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Literature summary for 1.4.3.4 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]

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

Organic Solvent Stability

Organic Solvent Comment Organism
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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Homo sapiens
-

Substrates and Products (Substrate)

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
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
7.75
-
soluble enzyme Homo sapiens