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Literature summary extracted from

  • Sugawara, A.; Matsui, D.; Yamada, M.; Asano, Y.; Isobe, K.
    Characterization of two amine oxidases from Aspergillus carbonarius AIU 205 (2015), J. Biosci. Bioeng., 119, 629-635 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.21 8-hydroxyquinoline strong inhibition at 1 mM Aspergillus carbonarius
1.4.3.21 CuCl2 strong inhibition at 1 mM Aspergillus carbonarius
1.4.3.21 hydrazine complete inhibition at 1 mM Aspergillus carbonarius
1.4.3.21 hydroxylamine complete inhibition at 1 mM Aspergillus carbonarius
1.4.3.21 Iproniazid nearly complete inhibition at 1 mM Aspergillus carbonarius
1.4.3.21 isoniazid nearly complete inhibition at 1 mM Aspergillus carbonarius
1.4.3.21 additional information not inhibited by MgCl2, MnCl2, CoCl2, ZnCl2, FeCl3, sodium azide, N-ethylmaleimide, and iodoacetate Aspergillus carbonarius
1.4.3.21 phenylhydrazine complete inhibition at 1 mM Aspergillus carbonarius
1.4.3.21 Semicarbazide nearly complete inhibition at 1 mM Aspergillus carbonarius

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.3.21 69100
-
enzyme III, gel filtration Aspergillus carbonarius
1.4.3.21 130000
-
enzyme II, gel filtration Aspergillus carbonarius

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.21 Aspergillus carbonarius
-
-
-
1.4.3.21 Aspergillus carbonarius AIU 205
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.3.21 DEAE-Toyopearl column chromatography, and phenyl-Toyopearl column chromatography Aspergillus carbonarius

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.21 mycelium
-
Aspergillus carbonarius
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.21 1,4-diaminobutane + H2O + O2 enzyme II shows 23% activity and enzyme III 12% activity compared to 4-aminobutanamide Aspergillus carbonarius ?
-
?
1.4.3.21 1,5-diaminopentane + H2O + O2 enzyme II shows 5% activity and enzyme III 31% activity compared to 4-aminobutanamide Aspergillus carbonarius ?
-
?
1.4.3.21 2-phenylethylamine + H2O + O2 enzyme II shows 134% activity and enzyme III 591% activity compared to 4-aminobutanamide Aspergillus carbonarius phenylacetaldehyde + NH3 + H2O2
-
?
1.4.3.21 3-aminopentanamide + H2O + O2 enzyme II shows 214% activity and enzyme III 11% activity compared to 4-aminobutanamide Aspergillus carbonarius 3-oxopentanamide + NH3 + H2O2
-
?
1.4.3.21 4-amino-1-butanol + H2O + O2 enzyme II shows 525% activity and enzyme III 267% activity compared to 4-aminobutanamide Aspergillus carbonarius 4-hydroxybutanal + NH3 + H2O2
-
?
1.4.3.21 4-aminobutanamide + H2O + O2 100% activity Aspergillus carbonarius 4-oxobutanamide + NH3 + H2O2
-
?
1.4.3.21 4-aminobutyric acid + H2O + O2 enzyme II shows no activity and enzyme III 10% activity compared to 4-aminobutanamide Aspergillus carbonarius 4-oxobutanoate + NH3 + H2O2
-
?
1.4.3.21 4-phenylbutylamine + H2O + O2 enzyme II shows 122% activity and enzyme III 493% activity compared to 4-aminobutanamide Aspergillus carbonarius 4-phenylbutanal + NH3 + H2O2
-
?
1.4.3.21 4-phenylbutylamine + H2O + O2 enzyme II shows 122% activity and enzyme III 493% activity compared to 4-aminobutanamide Aspergillus carbonarius AIU 205 4-phenylbutanal + NH3 + H2O2
-
?
1.4.3.21 5-amino-1-pentanol + H2O + O2 enzyme II shows 86% activity and enzyme III 388% activity compared to 4-aminobutanamide Aspergillus carbonarius 5-hydroxypentanal + NH3 + H2O2
-
?
1.4.3.21 5-aminopentanoic acid + H2O + O2 enzyme II shows 3% activity and enzyme III 7% activity compared to 4-aminobutanamide Aspergillus carbonarius 5-oxopentanoate + NH3 + H2O2
-
?
1.4.3.21 5-hydroxytryptamine + H2O + O2 enzyme II shows no activity and enzyme III 6% activity compared to 4-aminobutanamide Aspergillus carbonarius ?
-
?
1.4.3.21 5-hydroxytryptamine + H2O + O2 enzyme II shows no activity and enzyme III 6% activity compared to 4-aminobutanamide Aspergillus carbonarius AIU 205 ?
-
?
1.4.3.21 benzylamine + H2O + O2 enzyme II shows 4% activity and enzyme III 157% activity compared to 4-aminobutanamide Aspergillus carbonarius benzaldehyde + NH3 + H2O2
-
?
1.4.3.21 benzylamine + H2O + O2 enzyme II shows 4% activity and enzyme III 157% activity compared to 4-aminobutanamide Aspergillus carbonarius AIU 205 benzaldehyde + NH3 + H2O2
-
?
1.4.3.21 ethylamine + H2O + O2 enzyme II shows 1124% activity and enzyme III 119% activity compared to 4-aminobutanamide Aspergillus carbonarius acetaldehyde + NH3 + H2O2
-
?
1.4.3.21 histamine + H2O + O2 enzyme II shows 6% activity and enzyme III 322% activity compared to 4-aminobutanamide Aspergillus carbonarius 1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
-
?
1.4.3.21 histamine + H2O + O2 enzyme II shows 6% activity and enzyme III 322% activity compared to 4-aminobutanamide Aspergillus carbonarius AIU 205 1H-imidazol-4-ylacetaldehyde + NH3 + H2O2
-
?
1.4.3.21 additional information no activity with dopamine, 2-aminoacetic acid, 3-aminopropanoic aid, L-Arg, L-Orn, L-Lys, L-Phe, and D-Lys Aspergillus carbonarius ?
-
?
1.4.3.21 additional information no activity with dopamine, 2-aminoacetic acid, 3-aminopropanoic aid, L-Arg, L-Orn, L-Lys, L-Phe, and D-Lys Aspergillus carbonarius AIU 205 ?
-
?
1.4.3.21 n-butylamine + H2O + O2 enzyme II shows 368% activity and enzyme III 454% activity compared to 4-aminobutanamide Aspergillus carbonarius butanal + NH3 + H2O2
-
?
1.4.3.21 n-hexylamine + H2O + O2 enzyme II shows 244% activity and enzyme III 589% activity compared to 4-aminobutanamide Aspergillus carbonarius hexanal + NH3 + H2O2
-
?
1.4.3.21 n-pentylamine + H2O + O2 enzyme II shows 314% activity and enzyme III 596% activity compared to 4-aminobutanamide Aspergillus carbonarius pentanal + NH3 + H2O2
-
?
1.4.3.21 n-propylamine + H2O + O2 enzyme II shows 515% activity and enzyme III 201% activity compared to 4-aminobutanamide Aspergillus carbonarius propanal + NH3 + H2O2
-
?
1.4.3.21 Nalpha-benzyloxycarbony-L-lysine + H2O + O2 enzyme II shows 3% activity and enzyme III 12% activity compared to 4-aminobutanamide Aspergillus carbonarius ?
-
?
1.4.3.21 Nalpha-Z-D-lysine + H2O + O2 enzyme II shows no activity and enzyme III 10% activity compared to 4-aminobutanamide Aspergillus carbonarius ?
-
?
1.4.3.21 tryptamine + H2O + O2 enzyme II shows 4% activity and enzyme III 175% activity compared to 4-aminobutanamide Aspergillus carbonarius (1H-indol-3-yl)acetaldehyde + NH3 + H2O2
-
?

Subunits

EC Number Subunits Comment Organism
1.4.3.21 homodimer 2 * 67100, native enzyme II, SDS-PAGE Aspergillus carbonarius
1.4.3.21 monomer 1 * 65000, native enzyme III, SDS-PAGE Aspergillus carbonarius

Synonyms

EC Number Synonyms Comment Organism
1.4.3.21 copper-containing amine oxidase
-
Aspergillus carbonarius

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.3.21 40
-
enzyme III, isoelectric focusing Aspergillus carbonarius
1.4.3.21 45
-
enzyme II, isoelectric focusing Aspergillus carbonarius

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.3.21 20 50 when enzymes II and III are incubated at pH 7.0 for 30 min at 20-60°C without a substrate, more than 85% of the original activity remains below 40°C in both enzymes. At 50°C, enzyme II remains 60% of enzyme activity, while enzyme III loses 90% of its original activity Aspergillus carbonarius

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.21 7.5
-
enzyme III Aspergillus carbonarius
1.4.3.21 8.5
-
enzyme II Aspergillus carbonarius

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.4.3.21 5 8.5 when enzymes II and III are incubated at 40°C for 30 min in a pH range from 5.0 to 8.5 without a substrate, enzymes II and III remain at more than 80% of their original activity levels between pH 7.0 and 8.5 as well as between pH 6.5 and 8.5 Aspergillus carbonarius

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.4.3.21 Aspergillus carbonarius enzyme III, isoelectric focusing
-
5
1.4.3.21 Aspergillus carbonarius enzyme II, isoelectric focusing
-
5.3