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Literature summary for 1.4.3.4 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)

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

Protein Variants

Protein Variants Comment Organism
C397A expressed protein catalytically inactive Homo sapiens
C397H expressed protein catalytically inactive Homo sapiens
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

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Km of wild-type MAO-A and B and of their chimera Homo sapiens
0.19
-
5-hydroxytryptamine
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
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

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