification, it receives electrons directly from the distal pocket from NADH and/or NADPH without any help from a flavoprotein
physiological function
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P450nor is involved in fungal denitrification, it receives electrons directly from the distal pocket from NADH and/or NADPH without any help from a flavoprotein
physiological function
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P450nor is involved in fungal denitrification, it receives electrons directly from the distal pocket from NADH and/or NADPH without any help from a flavoprotein
physiological function
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P450nor is involved in fungal denitrification, it receives electrons directly from the distal pocket from NADH and/or NADPH without any help from a flavoprotein
physiological function
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P450nor is involved in nitrate respiration in mitochondria
physiological function
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Nor1p plays a protective role against macrophage-derived nitric oxide
physiological function
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isozyme Cnor2 enhances the reduction of nitrate to N2O in transgenic tobacco BY-2 cells
physiological function
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P450nor has an important role in protecting the fungus from NO inhibition of mitochondria especially when dioxygen becomes limiting; P450nor is involved in nitrate respiration in mitochondria
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NO + N3-
N2O + ?
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the co-denitrification reaction does not require an electron donor such as NADH
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?
NO + NADP + H+
N2O + NADP+ + H2O
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isozyme P450Nor2 prefers NADPH to NADH
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?
NO + NH4+
N2O + ?
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the co-denitrification reaction does not require an electron donor such as NADH
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?
NO + NADH + H+
N2O + NAD+ + H2O
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isozyme Cnor1 is specific to NADH, while isozyme Cnor2 can use both NADH and NADPH as electron donor
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?
NO + NADH + H+
N2O + NAD+ + H2O
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isozyme P450nor1 uses specifically NADH as electron donor, while isozyme P450Nor2 prefers NADPH to NADH
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?
NO + NADH + H+
N2O + NAD+ + H2O
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isozyme Fnor utilizes only NADH as electron donor
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-
?
NO + NADH + H+
N2O + NAD+ + H2O
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isozyme Tnor utilizes both NADH and NADPH as electron donors
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?
NO + NADPH + H+
N2O + NADP+ + H2O
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isozyme Cnor2 can use both NADH and NADPH as electron donor
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?
additional information
?
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P450nor is a reductase without monooxygenase activity
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additional information
?
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ammonium is not a direct substrate for P-450nor
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additional information
?
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P450nor is a reductase without monooxygenase activity
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additional information
?
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P450nor is a reductase without monooxygenase activity
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additional information
?
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the enzyme is peculiar in requiring only NADH and no electron transport system for the reduction of NO. NADPH is much less active as the cosubstrate
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additional information
?
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quantum chemical and combined quantum mechanics/molecular mechanics clearly favor a direct hydride transfer taking place between the NADH cofactor and NO, where the hydride is shifted to the N of NO. The barriers obtained for the syn, Pro-R conformation of NADH are lower and show significantly less variation than the barriers obtained in the case of anti conformation
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additional information
?
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the enzyme is peculiar in requiring only NADH and no electron transport system for the reduction of NO. NADPH is much less active as the cosubstrate
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additional information
?
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P450nor is a reductase without monooxygenase activity
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
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isozyme P450nor1 uses specifically NADH as electron donor, while isozyme P450Nor2 prefers NADPH to NADH
NADH
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isozyme Cnor1 is specific to NADH, isozyme Cno2 can use both NADH and NADPH as electron donor
NADPH
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Nor activity of wild type with NADPH as electron donor is only 13% of that with NADH as electron donor
NADPH
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isozyme P450nor1 uses specifically NADH as electron donor, while isozyme P450Nor2 prefers NADPH to NADH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
P450nor in a complex with an NADH analogue, nicotinic acid adenine dinucleotide, sitting drop vapor diffusion method, using 20-30% (w/v) PEG 8000, 0.2 M sodium acetate, 0.1 M sodium cacodylate (pH 5.5-7.5)
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sitting-drop vapor diffusion method, using 36% (w/v) PEG 4000, 0.1 M MES, 10% (v/v) glycerol at pH 7.0
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Resource Q column chromatography, Resource PHE column chromatography, and Superdex 200 gel filtration
DEAE cellulose column chromatography, phenyl-Superose column chromatography, and Mono Q column chromatography or Resource Q column chromatography
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DEAE-cellulose column chromatography and Mono Q or Resource Q column chromatography
Ni-NTA column chromatography and Poros HQ anion-exchange column chromatography
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DEAE-cellulose column chromatography and Mono Q or Resource Q column chromatography
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DEAE-cellulose column chromatography and Mono Q or Resource Q column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 404 amino acid fragment of Nor1p is expressed in Escherichia coli JM109 cells
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expressed in Escherichia coli JM109 (DE3) cells
wild type and mutant enzymes are expressed in Escherichia coli JM109 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the addition of glucose as a carbon source to the culture medium leads to the production of much more isozyme P450nor2 than a non-fermentable substrate (glycerol or acetate) does
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G76A
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the mutation decreases the NADH-dependent activity to 40% of the wild type activity
S73G/S75G
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the double mutation significantly improves NADPH-dependent Nor activity without affecting, or even slightly increasing, the NADHd-ependent activity
S75G
S75G
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the mutation significantly improves the NADPH-dependent Nor activity of isozyme Fnor, and the overall activity is accelerated via the NADPH-enhanced reduction step
S75G
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the mutation enormously improves the reactivity as compared to NADPH of P450nor
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LINKS TO OTHER DATABASES (specific for EC-Number 1.7.1.14)
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