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Literature summary extracted from
- Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases (2009), Biochemistry, 48, 4220-4230.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.4.3.4 | development of expression systems for human MAO-B and MAO-A, e.g. overexpression in the outer mitochondrial membranes of a Pichia pastoris or a Saccharomyces cerevisiae yeast system | Homo sapiens |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.4.3.4 | MAO A, X-ray diffraction structure determination at 3.3 A resolution. The dimer structure of rat MAO A is more readily crystallized than its monomeric form | Rattus norvegicus |
| 1.4.3.4 | MAO-A, X-ray diffraction structure determination at 2.2 A resolution. MAO-B in complex with a range of inhibitors, X-ray diffraction structure determination at 1.65 A resolution. The human MAO-A monomer species is more likely to crystallize than its dimeric form | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.4.3.4 | I199F | the bulky Phe side chain impedes such conformational flexibility, reduces the space of the entrance cavity and interferes with the binding of MAO B-specific inhibitors | Homo sapiens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.3.4 | (2E,6E)-farnesol | - |
Homo sapiens |  |
| 1.4.3.4 | 1,4-diphenyl-2-butene | a component of polystyrene plasticware | Homo sapiens | |
| 1.4.3.4 | Clorgyline | - |
Homo sapiens | |
| 1.4.3.4 | Deprenyl | an acetylenic compound that forms covalent adducts with the N5 of the covalent FAD of MAO-B, pharmacologically inert as MAO-A inhibitor | Homo sapiens | |
| 1.4.3.4 | di(2-hydroxyethyl)methyldodecylammonium ion | a biocide, inhibits MAO-B | Homo sapiens | |
| 1.4.3.4 | isatin | - |
Homo sapiens | |
| 1.4.3.4 | mofegiline | a vinyl fluoroamine | Homo sapiens | |
| 1.4.3.4 | additional information | inhibitor binding affects the active site structures of MAO-A and MAO-B, overview | Homo sapiens | |
| 1.4.3.4 | additional information | inhibitor binding affects the active site structures of MAO A and MAO B, overview | Rattus norvegicus | |
| 1.4.3.4 | N-(2-aminoethyl)-p-chlorobenzamide | - |
Homo sapiens | |
| 1.4.3.4 | oleamide | inhibits MAO B | Homo sapiens | |
| 1.4.3.4 | rasagiline | an acetylenic compound that forms covalent adducts with the N5 of the covalent FAD of MAO-B, pharmacologically inert as MAO-A inhibitor. A rasagiline analog methylated on the amino moiety of the propargyline chain connecting the inhibitor to the flavin loses this characteristic specificity for MAO-B | Homo sapiens | |
| 1.4.3.4 | safinamide | a very specific MAO B non-covalent inhibitor, may function effectively as a neuroprotectant | Homo sapiens | |
| 1.4.3.4 | tranylcypromine | - |
Homo sapiens | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.4.3.4 | mitochondrial outer membrane | both MAO A and MAO B are membrane-associated enzymes that are located specifically to the outer mitochondrial membrane | Mus musculus | 5741 | - |
| 1.4.3.4 | mitochondrial outer membrane | both MAO A and MAO B are membrane-associated enzymes that are located specifically to the outer mitochondrial membrane | Rattus norvegicus | 5741 | - |
| 1.4.3.4 | mitochondrial outer membrane | both MAO A and MAO B are membrane-associated enzymes that are located specifically to the outer mitochondrial membrane | Bos taurus | 5741 | - |
| 1.4.3.4 | mitochondrial outer membrane | both MAO-A and MAO-B are membrane-associated enzymes that are located specifically to the outer mitochondrial membrane | Homo sapiens | 5741 | - |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.4.3.4 | Bos taurus | - |
MAO A and MAO B are encoded by separate genes | - |
| 1.4.3.4 | Homo sapiens | - |
MAO-A and MAO-B are encoded by separate genes | - |
| 1.4.3.4 | Mus musculus | - |
MAO A and MAO B are encoded by separate genes | - |
| 1.4.3.4 | Rattus norvegicus | - |
MAO A and MAO B are encoded by separate genes | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.4.3.4 | native MAO B from liver | Bos taurus |
| 1.4.3.4 | purification of large quantities of recombinant enzyme from Pichia pastoris or Saccharomyces cerevisiae. Native MAO-A from placenta | Homo sapiens |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.4.3.4 | RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 | reaction mechanism of C-H bond cleavage, MAO B shows H tunneling to contribute in the H transfer step, overview | Bos taurus | |
| 1.4.3.4 | RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 | reaction mechanism of C-H bond cleavage, overview | Mus musculus | |
| 1.4.3.4 | RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 | reaction mechanism of C-H bond cleavage, overview | Rattus norvegicus | |
| 1.4.3.4 | RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 | reaction mechanism of C-H bond cleavage, overview. MAO oxidation of benzylamines and phenethylamines exhibit large deuterium kinetic isotope effects showing, in most instances, that C-H bond cleavage is rate limiting in catalysis | Homo sapiens |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.4.3.4 | liver | - |
Bos taurus | - |
| 1.4.3.4 | placenta | MAO-A | Homo sapiens | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.4.3.4 | additional information | active site cavities in MAO-B and in MAO-A, in MAO-B the cavity is extended and substrate binding is likely to occur in proximity to the outer mitochondrial membrane surface region with the entrance loop, residues 99-110, involved in the access, overview | Homo sapiens | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.4.3.4 | dimer | MAO B is 100% dimeric, whereas MAO A exist only fractionally to 50% in its dimeric form | Rattus norvegicus |
| 1.4.3.4 | dimer | MAO-B is 100% dimeric, whereas MAO A exist only fractionally to 50% in its dimeric form | Homo sapiens |
| 1.4.3.4 | monomer | MAO A | Rattus norvegicus |
| 1.4.3.4 | monomer | MAO-A | Homo sapiens |
| 1.4.3.4 | More | MAO A three-dimensional structure, overview | Rattus norvegicus |
| 1.4.3.4 | More | MAO-B and MAO-A three-dimensional structures, overview | Homo sapiens |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.4.3.4 | MAO A | - |
Mus musculus |
| 1.4.3.4 | MAO A | - |
Homo sapiens |
| 1.4.3.4 | MAO A | - |
Rattus norvegicus |
| 1.4.3.4 | MAO A | - |
Bos taurus |
| 1.4.3.4 | MAO B | - |
Mus musculus |
| 1.4.3.4 | MAO B | - |
Homo sapiens |
| 1.4.3.4 | MAO B | - |
Rattus norvegicus |
| 1.4.3.4 | MAO B | - |
Bos taurus |
| 1.4.3.4 | monoamine oxidase A | - |
Mus musculus |
| 1.4.3.4 | monoamine oxidase A | - |
Homo sapiens |
| 1.4.3.4 | monoamine oxidase A | - |
Rattus norvegicus |
| 1.4.3.4 | monoamine oxidase A | - |
Bos taurus |
| 1.4.3.4 | monoamine oxidase B | - |
Mus musculus |
| 1.4.3.4 | monoamine oxidase B | - |
Homo sapiens |
| 1.4.3.4 | monoamine oxidase B | - |
Rattus norvegicus |
| 1.4.3.4 | monoamine oxidase B | - |
Bos taurus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.3.4 | FAD | covalently bound at the active site | Mus musculus | |
| 1.4.3.4 | FAD | covalently bound at the active site | Rattus norvegicus | |
| 1.4.3.4 | FAD | covalently bound at the active site | Bos taurus | |
| 1.4.3.4 | FAD | covalently bound at the active site, MAO-A and MAO-B binding structure, overview | Homo sapiens | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.4.3.4 | physiological function | MAO A and MAO B play roles in the oxidative catabolism of important amine neurotransmitters including serotonin, dopamine, and epinephrine. Inhibition of MAO B results in a protective effect from this cell-destructive bio-activation. MAO A functions specifically in the oxidative metabolism of serotonin although it also oxidizes dopamine effectively | Mus musculus |
| 1.4.3.4 | physiological function | MAO A and MAO B play roles in the oxidative catabolism of important amine neurotransmitters including serotonin, dopamine, and epinephrine. Inhibition of MAO B results in a protective effect from this cell-destructive bio-activation. MAO A functions specifically in the oxidative metabolism of serotonin although it also oxidizes dopamine effectively | Rattus norvegicus |
| 1.4.3.4 | physiological function | MAO A and MAO B play roles in the oxidative catabolism of important amine neurotransmitters including serotonin, dopamine, and epinephrine. Inhibition of MAO B results in a protective effect from this cell-destructive bio-activation. MAO A functions specifically in the oxidative metabolism of serotonin although it also oxidizes dopamine effectively | Bos taurus |
| 1.4.3.4 | physiological function | MAO-A and MAO-B play roles in the oxidative catabolism of important amine neurotransmitters including serotonin, dopamine, and epinephrine. Inhibition of MAO-B results in a protective effect from this cell-destructive bio-activation. MAO-A functions specifically in the oxidative metabolism of serotonin although it also oxidizes dopamine effectively | Homo sapiens |
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