Information on EC 1.7.99.1 - hydroxylamine reductase

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

EC NUMBER
COMMENTARY hide
1.7.99.1
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RECOMMENDED NAME
GeneOntology No.
hydroxylamine reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NH3 + H2O + acceptor = hydroxylamine + reduced acceptor
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
nitrate assimilation
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Nitrogen metabolism
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SYSTEMATIC NAME
IUBMB Comments
ammonia:acceptor oxidoreductase
A flavoprotein. Reduced pyocyanine, methylene blue and flavins act as donors for the reduction of hydroxylamine. May be identical to EC 1.7.2.1, nitrite reductase (NO-forming).
CAS REGISTRY NUMBER
COMMENTARY hide
37256-42-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
iron-chlorin protein also catalyzes methyl viologen-linked reduction of hydroxylamine and that of nitrite at a slower rate
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Manually annotated by BRENDA team
low activity
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Manually annotated by BRENDA team
low activity
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
low activity
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Manually annotated by BRENDA team
hydroxylamine reductase 1, hydroxylamine reductase 2
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Manually annotated by BRENDA team
wheat, nitrite reductase and hydroxylamine reductase are distinct enzymes
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Manually annotated by BRENDA team
low activity
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
show the reaction diagram
hydroxylamine + reduced methyl viologen
ammonia + oxidized methyl viologen
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
-
flavoprotein, contains 0.9 nmol FAD per mg protein
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
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can substitute for Mn2+, only 10% as effective
Mn2+
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required for maximal activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Atabrine
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hydroxylamine reductase 1
bathophenanthroline
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50% inhibition of hydroxylamine reductase 2 at 1 mM
CO
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with reduced benzyl viologen as electron donor, reductase 1: irreversible inhibition by light, reductase 2 : reversible inhibition by light
Cu2+
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inhibition of dialyzed enzyme at 0.0005 mM
cyanide
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100% inhibition at 5 mM
Guanidinium chloride
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25% inhibition at 2 mM, 30% inhibition at 3 mM
hydrazine
Isonicotinic acid
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hydroxylamine reductase 2, slight
nitrite
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oxygen
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reversible inhibition
p-chloromercuribenzoate
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47% inhibition at 0.5 mM
phenylmercuric acetate
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73% inhibition at 0.5 mM
pyruvate
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20% inhibition at 3.5 mM
Semicarbazide
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hydroxylamine reductase 2, slight
Zn2+
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inhibition of dialyzed enzyme at 0.0005 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-bipyridyl
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10% stimulation at 1 mM
8-hydroxyquinoline
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5% stimulation at 1 mM
CN-
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stimulates at concentrations above 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0075
benzyl viologen
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0.00001
FADH2
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0.0000004 - 38.9
hydroxylamine
0.000044
reduced methylene blue
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0.000012
reduced pyocyanine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.8
hydroxylamine
Pyrococcus furiosus
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purified enzyme, at 70C and pH 9.0
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.5
hydroxylamine
Pyrococcus furiosus
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purified enzyme, at 70C and pH 9.0
85
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.7
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purified enzyme, at 70C and pH 9.0
92
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at pH 7.5
458
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at pH 9
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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no clear or consistent pH optima observed with hydroxylamine reductase 1 and hydroxylamine reductase 2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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hydroxylamine reductase 1, gel filtration
35000
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hydroxylamine reductase 2, gel filtration
60000
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hydroxylamine reductase 1, gel filtration
65000
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hydroxylamine reductase 2, gel filtration
102000
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native PAGE
102600
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calculated from amino acid sequence
280000 - 320000
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gel filtration and sedimentation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 51300, calculated from amino acid sequence; 2 * 52000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gradual concentration for 7 weeks
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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20 min, 25-38% loss of activity
55
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10 min, 25-40% loss of activity
60
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10 min, 50-85% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, DEAE-cellulose fraction, often stable for several weeks, but unpredictable loss of activity
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0C, 65% activity with methyl viologen after 24 hours, 40% activity with benzyl viologen after 24 hours
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Poros HQ anion-exchange column chromatography and Superdex 200 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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