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Literature summary for 1.4.3.4 extracted from

  • Ramsay, R.R.; Olivieri, A.; Holt, A.
    An improved approach to steady-state analysis of monoamine oxidases (2011), J. Neural Transm., 118, 1003-1019.
    View publication on PubMed
Search for more literature for 1.4.3.4

Inhibitors

Inhibitors Comment Organism Structure
(+)-amphetamine reversible competitive inhibitor Homo sapiens
2-(4,5-dihydroimidazol-2-yl)-isoquinoline reversible non-competitive/mixed inhibitor Homo sapiens
2-(4,5-dihydroimidazol-2-yl)-quinoline reversible non-competitive/mixed inhibitor Homo sapiens
2-(5,7-dibromobenzofuran-2-yl)-imidazoline reversible non-competitive/mixed inhibitor Homo sapiens
amitriptyline competive inhibition with 2-phenylethylamine as substrate Homo sapiens
di(2-hydroxyethyl)methyldodecylammonium reversible competitive inhibitor Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic constants for pure hMAO-B oxidising different substrates in the presence of reversible competitive inhibitors or reversible non-competitive/mixed inhibitors Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P27338
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-phenylethylamine + H2O + O2 proposed pathways for amine oxidation: the amine substrate may bind to oxidised enzyme (E/FADox), leading to the release of product imine via a binary (1) or ternary (2) pathway. The relative contributions of these pathways cannot be determined directly by steady-state approaches. In following pathway 1, the unoccupied reduced enzyme (E/FADred) is generated, to which substrate may also bind. Reoxidation of the E/FADred–S species (pathway 3) bypasses direct regeneration of E/FADox, with the consequence that imine released subsequent to this step, whether through the binary or ternary pathways leading from E/FADred–imine, is a product of substrate binding to a second enzyme species Homo sapiens 2-phenylethanal + NH3 + H2O2
-
 ?
4-phenylbutylamine + H2O + O2 proposed pathways for amine oxidation: the amine substrate may bind to oxidised enzyme (E/FADox), leading to the release of product imine via a binary (1) or ternary (2) pathway. The relative contributions of these pathways cannot be determined directly by steady-state approaches. In following pathway 1, the unoccupied reduced enzyme (E/FADred) is generated, to which substrate may also bind. Reoxidation of the E/FADred–S species (pathway 3) bypasses direct regeneration of E/FADox, with the consequence that imine released subsequent to this step, whether through the binary or ternary pathways leading from E/FADred–imine, is a product of substrate binding to a second enzyme species Homo sapiens 4-phenylbutanal + NH3 + H2O2
-
 ?
benzylamine + H2O + O2 proposed pathways for amine oxidation: the amine substrate may bind to oxidised enzyme (E/FADox), leading to the release of product imine via a binary (1) or ternary (2) pathway. The relative contributions of these pathways cannot be determined directly by steady-state approaches. In following pathway 1, the unoccupied reduced enzyme (E/FADred) is generated, to which substrate may also bind. Reoxidation of the E/FADred–S species (pathway 3) bypasses direct regeneration of E/FADox, with the consequence that imine released subsequent to this step, whether through the binary or ternary pathways leading from E/FADred–imine, is a product of substrate binding to a second enzyme species Homo sapiens benzaldehyde + NH3 + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
MAO-B
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information kinetic constants for pure hMAO-B oxidising different substrates in the presence of reversible competitive inhibitors or reversible non-competitive/mixed inhibitors Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information kinetic constants for pure hMAO-B oxidising different substrates in the presence of reversible competitive inhibitors or reversible non-competitive/mixed inhibitors Homo sapiens
0.00298
-
 di(2-hydroxyethyl)methyldodecylammonium 30°C, pH 7, oxidative half-reaction, substrate: 2-phenylethylamine or benzylamine Homo sapiens
0.00374
-
 di(2-hydroxyethyl)methyldodecylammonium 30°C, pH 7, oxidative half-reaction, substrate: 4-phenylbutylamine Homo sapiens
0.008
-
 2-(5,7-dibromobenzofuran-2-yl)-imidazoline 30°C, pH 7, oxidative half-reaction, substrate: benzylamine Homo sapiens
0.0177
-
 amitriptyline 30°C, pH 7, oxidative half-reaction, substrate: 2-phenylethylamine Homo sapiens
0.0652
-
 2-(4,5-dihydroimidazol-2-yl)-isoquinoline 30°C, pH 7, oxidative half-reaction, substrate: 2-phenylethylamine Homo sapiens
0.0799
-
 di(2-hydroxyethyl)methyldodecylammonium 30°C, pH 7, reductive half-reaction, substrate: 2-phenylethylamine, benzylamine or 4-phenylbutylamine Homo sapiens
0.0817
-
 2-(4,5-dihydroimidazol-2-yl)-quinoline 30°C, pH 7, oxidative half-reaction, substrate: 2-phenylethylamine Homo sapiens
0.114
-
 2-(5,7-dibromobenzofuran-2-yl)-imidazoline 30°C, pH 7, reductive half-reaction, substrate: benzylamine Homo sapiens
0.385
-
 2-(4,5-dihydroimidazol-2-yl)-quinoline 30°C, pH 7, reductive half-reaction, substrate: 2-phenylethylamine Homo sapiens
0.506
-
 (+)-amphetamine 30°C, pH 7, oxidative half-reaction, substrate: 2-phenylethylamine or benzylamine Homo sapiens
0.513
-
 2-(4,5-dihydroimidazol-2-yl)-isoquinoline 30°C, pH 7, reductive half-reaction, substrate: 2-phenylethylamine Homo sapiens
0.55
-
 amitriptyline 30°C, pH 7, reductive half-reaction, substrate: 2-phenylethylamine Homo sapiens
2.56
-
 (+)-amphetamine 30°C, pH 7, reductive half-reaction, substrate: 2-phenylethylamine or benzylamine Homo sapiens