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Literature summary extracted from

  • Roth, J.A.; Eddy, B.J.
    Kinetic properties of membrane-bound and Triton X-100-solubilized human brain monoamine oxidase (1980), Arch. Biochem. Biophys., 205, 260-266.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.4 additional information
-
 additional information Km of membrane-bound and Triton X-100-solubilized enzyme Homo sapiens

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.4.3.4 Triton X-100 solubilization of MAO-A and MAO-B alters the energies of activation and Km for a number of substrates Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.4 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.4.3.4 brain
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.4 2-phenylethylamine + H2O + O2 MAO-B selective substrate Homo sapiens 2-phenylethanal + NH3 + H2O2
-
 ?
1.4.3.4 benzylamine + H2O + O2
-
 Homo sapiens benzaldehyde + NH3 + H2O2
-
 ?
1.4.3.4 RCH2NH2 + H2O + O2 5-hydroxytryptamine, MAO-A selective substrate Homo sapiens RCHO + NH3 + H2O2
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.4 additional information
-
 pH-value for optimal deamination by a membrane-bound preparation of enzyme was dependent of the concentration of the amine employed Homo sapiens
1.4.3.4 7.75
-
 soluble enzyme Homo sapiens