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Literature summary extracted from

  • Gottowik, J.; Cesura, A.M.; Malherbe, P.; Lang, G.; Da Prada, M.
    Characterization of wild-type and mutant forms of human monoamine oxidase A and B expressed in a mammalian cell line (1993), FEBS Lett., 317, 152-156.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.3.4 expression in a human embryonic kidney cell line and expression in mammalian cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.4.3.4 C397A expressed protein catalytically inactive Homo sapiens
1.4.3.4 C397H expressed protein catalytically inactive Homo sapiens
1.4.3.4 additional information MAO-A chimeric form containing the N-terminus of MAO-B, the first 36 acid sequence, do not significantly differ in their affinity for 5-hydroxytryptamine and phenylethylamine, MAO-B chimeric form containing the N-terminus of MAO-A , the first 45 acid sequence, but kinetic properties could not be detemined Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.4 Deprenyl
-
Homo sapiens
1.4.3.4 Harmaline
-
Homo sapiens
1.4.3.4 lazabemide
-
Homo sapiens
1.4.3.4 Ro 19-6327
-
Homo sapiens
1.4.3.4 Ro 41-1049
-
Homo sapiens

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 wild-type MAO-A and B and of their chimera Homo sapiens
1.4.3.4 0.19
-
5-hydroxytryptamine
-
Homo sapiens

Organism

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

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.4.3.4 More the N-terminal region of the two isoenzymes is not involved in the different specificity of the two isoenzymes for substrates and inhibitors Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.4 flavin covalent coupling of FAD to MAO occurs specifically at the -SH-groups of cysteine Homo sapiens