Information on EC 1.7.1.10 - hydroxylamine reductase (NADH)

Word Map on EC 1.7.1.10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.7.1.10
-
RECOMMENDED NAME
GeneOntology No.
hydroxylamine reductase (NADH)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NH3 + NAD+ + H2O = hydroxylamine + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
protein S-nitrosylation and denitrosylation
-
-
Nitrogen metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
ammonium:NAD+ oxidoreductase
Also acts on some hydroxamates.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-06-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
nitrite and hydroxylamine reductase are associated within the same enzyme
-
-
Manually annotated by BRENDA team
very low activity
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Amphibia
-
-
-
Manually annotated by BRENDA team
no activity in fish
-
-
-
Manually annotated by BRENDA team
no activity in reptilia
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cyanobacterium
-
-
Manually annotated by BRENDA team
Pigeon
-
-
-
Manually annotated by BRENDA team
strain E1F1, highest activity in cells grown in the presence of hydroxylamine
-
-
Manually annotated by BRENDA team
strain E1F1, highest activity in cells grown in the presence of hydroxylamine
-
-
Manually annotated by BRENDA team
engineered enzyme, H256V mutant of carbon monoxide dehydrogenase displays hydroxylamine reductase activity
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
anthranillic hydroxamate + NADH + H+
anthranilamide + NAD+ + H2O
show the reaction diagram
benzamidoxime + NADH + H+
benzamidine + NAD+ + H2O
show the reaction diagram
dinitrobenzene + NADH
?
show the reaction diagram
-
-
-
-
?
guanoxabenz + NADH
?
show the reaction diagram
hydroxylamine + methyl viologen
NH3 + H2O + ?
show the reaction diagram
hydroxylamine + NADH
NH3 + H2O + NAD+
show the reaction diagram
hydroxylamine + NADH
NH3 + NAD+ + H2O
show the reaction diagram
N,N-dimethylhydroxylamine + NADH
dimethylamine + NAD+ + H2O
show the reaction diagram
-
-
-
?
N-hydroxy-1-naphthylamine + NADH
1-naphthylamine + NAD+ + H2O
show the reaction diagram
N-hydroxy-2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine + NADH
2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine + NAD+ + H2O
show the reaction diagram
N-hydroxy-2-amino-3,8-dimethylimidazo[4,5-f]quinoxaline + NADH
2-amino-3-methylimidazo[4,5-f]quinoxaline + NAD+ + H2O
show the reaction diagram
N-hydroxy-2-amino-alpha-carboline + NADH
2-amino-alpha-carboline + NAD+ + H2O
show the reaction diagram
N-hydroxy-2-aminofluorene + NADH
2-aminofluorene + NAD+ + H2O
show the reaction diagram
N-hydroxy-2-naphthylamine + NADH
2-naphthylamine + NAD+ + H2O
show the reaction diagram
N-hydroxy-4,4'-methylenebis(2-chloroaniline) + NADH
4,4'-methylenebis(2-chloroaniline) + NAD+
show the reaction diagram
N-hydroxy-4-aminoazobenzene + NADH
4-aminoazobenzene + NAD+ + H2O
show the reaction diagram
N-hydroxy-4-aminobiphenyl + NADH
4-aminobiphenyl + NAD+ + H2O
show the reaction diagram
N-hydroxy-aniline + NADH
aniline + NAD+ + H2O
show the reaction diagram
N-hydroxy-arylamines + NADH
N-arylamines + NAD+ + H2O
show the reaction diagram
N-hydroxyamphetamine + NADH
amphetamine + NAD+ + H2O
show the reaction diagram
-
-
-
?
N-hydroxydebrisoquine + NADH
debrisquine + NAD+ + H2O
show the reaction diagram
N-hydroxypiperidine + NADH
piperidine + NAD+ + H2O
show the reaction diagram
-
-
-
?
N-methyl-N-benzyl-hydroxylamine + NADH
N-methylbenzylamine + NAD+ + H2O
show the reaction diagram
-
-
-
?
N-methyl-N-n-octyl-hydroxylamine + NADH
N-methyl-n-octylamine + NAD+ + H2O
show the reaction diagram
-
-
-
?
N-methylhydroxylamine + NADH
methylamine + NAD+ + H2O
show the reaction diagram
NO2- + NADH
NH3 + H2O + NAD+
show the reaction diagram
phenylhydroxylamine + NADH
phenylamine + NAD+ + H2O
show the reaction diagram
sulphamethoxazole hydroxylamine + NADH
sulphamethoxazole + NADH
show the reaction diagram
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
hydroxylamine + NADH
NH3 + NAD+ + H2O
show the reaction diagram
N-hydroxy-arylamines + NADH
N-arylamines + NAD+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
stimulates
iron-sulfur centre
NADPH
additional information
-
purified enzyme: absolute requirement for an unidentified, dissociable, heat-stable, organic factor obtained from soybean leaf extract, no flavin requirement
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CN-
-
stimulating at concentrations above 5 mM, inhibitory after 1 h preincubation
CO
-
slight inhibition
Mn2+
-
0.1 mM, approx. 6fold stimulation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluenesulfonate
-
1.5 mM, 68% inhibition, hydroxylamine protects
2,2'-dipyridyl
8-hydroxyquinoline
Antimycin 1
-
0.1 mM, 26% inhibition of hydroxylamine reductase activity
Bromelain
-
-
-
CaCl2
-
reactivation by washing
deoxycholic acid
-
-
Dinitrophenol
-
0.1 mM, 80% inhibition of hydroxylamine reductase activity
dithioerythritol
-
-
Duponol C
-
-
HgCl2
hydrazine
-
1 mM, complete inhibition
Iodine
-
0.5 mM, 80% inhibition, preincubation with hydroxylamine protects
KCl
-
reactivation by washing
Murine phospholipase
-
-
-
N-ethylmaleimide
N-Methyl hydroxylamine
-
-
N-Methylhydroxylamine
NaCl
-
reactivation by washing
NADH
-
inhibits in absence of hydroxylamine
nitrite
-
nitrite and hydroxylamine reductase activity are associated with the same enzyme, nitrite and hydroxylamine are competitive for the same binding site
o-phenanthroline
p-chloromercuribenzoate
p-hydroxymercuribenzoate
papain
-
-
-
potassium cyanide
-
-
potassium ethyl xanthate
potassium thiocyanate
-
0.1 mM, 90% inhibition of hydroxylamine reductase activity, nitrite reductase activity is not inhibited
Propanol
-
-
Rose bengal
-
0.5 mM, 94% inhibition
rotenone
-
0.1 mM, 52% inhibition of hydroxylamine reductase activity
Salicylaldoxime
Sodium arsenate
-
-
Sodium diethyl dithiocarbamate
Subtilopeptidase A
-
-
-
sulfite
Trypsin
-
-
-
Uranyl acetate
-
ATP, ADP, sodium diphosphate restores activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 5.3
hydroxylamine
0.007
methyl viologen
-
pH 9.3, 40C
0.07 - 0.15
NADH
0.1
NADPH
-
-
0.0048
NO2-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.52
NO2-
-
-
0.7
sulfite
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.422
-
reduction of nitrite
0.68
-
reduction of hydroxylamine
458
-
pH 9.0
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.3
-
-
6.6 - 7.1
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4 - 8.4
-
pH 5.4: considerable activity in Tris-maleate buffer, pH 8.4: about 50% activity
5.5 - 7.2
-
pH 5.5: about 70% of activity maximum, pH 7.2: 50% activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
firmly attached to mitochondrial membrane
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
53000
-
SDS-PAGE
57800
-
calculated from the deduced amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
3 protein fractions are required to reconstitute NADH-hydroxylamine reductase activity: detergent-extracted cytochrome b5 and its flavoprotein and a third microsomal protein
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
-
complete loss of activity after brief exposure
394438
7.5 - 9.5
-
highest stability
394440
8.4
-
no loss of activity after brief exposure
394438
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27
-
stable for more than 1 h
38
-
1 h, inactivation
40
-
membrane bound enzyme, 10 min, pH 7.4, dithiothreitol, no loss of activity
60
-
membrane bound enzyme, pH 7.4, dithiothreitol, complete loss of activity
additional information
-
NADH prevents heat damage
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against 3 mM sodium diphosphate, 1 mM cysteine solution, pH 8, 2 h, less than 50% loss of activity, against 10 mM phosphate, pH 8, 1 h, complete loss of activity
-
dithiothreitol stabilizes during storage
-
freezing partially inactivates membrane bound enzyme
-
little or no activity in phosphate buffer unless 1 mM EDTA is included in the reaction mixture
-
NADH prevents heat damage
-
solubilization with deoxycholate, n-butanol or acetone destroys membrane bound enzyme
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
very unstable in the absence of sulfhydryl protecting agents, stable in the presence of 0.2 mM dithiothreitol
-
394434
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, slow loss of activity over several weeks
-
-20C, 1 month, 60-90% loss of activity
-
4C, 1 week, no loss in activity
-
4C, overnight
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme not seperated from pyridine nucleotide-nitrite reductase
-
nitrite and hydroxylamine reductase are associated with the same enzyme
-
recombinant protein using His-tag
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli JM109 as His-tag fusion protein
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in cells exposed to nitric oxide, enzyme is upregulated 1.4fold. In addition, 178 genes are upregulated and 201 genes downregulated more than 2fold