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1.4.3.21: primary-amine oxidase

This is an abbreviated version!
For detailed information about primary-amine oxidase, go to the full flat file.

Word Map on EC 1.4.3.21

Reaction

RCH2NH2
+
H2O
+
O2
=
RCHO
+
NH3
+
H2O2

Synonyms

AGAO, AMAO2, AMAO3, amine oxidase 1, amine oxidase, copper containing, AO1, AO2, AOC2, AOC3, BAO, benzylamine oxidase, bovine plasma amine oxidase, bovine serum amine oxidase, BPAO, BSAO, CAO, Copper amine oxidase, copper amine oxidase 1, copper amine oxidase 8, copper-containing amine oxidase, copper-containing AO, copper-containing monoamine oxidase, copper-dependent amine oxidase, copper/quinone containing amine oxidase, Cu/TPQ amine oxidase, CuAO, CuAO1, CuAO2, CuAO3, CuAO8, EC 1.4.3.6, ECAO, ELAO, GPAO, grass pea amine oxidase, Hansenula polymorpha amine oxidase, HPAO, hPAO-1, HPAO-2, lentil seedling amine oxidase, LSAO, MAO-N, More, OVAO, PAO, pea seedling amine oxidase, plasma amine oxidase, PrAO, primary amine oxidase, primary-amine:oxygen oxidoreductase, PSAO, quinone- and copper-containing amine oxidase, quinone-containing copper amine oxidase, quinone-dependent amine oxidase, quinoprotein copper-containing amine oxidase, RAO, sainfoin amine oxidase, semicarbazide-sensitive amine oxidase, semicarbazide-sensitive amine oxidase/vascular adhesion protein-1, SSAO, SSAO/VAP-1, TPQ-containing CuAO, tynA, tyramine oxidase, copper-requiring, VAP-1, vascular adhesion protein 1, vascular adhesion protein-1

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.21 primary-amine oxidase

Crystallization

Crystallization on EC 1.4.3.21 - primary-amine oxidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with benzylhydrazine, 4-hydroxybenzylhydrazine and phenylhydrazine, micro dialysis method, using 1.05 M potassium sodium tartrate in 25mM HEPES buffer, pH 6.8, at 16°C
-
hanging-drop vapor diffusion method. Crystal structures of a series of Ru(II)-wire-enzyme complexes differing with respect to the length of the alkane linker
holenzyme, in which topaquinone is generated by incubation with Co2+ or Ni2+ and apoenzyme are crystallized by microdialysis method
microdialysis using 1.05 M potassium-sodium tartrate in 25 mM HEPES buffer, pH 6.8 containing 45% (v/v) glycerol
purified recombinant C-terminal StrepII-tagged enzyme in complex with inhibitors benzylhydrazine or tranylcypromine, vapour diffusion in hanging drop method, mixing of protein solution containing about 10 mg/ml protein in 50 mM HEPES, pH 7.0, with well solution containing 1.6 M ammonium sulfate and 150 mM sodium citrate pH 7.0. CuSO4, in a twofold molar excess, 2 weeks. The crystals are then transferred to a sitting drop well solution containing 30% v/v glycerol and 2 mM benzylhydrazine dihydrochloride or 0.4 mM tranylcypromine for 30 min, X-ray diffraction structure determination and analysis at 1.65-1.86 A resolution
the X-ray crystal structure of D298K at 1.7 A resolution
X-ray crystal structures of the Co2+ and Ni2+-enzyme are solved at 2.0-1.8 A resolution
hanging drop vapor diffusion method, using 0.2M (NH4)2SO4 and 0.1 M sodium acetate (pH 4.4) with 25% (w/v) PEG 2000 MME
-
purified recombinant genetic variants MAO-N-3 and MAO-N-5, from 10% w/v PEG 3350, 0.2 M proline, 0.1 M HEPES, pH 7.5, or 10% w/v PEG 5000 MME, 5% v/v tacsimate, 0.1 M HEPES, pH 7.0, with no difference in diffraction quality between the crystals from the two conditions, X-ray diffraction structure determination and analysis at 2.45 A and 1.85 A resolution, respectively
-
purified recombinant mutants MAO-N-D3 and MAO-N-D5, and truncated selenomethionine-labeled mutant MAO-N-D5, X-ray diffraction structure determination and analysis, multiple-wavelength anomalous diffraction and molecular replacement
-
purified enzyme with xenon is used as a molecular oxygen binding-site probe, 8 mg/ml protein in 100 mM HEPES pH 7 and 1.2 M sodium citrate, vappour diffusion method, 18°C, 2 weeks, X-ray diffraction structure determination and analysis at 2.5 A resolution, modelling
hanging drop vapor diffusion method, using 0.7 M potassium/sodium tartrate, 100 mM imidazole (pH 7.4), and 200 mM NaCl, at room temperature
hanging drop vapor diffusion method, using 8.0-9.5% (w/v) PEG 8000, 0.28-0.3 M phosphate at pH 6.0
in complex with ethylamine and benzylamine, hanging drop vapor diffusion method, using 8-9% (w/v) polyethylene glycol 8000 in 0.22-0.25 M potassium phosphate (pH 6.0)
isoform HPAO-2, sitting drop vapor diffusion method, using 0.5-0.75 M potassium sodium tartrate tetrahydrate in 0.10 M phosphate, pH 6.0-7.5, at 20°C
sitting drop, orthorhombic crystals, X-ray structure, 2.4 A
-