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MetaCyc Enzyme: amine oxidase A

Gene: MAOA Accession Number: HS01798 (MetaCyc)

Synonyms: monoamine oxidase, MAO-A, monoamine oxidase A

Species: Homo sapiens

Summary:
Monoamine oxidase A is involved in the degradation of various biogenic amine hormones such as dopamine, norepinephrine, and serotonin.

The recombinant enzyme from human liver has been expressed at high level in Komagataella pastoris and purified. The apparent molecular mass was determined by electrospray mass spectrometry [Li02d]. It has also been expressed in Saccharomyces cerevisiae [Weyler90]. The crystal structure of the human enzyme had been determined and was found to be unique in its crystallization as a monomer and its hydrodynamic behavior in solution as a monomer [De05]. The cofactor (prosthetic group) FAD is covalently attached [Weyler90]. Reviewed in [Nagatsu04].

Deficiency of this enzyme results in Brunner syndrome.

Gene Citations: [Chen91d]

Locations: mitochondrial membrane

Map Position: [41,794,572 -> 41,864,469] (27.57 centisomes)

Molecular Weight of Polypeptide: 59.682 kD (from nucleotide sequence), 60.512 kD (experimental) [Li02d ]

Unification Links: ArrayExpress:P21397 , Ensembl:ENSG00000094598 , Entrez-gene:4128 , Entrez:AAA59547 , Entrez:AAA59548 , Entrez:AAA59549 , Entrez:AAB46385 , Entrez:AAD14113 , Entrez:AAD14361 , Entrez:AAH08064 , GeneCards:MAOA , GO:0004041 , Mint:MINT-4054607 , OMIM:309850 , PhosphoSite:P21397 , PhylomeDB:P21397 , Pride:P21397 , Protein Model Portal:P21397 , RefSeq:NM_000240 , RefSeq:NP_000231 , SMR:P21397 , String:9606.ENSP00000340684 , UCSC Human Genome:NM_000240 , UniGene:183109 , UniProt:P21397

Relationship Links: Entrez-Nucleotide:PART-OF:BC008064 , Entrez-Nucleotide:PART-OF:M68840 , Entrez-Nucleotide:PART-OF:M68857 , Entrez-Nucleotide:PART-OF:M69226 , Entrez-Nucleotide:PART-OF:M89636 , InterPro:IN-FAMILY:IPR001613 , InterPro:IN-FAMILY:IPR002937 , PDB:Structure:1H8Q , PDB:Structure:2BXR , PDB:Structure:2BXS , PDB:Structure:2Z5X , PDB:Structure:2Z5Y , Pfam:IN-FAMILY:PF01593 , Prints:IN-FAMILY:PR00757

Gene-Reaction Schematic: ?

GO Terms:

Cellular Component: GO:0044455 - mitochondrial membrane part [Pearce83]


Enzymatic reaction of: dopamine oxidase (amine oxidase A)

EC Number: 1.4.3.4

dopamine + H2O + oxygen <=> 3,4-dihydroxyphenylacetaldehyde + ammonium + hydrogen peroxide

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Alternative Substrates for dopamine: kynuramine [Li02d , Weyler90 ] , tyramine [Pearce83 ] , serotonin [Li02d ] , 2-phenylethylamine [Li02d ]

In Pathways: dopamine degradation

Summary:
Monoamine oxidase catalyzes the oxidation of biologically important amines, including the neurotransmitters dopamine, noradrenaline and serotonin.

Cofactors or Prosthetic Groups: FAD [Li02d]

Inhibitors (Competitive): phentermine [Nandigama02]

Inhibitors (Unknown Mechanism): octylglucoside [Pearce83] , clorgyline [Tsugeno97, Weyler90] , (R)-amphetamine [Weyler90] , (S)-amphetamine [Weyler90]

Kinetic Parameters:

Substrate
Km (μM)
Citations
dopamine
249.0
[Li02d]


Enzymatic reaction of: serotonin oxidase (amine oxidase A)

EC Number: 1.4.3.4

serotonin + oxygen + H2O <=> 5-hydroxyindole acetaldehyde + ammonium + hydrogen peroxide

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: serotonin degradation

Cofactors or Prosthetic Groups: FAD [Li02d]


Enzymatic reaction of: monoamine oxidase (amine oxidase A)

EC Number: 1.4.3.4

a monoamine + H2O + oxygen <=> an aldehyde + a primary amine + hydrogen peroxide

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Cofactors or Prosthetic Groups: FAD [Li02d]


References

Chen91d: Chen ZY, Hotamisligil GS, Huang JK, Wen L, Ezzeddine D, Aydin-Muderrisoglu N, Powell JF, Huang RH, Breakefield XO, Craig I (1991). "Structure of the human gene for monoamine oxidase type A." Nucleic Acids Res 19(16);4537-41. PMID: 1886775

De05: De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A (2005). "Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B." Proc Natl Acad Sci U S A 102(36);12684-9. PMID: 16129825

Li02d: Li M, Hubalek F, Newton-Vinson P, Edmondson DE (2002). "High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae." Protein Expr Purif 24(1);152-62. PMID: 11812236

Nagatsu04: Nagatsu T (2004). "Progress in monoamine oxidase (MAO) research in relation to genetic engineering." Neurotoxicology 25(1-2);11-20. PMID: 14697876

Nandigama02: Nandigama RK, Newton-Vinson P, Edmondson DE (2002). "Phentermine inhibition of recombinant human liver monoamine oxidases A and B." Biochem Pharmacol 63(5);865-9. PMID: 11911838

Pearce83: Pearce LB, Roth JA (1983). "Human brain monoamine oxidase: solubilization and kinetics of inhibition by octylglucoside." Arch Biochem Biophys 224(2);464-72. PMID: 6870271

Tsugeno97: Tsugeno Y, Ito A (1997). "A key amino acid responsible for substrate selectivity of monoamine oxidase A and B." J Biol Chem 272(22);14033-6. PMID: 9162023

Weyler90: Weyler W, Titlow CC, Salach JI (1990). "Catalytically active monoamine oxidase type A from human liver expressed in Saccharomyces cerevisiae contains covalent FAD." Biochem Biophys Res Commun 173(3);1205-11. PMID: 2125217


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, BIOCYC13A.