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1.4.3.4: monoamine oxidase

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

Word Map on EC 1.4.3.4

Reaction

RCH2NHR'
+
H2O
+
O2
=
RCHO
+
R'NH2
+
H2O2

Synonyms

adrenaline oxidase, amine-oxygen oxidoreductase, C-MAO, EC 1.4.3.9, epinephrine oxidase, MAO, MAO A, MAO B, MAO type B, MAO-A, MAO-B, MAO-N, MAO-N-D5, MAOA, MAOB, monoamine oxidase, monoamine oxidase A, monoamine oxidase B, monoamine oxidase N, monoamine oxidase type B, monoamine oxidase-A, monoamine oxidase-B, monoamine oxidaseA, monoamine oxidases A, monoamine oxidases B, monoamine-oxidase-A, monoamine: O2-oxidoreductase, deaminated, monoamine: O2-oxidoreductase, deaminating, monoamine: O2-oxidoreductase: deaminating, monoamine:O2 oxidoreductase (deaminating), monoamine:O2 oxidoreductase, deaminating, monoamine:O2-oxidoreductase deaminating, monoaminoxidase B, More, semicarbazide-sensitive amine oxidase, serotonin deaminase, SSAO, tyraminase, tyramine oxidase, zMAO

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.4 monoamine oxidase

Crystallization

Crystallization on EC 1.4.3.4 - monoamine oxidase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of human MAO B in complex with the three inhibitors (safinamide, 7-(3-chlorobenzyloxy)-4-(methylamino)methylcoumarin or 7-(3-chlorobenzyloxy)-4-carboxaldehydecoumarin) reveal that they all bind noncovalently to the enzyme
MAO-A, X-ray diffraction structure determination at 2.2 A resolution. MAO-B in complex with a range of inhibitors, X-ray diffraction structure determination at 1.65 A resolution. The human MAO-A monomer species is more likely to crystallize than its dimeric form
-
sitting-drop vapor diffusion method, crystal structures of MAO B in complex with trans,trans-farnesol and that of the I199F MAO B mutant protein
sitting-drop vapor diffusion method, mutant enzymes Y435H, Y435F, Y435L, Y435W and wild-type enzyme in complex with p-nitrobenzylamine
sitting-drop vapour diffusion method,1.7 A structure of the reversible isatin-MAO-B complex, 2.3 A structure of the 1,4-diphenyl-2-butene-MAO-B complex, 2.2 A structure of the tranylcypromine-MAO B complex, 2.4 A structure of the N-(2-aminoethyl)-p-chlorobenzamide-MAO-B complex, 3.1 A structure of the lauryldimethylamine N-oxide-MAO-B complex
-
sitting-drop vapour diffusion method. Crystal structures of MAO B in complex with four of the N-propargylaminoindane class of MAO B inhibitors, rasagiline, N-propargyl-1(S)-aminoindane, 6-hydroxy-N-propargyl-1(R)-aminoindane, and N-methyl-N-propargyl-1(R)-aminoindane are determined at a resolution of better than 2.1 A. Rasagiline, 6-hydroxy-N-propargyl-1(R)-aminoindane, and N-methyl-N-propargyl-1(R)-aminoindane adopt essentially the same conformation with the extended propargyl chain covalently bound to the flavin and the indane ring located in the rear of the substrate cavity. N-propargyl-1(S)-aminoindane binds with the indane ring in a flipped conformation with respect to the other inhibitors, which causes a slight movement of the Tyr326 side chain
three-dimensional structure of the enzyme in complex with different reversible (isatin, 1,4-diphenyl-2-butene) and irreversible inhibitors (pargyline, N-(2,aminoethyl)-p-chlorobenzamide, and trans-2-phenylcyclopropylamine), up to 1.7 A resolution
-
using 12% (w/v) polyethylene glycol 4000, 100 mM N-(2-acetamido)-2-iminodiacetic acid buffer pH 6.5, and 70 mM lithium sulfate
-
vapour diffusion method at 4°C with a precipitant solution consisting of 12% w/v PEG 4000, 100 mM N-(2-acetamido)-2-iminodiacetic acid, pH 6.5, 70 mM lithium sulfate. Determination of structure at 3 A resolution
hanging drop vapour diffusion method, crystal structure of the enzyme complexed with the specific inhibitor, clorgyline, at 3.2 A resolution
hanging drop vapour-diffusion method at 277K with a reservoir containing 12% w/v polyethylene glycol 2000 monomethylether, 100 mM sodium acetate, 100 mM sodium phosphate buffer, pH 6.2, and 26% v/v glycerol. Enzyme complexed with clorgyline, 3.2 A resolution, crystals belong to the space group P4(3)2(1)2, with unit-cell parameters a = b = 158.2, c = 258.4 A
-
MAO A, X-ray diffraction structure determination at 3.3 A resolution. The dimer structure of rat MAO A is more readily crystallized than its monomeric form
-