Ligand hydroxylamine

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Basic Ligand Information

Molecular Structure
Picture of hydroxylamine (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
H3NO
hydroxylamine
AVXURJPOCDRRFD-UHFFFAOYSA-N
Synonyms:
hydroxyamine, NH2OH

Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (21 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
hydroxylamine + reduced ferredoxin = NH3 + H2O + oxidized ferredoxin
show the reaction diagram
-
hydroxylamine + NADH = NH3 + NAD+ + H2O
show the reaction diagram
-
hydroxylamine + 2 ferricytochrome c = nitroxyl + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
benzonitrile + hydroxylamine + H2O = benzohydroxamic acid + NH3
show the reaction diagram
-

In Vivo Product in Enzyme-catalyzed Reactions (6 results)

EC NUMBER
PROVEN IN VIVO REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
nitrite + 4 reduced ferredoxin + 5 H+ = hydroxylamine + H2O + 4 oxidized ferredoxin
show the reaction diagram
-
-
nitrite + 4 ferrocytochrome c + 5 H+ = hydroxylamine + H2O + 4 ferricytochrome c
show the reaction diagram
-

Substrate in Enzyme-catalyzed Reactions (177 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
hydroxylamine + reduced ferredoxin = NH3 + H2O + oxidized ferredoxin
show the reaction diagram
-
NH2OH + ATP + H2O = ?
show the reaction diagram
-
hydroxylamine + NADH + H+ = ?
show the reaction diagram
-
NAD(P)H + NH2OH = NAD(P)+ + NH3 + H2O
show the reaction diagram
-
hydroxylamine + (ferrocytochrome c)-subunit = ? + (ferricytochrome c)-subunit
show the reaction diagram
-
hydroxylamine + NADPH = ammonia + NADP+
show the reaction diagram
-
hydroxylamine + a [DsrC protein]-dithiol + 2 reduced acceptor + 2 H+ = ? + a [DsrC protein]-disulfide + 2 acceptor + 3 H2O
show the reaction diagram
-
acetyl-CoA + hydroxylamine = CoA + N-acetylhydroxylamine
show the reaction diagram
-
acetyl phosphate + hydroxylamine = acetyl hydroxamate + phosphate
show the reaction diagram
-
malonamic acid + hydroxylamine = malonohydroxamate + ?
show the reaction diagram
-
theanine + hydroxylamine = gamma-glutamylhydroxamic acid + ethylamine
show the reaction diagram
-
benzonitrile + hydroxylamine + H2O = benzohydroxamic acid + NH3
show the reaction diagram
-
Crotonyl-CoA + hydroxylamine = CoA + 3-methyl-5-isoxazolidinone
show the reaction diagram
-
mesaconate + hydroxylamine = ?
show the reaction diagram
-
ATP + methionine + hydroxylamine = methionine hydroxamate + AMP + diphosphate
show the reaction diagram
-
ATP + D-Ala + hydroxylamine = D-Alanine hydroxamate + AMP + diphosphate
show the reaction diagram
-
ATP + L-Asp + hydroxylamine = AMP + diphosphate + Asn + beta-aspartyl hydroxamate
show the reaction diagram
-
ATP + L-Asp + hydroxylamine = ADP + phosphate + beta-aspartylhydroxamate
show the reaction diagram
-
ATP + 4-methylene-L-glutamate + hydroxylamine = AMP + diphosphate + 4-methylene-L-glutamylhydroxamate
show the reaction diagram
-
ATP + L-Glu + hydroxylamine = ADP + phosphate + gamma-L-Glu-hydroxylamine
show the reaction diagram
-
ATP + gamma-Glu-2-aminobutyrate + hydroxylamine = ADP + phosphate + gamma-(alpha-aminomethyl)Glu-2-aminobutyryl-Gly
show the reaction diagram
-
ATP + L-glutamate + hydroxylamine = ADP + phosphate + N5-hydroxy-L-glutamine
show the reaction diagram
-
GTP + IMP + hydroxylamine = GDP + phosphate + ?
show the reaction diagram
-
ATP + L-Asp + NH2OH = AMP + diphosphate + beta-aspartylhydroxamate
show the reaction diagram
-
ATP + hydroxylamine + HCO3- = ATP + phosphate + N-hydroxy carbamoyl phosphate
show the reaction diagram
-

Product in Enzyme-catalyzed Reactions (37 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
ammonia + NAD(P)H + O2 = hydroxylamine + NAD(P)+ + H2O
show the reaction diagram
-
-
4-amino-2,6-dichlorophenol + NADPH + O2 = 2,6-dichloro-p-hydroquinone + NADP+ + NH2OH
show the reaction diagram
-
nitrite + 4 reduced ferredoxin + 5 H+ = hydroxylamine + H2O + 4 oxidized ferredoxin
show the reaction diagram
-
-
hyponitrite + NAD+ = hydroxylamine + NADH
show the reaction diagram
-
nitrite + 4 ferrocytochrome c + 5 H+ = hydroxylamine + H2O + 4 ferricytochrome c
show the reaction diagram
-
hydroxylamine N-oxide + electron donor = hydroxylamine + H2O + oxidized electron donor
show the reaction diagram
-
NO + ferrocytochrome c + 2 H+ = hydroxylamine + H2O + ferricytochrome c
show the reaction diagram
-
hydroxyguanidine + glycine = hydroxylamine + guanidinoacetate
show the reaction diagram
-
-
hydroxyurea = HCO3- + NH4+ + NH2OH
show the reaction diagram
-
-
L-Glutamic acid gamma-monohydroxamate + H2O = Hydroxylamine + Glu
show the reaction diagram
-
-

Activator in Enzyme-catalyzed Reactions (10 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
stimulation at high concentrations
-
activates, restores the inhibition by Fe2+
-
1 mM, 108% of initial activity
-
uncompetitive activation
-
11% activation aat 1 mM
-
20% activation at 1 mM
-
0.4-1.2 M, 7fold stimulation of alpha subunit
-
activates Ser racemase activity, but inhibits Asp racemase activity
-

Inhibitor in Enzyme-catalyzed Reactions (376 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
1 mM, complete inhibition
-
inhibitory at 100 mM
-
1mM, 29.5% residual activity
-
deactivation
-
1 mM, 57.1% inhibition
-
2 mM, 23% residual activity
-
50% inhibition at 5 mM, competitive
-
87% inhibition at 1 mM
-
83% residual activity at 1 mM
-
0.05 mM, 50% inhibition of brominating activity
-
25% residual activity at 2 mM
-
competitive and uncompetitive inhibition; inhibits rVCPO both competitively and uncompetitively. The competitive inhibition constant: 0.04 mM, uncompetitive inhibition 0.08 mM
-
complete loss of activity
-
slight inhibition at 10 mM
-
10 mM, complete inhibition
-
1-3 mM
-
inhibition of the exchange reaction of diphosphate and ATP
-
in presence of substrate
-
protonated and neutral form, compete with the attacking water molecule for the binding site E268, inhibition mechanism
-
1 mM, 52% residual activity
-
0.1 mM concentration 100% inhibition
-
inhibits protein B and fraction C
-
enzyme preincubated with the inhibitor, 0.00166 mM, for 60 min at room temperature before the addition of the substrate, 9% inhibition
-
competitive inhibitor with ammonia and uncompetitive inhibitor with both 2-oxoglutarate and NADPH
-
0.1 M, strong inhibition
-
3 mM, 33% loss of activity
-
slight
-
0.1 mM, 69% inhibition
-
15% inhibition at 1 mM
-
22% inhibition at 5 mM
-
at 5 mM 58% inhibition
-
slight
-
34% inhibition at 10 mM
3 mM, 80% inhibition
-
reversible
-
0.01 M
-
pyridoxal 5'-phosphate restores
-
slightly inhibitory
-
100 mM, complete inhibition
-
95% inhibition at 1 mM, 76% at 0.1 mM
-
50 mM, almost complete inhibition
-
100 mM, complete
-
1 mM, 23% inhibition
-
inhibition of PfAspAT abolishes all glutamate oxaloacetate transamination activity in the cytoplasm of cultured parasites, demonstrating that no other enzyme within the cytoplasm can complement PfAspAT activity
-
strong inhibition
-
70% inhibition at 1 mM
-
complete inhibition at 0.5 mM
-
complete inhibition by a mixture of hydroxylamine, (aminooxy)acetic acid, and gabaculine as inhibitors specific for pyridoxal 5'-phosphate-dependent enzymes
-
1 mM, 50% inhibition
-
3.3 mM: 87% inhibition, 0.33 mM: 58.3% inhibition, 0.033 mM: 16.6% inhibition
-
2 mM, 58% inhibition
-
0.5 mM: 63% inhibition
-
inhibits the aldehyde form of the enzyme while the amino form is found to be inert
-
37% activity retained at 1 mM, 6% activity retained at 10 mM
-
1 mM, complete inhibition of the three isoenzymes
-
0.004 M, 80% inhibition
-
inhibits acetate kinase reaction in a nonlinear and noncompetitive fashion, substantial inhibition at concentrations of 704 mM and minimal inhibition at concentrations of 250 microM hydroxylamine
-
rapid and irreversible inactivation
-
after incubation with 200 mM hydroxylamine at pH 7.0 in the presence of 0.2 mM (R)-2-hydroxyisocaproyl-CoA and removal of the small molecules by gel filtration, the transferase sample shows 94% inactivation, while no inactivation is observed under the same conditions in the absence of (R)-2-hydroxyisocaproyl-CoA
-
inhibits the reaction between ADP-ribose and polypeptides
-
inactivates the thioester bond on C3, dramatically decreases the deposition of C3b on microbes
-
competitive inhibitor at pH 7.2
-
complete inhibition at 0.05 mM, reversible by 100 nM pyridoxal 5'-phosphate
-
1 mM
-
67% inhibition at 1 mM
-
weak
-
2 mM, complete inhibition
-
formation of a catalytically inactive SH-enzyme from the catalytically active acetyl-S-enzyme
-
formation of a catalytically inactive SH-enzyme from the catalytically active acetyl-S-enzyme
-
1 mM, 23% inhibition of carboxylation activity, 9% inhibition of decarboxylation activity
-
1 mM, 35% inhibition
-
82.7% residual activity at 1 mM
-
1 mM, 95% inhibition
-
1 mM, 100% inhibition
-
1 mM, complete inhibition
-
reversed with acetic anhydride
-
partial
-
1 mM, 10% inhibition
-
50 mM almost complete inhibition
-
65% inhibition at 1 mM
-
competitive
-
the enzyme is strongly inhibited by hydroxylamine (91.2% inhibition at 1 mM)
-
almost completely reversible by dialysis against pyridoxal 5'-phosphate
-
20 mM, 60% inhibition
-
inhibition of ATP-diphosphate exchange
-
above 400 mM
-
the enzyme is sensitive to treatment with hydroxylamine
-
sensitive to
-
complete inhibition
-

3D Structure of Enzyme-Ligand-Complex (PDB) (14 results)

Enzyme Kinetic Parameters

kcat Value (Turnover Number) (36 results)

EC NUMBER
TURNOVER NUMBER [1/S]
TURNOVER NUMBER MAXIMUM [1/S]
COMMENTARY
LITERATURE
383
-
oxidized
0.53
-
pH 8, temperature not specified in the publication
3.8
-
purified enzyme, at 70°C and pH 9.0
29
-
pH 7.6, 22°C
0.00177
-
-
12.83
-
60°C, pH 7.8

KM Value (116 results)

EC NUMBER
KM VALUE [MM]
KM VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
2.91
-
apparent value, at pH 8.0 and 30°C
0.35
-
in 10 mM Tris-HC1 (pH 8.0), at 30°C
48
-
pH 7.6, 22°C
329.4
-
-
19.3
-
-
131
-
strain R312, transfer reaction

Ki Value (19 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.0308
-
-
0.00014
-
-
0.12
-
-
0.00043
-
pH 8, 37°C
0.16
-
-

IC50 Value (12 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.069
-
pH 8, 37°C
0.0048
-
pH 8.2, 37°C
0.0159
-
at 10 microM, IC50 value is 0.0159 mM

References & Links