Literature summary for 1.4.3.4 extracted from

Edmondson, D.E.; Binda, C.; Wang, J.; Upadhyay, A.K.; Mattevi, A.
Molecular and mechanistic properties of the membrane-bound mitochondrial monoamine oxidases (2009), Biochemistry, 48, 4220-4230.

Search for more literature for 1.4.3.4

Cloned(Commentary)

Cloned (Comment)	Organism
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)

Crystallization (Comment)	Organism
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
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

Protein Variants	Comment	Organism
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

Inhibitors	Comment	Organism	Structure
(2E,6E)-farnesol	-	Homo sapiens
1,4-diphenyl-2-butene	a component of polystyrene plasticware	Homo sapiens
Clorgyline	-	Homo sapiens
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
di(2-hydroxyethyl)methyldodecylammonium ion	a biocide, inhibits MAO-B	Homo sapiens
isatin	-	Homo sapiens
mofegiline	a vinyl fluoroamine	Homo sapiens
additional information	inhibitor binding affects the active site structures of MAO-A and MAO-B, overview	Homo sapiens
additional information	inhibitor binding affects the active site structures of MAO A and MAO B, overview	Rattus norvegicus
N-(2-aminoethyl)-p-chlorobenzamide	-	Homo sapiens
oleamide	inhibits MAO B	Homo sapiens
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
safinamide	a very specific MAO B non-covalent inhibitor, may function effectively as a neuroprotectant	Homo sapiens
tranylcypromine	-	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
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	-
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	-
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	-
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

Organism	UniProt	Comment	Textmining
Bos taurus	-	MAO A and MAO B are encoded by separate genes	-
Homo sapiens	-	MAO-A and MAO-B are encoded by separate genes	-
Mus musculus	-	MAO A and MAO B are encoded by separate genes	-
Rattus norvegicus	-	MAO A and MAO B are encoded by separate genes	-

Purification (Commentary)

Purification (Comment)	Organism
native MAO B from liver	Bos taurus
purification of large quantities of recombinant enzyme from Pichia pastoris or Saccharomyces cerevisiae. Native MAO-A from placenta	Homo sapiens

Reaction

Reaction	Comment	Organism	Reaction ID
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	a
RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2	reaction mechanism of C-H bond cleavage, overview	Mus musculus	a
RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2	reaction mechanism of C-H bond cleavage, overview	Rattus norvegicus	a
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	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Bos taurus	-
placenta	MAO-A	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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

Subunits	Comment	Organism
dimer	MAO B is 100% dimeric, whereas MAO A exist only fractionally to 50% in its dimeric form	Rattus norvegicus
dimer	MAO-B is 100% dimeric, whereas MAO A exist only fractionally to 50% in its dimeric form	Homo sapiens
monomer	MAO A	Rattus norvegicus
monomer	MAO-A	Homo sapiens
More	MAO A three-dimensional structure, overview	Rattus norvegicus
More	MAO-B and MAO-A three-dimensional structures, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
MAO A	-	Mus musculus
MAO A	-	Homo sapiens
MAO A	-	Rattus norvegicus
MAO A	-	Bos taurus
MAO B	-	Mus musculus
MAO B	-	Homo sapiens
MAO B	-	Rattus norvegicus
MAO B	-	Bos taurus
monoamine oxidase A	-	Mus musculus
monoamine oxidase A	-	Homo sapiens
monoamine oxidase A	-	Rattus norvegicus
monoamine oxidase A	-	Bos taurus
monoamine oxidase B	-	Mus musculus
monoamine oxidase B	-	Homo sapiens
monoamine oxidase B	-	Rattus norvegicus
monoamine oxidase B	-	Bos taurus

Cofactor

Cofactor	Comment	Organism	Structure
FAD	covalently bound at the active site	Mus musculus
FAD	covalently bound at the active site	Rattus norvegicus
FAD	covalently bound at the active site	Bos taurus
FAD	covalently bound at the active site, MAO-A and MAO-B binding structure, overview	Homo sapiens

General Information

General Information	Comment	Organism
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
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
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
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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Release 2023.1 (January 2023)