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Literature summary for 1.4.3.21 extracted from

  • Elovaara, H.; Kidron, H.; Parkash, V.; Nymalm, Y.; Bligt, E.; Ollikka, P.; Smith, D.; Pihlavisto, M.; Salmi, M.; Jalkanen, S.; Salminen, T.
    Identification of two imidazole binding sites and key residues for substrate specificity in human primary amine oxidase AOC3 (2011), Biochemistry, 50, 5507-5520.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli DH5alpha cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Homo sapiens

Protein Variants

Protein Variants Comment Organism
L469G the mutant shows increased affinity for benzylamine and methylamine compared to the wild type enzyme Homo sapiens
M211V the mutant shows increased affinity for benzylamine and methylamine compared to the wild type enzyme Homo sapiens
M211V/Y394N/L469G the mutant of AOC3 changes substrate preferences toward those of copper-containing monoamine oxidase AOC2 with high activity towards 2-phenylethylamine Homo sapiens
T212A the mutant shows increased affinity for benzylamine and reduced affinity for methylamine compared to the wild type enzyme Homo sapiens
Y394N the mutant shows reduced affinity for benzylamine and methylamine compared to the wild type enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
imidazole
-
Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.013
-
benzylamine mutant enzyme L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C Homo sapiens
0.018
-
benzylamine mutant enzyme M211V/Y394N/L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C Homo sapiens
0.025
-
benzylamine mutant enzyme M211V, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C Homo sapiens
0.084
-
benzylamine mutant enzyme T212A, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C Homo sapiens
0.184
-
benzylamine wild type enzyme, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C Homo sapiens
0.215
-
benzylamine mutant enzyme Y394N, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C Homo sapiens
0.236
-
methylamine mutant enzyme L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C Homo sapiens
0.28
-
methylamine mutant enzyme M211V, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C Homo sapiens
0.331
-
methylamine wild type enzyme, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C Homo sapiens
0.502
-
methylamine mutant enzyme T212A, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C Homo sapiens
1.26
-
methylamine mutant enzyme Y394N, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C Homo sapiens
2.043
-
methylamine mutant enzyme M211V/Y394N/L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Homo sapiens Q16853
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
blood plasma
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-phenylethylamine + H2O + O2
-
Homo sapiens 2-phenylethanal + NH3 + H2O2
-
?
4-tyramine + H2O + O2
-
Homo sapiens (4-hydroxyphenyl)acetaldehyde + NH3 + H2O2
-
?
benzylamine + H2O + O2
-
Homo sapiens benzaldehyde + NH3 + H2O2
-
?
methylamine + H2O + O2
-
Homo sapiens formaldehyde + NH3 + H2O2
-
?

Synonyms

Synonyms Comment Organism
AOC3
-
Homo sapiens
copper-containing monoamine oxidase
-
Homo sapiens
primary amine oxidase
-
Homo sapiens
VAP-1
-
Homo sapiens
vascular adhesion protein-1
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
2,4,5-trihydroxyphenylalanine quinone
-
Homo sapiens

General Information

General Information Comment Organism
physiological function the enzymatic activity plays a crucial role in leukocyte trafficking Homo sapiens