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Information on EC 1.7.99.1 - hydroxylamine reductase Word Map on EC 1.7.99.1
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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NH3 + H2O + acceptor = hydroxylamine + reduced acceptor
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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).
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reductase, hydroxylamine (acceptor)
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hybrid cluster protein
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i.e. HCP, formerly termed prismane protein
hybrid cluster protein
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iron-chlorin protein also catalyzes methyl viologen-linked reduction of hydroxylamine and that of nitrite at a slower rate
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hydroxylamine reductase 1, hydroxylamine reductase 2
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wheat, nitrite reductase and hydroxylamine reductase are distinct enzymes
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hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
hydroxylamine + reduced methyl viologen
ammonia + oxidized methyl viologen
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hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
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hydroxylamine reductase 1 reacts with reduced benzyl viologen, ferredoxin and FMNH2
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hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
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FADH2, NADPH
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hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
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reduced benzyl viologen as electron donor
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hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
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hydroxylamine reductase 2 reacts with benzyl viologen and dithionite
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hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
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hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
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with pyocyanine or reduced methylene blue as electron donor
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hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
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hydroxylamine reductase 1 reacts with reduced benzyl viologen, ferredoxin and FMNH2
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hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
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hydroxylamine reductase 2 reacts with reduced benzyl viologen
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hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
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FADH2, NADPH
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hydroxylamine + reduced acceptor
ammonia + oxidized acceptor
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methyl viologen is more effective than benzyl viologen, flavin nucleotides are also utilized but to a lesser extent
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FAD
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flavoprotein, contains 0.9 nmol FAD per mg protein
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Co2+
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can substitute for Mn2+, only 10% as effective
Mn2+
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required for maximal activity
Iron
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iron-chlorin protein also catalyzes methyl viologen-linked reduction of hydroxylamine and nitrite at a slower rate
Iron
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iron containing proteins: nitrite reductase-hydroxylamine reductase 1 and hydroxylamine reductase 2
Iron
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the enzyme contains 2.7 Fe per molecule, in the case of full occupation of a hybrid cluster and a [4Fe-4S] cluster 8 Fe/molecule can be expected
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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
Isonicotinic acid
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hydroxylamine reductase 2, slight
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
hydrazine
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hydroxylamine reductase 2, slight
hydrazine
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hydrazine sulfate inhibits 10-15% at 4 mM
hydrazine
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competitive inhibition
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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
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0.0075
benzyl viologen
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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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0.0000004
hydroxylamine
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0.05 - 0.9
hydroxylamine
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0.4
hydroxylamine
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purified enzyme, at 70°C and pH 9.0
2.5
hydroxylamine
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at pH 9
38.9
hydroxylamine
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at pH 7.5
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3.8
hydroxylamine
Pyrococcus furiosus
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purified enzyme, at 70°C and pH 9.0
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9.5
hydroxylamine
Pyrococcus furiosus
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purified enzyme, at 70°C and pH 9.0
85
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3.7
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purified enzyme, at 70°C and pH 9.0
additional information
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additional information
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specific activities after different purification methods
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additional information
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no clear or consistent pH optima observed with hydroxylamine reductase 1 and hydroxylamine reductase 2
7.8
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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 / DSM 644 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
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32000
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hydroxylamine reductase 1, gel filtration
35000
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hydroxylamine reductase 2, gel filtration
51300
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2 * 51300, calculated from amino acid sequence
52000
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2 * 52000, SDS-PAGE
60000
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hydroxylamine reductase 1, gel filtration
65000
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hydroxylamine reductase 2, gel filtration
102600
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calculated from amino acid sequence
280000 - 320000
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gel filtration and sedimentation
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homodimer
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2 * 51300, calculated from amino acid sequence; 2 * 52000, SDS-PAGE
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gradual concentration for 7 weeks
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20 min, 25-38% loss of activity
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10 min, 25-40% loss of activity
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10 min, 50-85% loss of activity
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-18°C, DEAE-cellulose fraction, often stable for several weeks, but unpredictable loss of activity
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0°C, 65% activity with methyl viologen after 24 hours, 40% activity with benzyl viologen after 24 hours
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Poros HQ anion-exchange column chromatography and Superdex 200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
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Walker, G.C.; Nicholas, D.J.D.
Hydroxylamine reductase from Pseudomonas aeruginosa
Biochim. Biophys. Acta
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361-368
1961
Pseudomonas aeruginosa
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Horie, S.; Watanabe, T.; Nakamura, S.
Isolation, properties, and crystallization of an iron-chlorin protein from Aspergillus niger
J. Biochem.
80
579-593
1976
Aspergillus niger
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Hucklesby, D.P.; Hewitt, E.J.; James, D.M.
Possible active sites in nitrite reductase and hydroxylamine reductases from vegetable marrow (Curcubita pepo L.)
Biochem. J.
117
30P
1970
Cucurbita pepo
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Hewitt, E.J.; Hucklesby, D.P.
Molecular exclusion chromatography of nitrite and hydroxylamine reductases from plants with reference to electron donor systems
Biochem. Biophys. Res. Commun.
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689-693
1966
Cucurbita pepo, Spinacia oleracea
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Wolfe, M.T.; Heo, J.; Garavelli, J.S.; Ludden, P.W.
Hydroxylamine reductase activity of the hybrid cluster protein from Escherichia coli
J. Bacteriol.
184
5898-5902
2002
Escherichia coli
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Hucklesby, D.P.; Hewitt, E.J.
Nitrite and hydroxylamine reduction in higher plants. Fractionation, electron donor and substrate specificity of leaf enzymes, principally from vegetable marrow (Cucurbita pepo L.)
Biochem. J.
119
615-627
1970
Cucurbita pepo
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Sawhney, S.K.; Nicholas, D.J.D.
Nitrite, hydroxylamine and sulphite reductases in wheat leaves
Phytochemistry
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1499-1503
1975
Triticum aestivum
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Cresswell, C.F.; Hageman, R.H.; Hewitt, E.J.; Hucklesby, D.P.
The reduction of nitrate, nitrite and hydroxylamine to ammonia by enzymes from Curcubita pepo L. in the presence of reduced benzyl viologen as electron donor
Biochem. J.
94
40-53
1965
Cucurbita pepo
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Overeijnder, M.L.; Hagen, W.R.; Hagedoorn, P.L.
A thermostable hybrid cluster protein from Pyrococcus furiosus: effects of the loss of a three helix bundle subdomain
J. Biol. Inorg. Chem.
14
703-710
2009
Pyrococcus furiosus
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