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Literature summary for 1.4.3.4 extracted from

  • Milczek, E.M.; Bonivento, D.; Binda, C.; Mattevi, A.; McDonald, I.A.; Edmondson, D.E.
    Structural and mechanistic studies of mofegiline inhibition of recombinant human monoamine oxidase B (2008), J. Med. Chem., 51, 8019-8026.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.3.4

Inhibitors

Inhibitors Comment Organism Structure
1,4-diphenyl-2-butene
-
 Homo sapiens
mofegiline mechanism-based irreversible, competitive inhibition versus substrate of MAO-B with a 1:1 molar stoichiometry, also competitively inhibits MAO-A. Effects on UV absorption spectra of flavin, and inhibitor-bound enzyme structure, overview Homo sapiens
N-(2-aminoethyl)-4-chlorobenzamide
-
 Homo sapiens
tranylcypromine inhibition of MAO-B Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrial outer membrane
-
 Homo sapiens 5741
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P27338
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
flavoprotein
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
MAO-B
-
 Homo sapiens
monoamine oxidase B
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD dependent on Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.000028
-
 mofegiline MAO B Homo sapiens
0.0011
-
 mofegiline MAO A Homo sapiens