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Identification
HMDB Protein ID HMDBP00169
Secondary Accession Numbers
  • 5401
  • HMDBP03761
Name Amine oxidase [flavin-containing] A
Synonyms
  1. MAO-A
  2. Monoamine oxidase type A
Gene Name MAOA
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity
Specific Function Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine.
Pathways
  • 3-Phosphoglycerate dehydrogenase deficiency
  • Alcoholism
  • Alkaptonuria
  • Amphetamine addiction
  • Arginine and proline metabolism
  • Citalopram Action Pathway
  • Citalopram Metabolism Pathway
  • Cocaine addiction
  • Dihydropyrimidine Dehydrogenase Deficiency (DHPD)
  • Dimethylglycine Dehydrogenase Deficiency
  • Dimethylglycine Dehydrogenase Deficiency
  • Disulfiram Action Pathway
  • Dopamine beta-hydroxylase deficiency
  • Dopaminergic synapse
  • Drug metabolism - cytochrome P450
  • Glycine and Serine Metabolism
  • Glycine, serine and threonine metabolism
  • Hawkinsinuria
  • Histidine Metabolism
  • Histidine metabolism
  • Histidinemia
  • Hyperglycinemia, non-ketotic
  • Monoamine oxidase-a deficiency (MAO-A)
  • Non Ketotic Hyperglycinemia
  • Phenylalanine metabolism
  • Sarcosinemia
  • Serotonergic synapse
  • Tryptophan metabolism
  • Tyrosine Metabolism
  • Tyrosine metabolism
  • Tyrosinemia Type I
  • Tyrosinemia, transient, of the newborn
Reactions
RCH(2)NHR' + Water + Oxygen → RCHO + R'NH(2) + Hydrogen peroxide details
Tryptamine + Water + Oxygen → Indoleacetaldehyde + Ammonia + Hydrogen peroxide details
Tyramine + Water + Oxygen → 4-Hydroxyphenylacetaldehyde + Ammonia + Hydrogen peroxide details
Aminoacetone + Water + Oxygen → Pyruvaldehyde + Ammonia + Hydrogen peroxide details
Norepinephrine + Water + Oxygen → 3,4-Dihydroxymandelaldehyde + Ammonia + Hydrogen peroxide details
Phenylethylamine + Oxygen + Water → Phenylacetaldehyde + Ammonia + Hydrogen peroxide details
Serotonin + Water + Oxygen → 5-Hydroxyindoleacetaldehyde + Ammonia + Hydrogen peroxide details
Epinephrine + Water + Oxygen → 3,4-Dihydroxymandelaldehyde + Methylamine + Hydrogen peroxide details
N-Acetylputrescine + Water + Oxygen → N4-Acetylaminobutanal + Ammonia + Hydrogen peroxide details
Dopamine + Water + Oxygen → 3,4-Dihydroxyphenylacetaldehyde + Ammonia + Hydrogen peroxide details
1-Methylhistamine + Water + Oxygen → Methylimidazole acetaldehyde + Ammonia + Hydrogen peroxide details
3-Methoxytyramine + Water + Oxygen → Homovanillin + Hydrogen peroxide + Ammonia details
Normetanephrine + Water + Oxygen → 3-Methoxy-4-hydroxyphenylglycolaldehyde + Ammonia + Hydrogen peroxide details
Metanephrine + Water + Oxygen → 3-Methoxy-4-hydroxyphenylglycolaldehyde + Hydrogen peroxide + Methylamine details
3-Hydroxykynurenamine + Oxygen → Quinoline-4,8-diol + Ammonia + Hydrogen peroxide details
5-Hydroxykynurenamine + Water + Oxygen → 4,6-Dihydroxyquinoline + Ammonia + Hydrogen peroxide + Water details
Citalopram + Oxygen + Water → Citalopram aldehyde + Dimethylamine + Hydrogen peroxide details
N-Desmethylcitalopram + Oxygen + Water → Citalopram aldehyde + Methylamine + Hydrogen peroxide details
Didemethylcitalopram + Water + Oxygen → Citalopram aldehyde + Ammonia + Hydrogen peroxide details
GO Classification
Biological Process
small molecule metabolic process
neurotransmitter biosynthetic process
xenobiotic metabolic process
behavior
cellular biogenic amine metabolic process
dopamine catabolic process
neurotransmitter catabolic process
neurotransmitter secretion
phenylethylamine metabolic process
serotonin metabolic process
Cellular Component
mitochondrial outer membrane
integral to membrane
Function
catalytic activity
oxidoreductase activity
Molecular Function
primary amine oxidase activity
serotonin binding
flavin adenine dinucleotide binding
Process
metabolic process
oxidation reduction
Cellular Location
  1. Cytoplasmic side
  2. Mitochondrion outer membrane
  3. Single-pass type IV membrane protein
Gene Properties
Chromosome Location X
Locus Xp11.3
SNPs MAOA
Gene Sequence
>1584 bp
ATGGAGAATCAAGAGAAGGCGAGTATCGCGGGCCACATGTTCGACGTAGTCGTGATCGGA
GGTGGCATTTCAGGACTATCTGCTGCCAAACTCTTGACTGAATATGGCGTTAGTGTTTTG
GTTTTAGAAGCTCGGGACAGGGTTGGAGGAAGAACATATACTATAAGGAATGAGCATGTT
GATTACGTAGATGTTGGTGGAGCTTATGTGGGACCAACCCAAAACAGAATCTTACGCTTG
TCTAAGGAGCTGGGCATAGAGACTTACAAAGTGAATGTCAGTGAGCGTCTCGTTCAATAT
GTCAAGGGGAAAACATATCCATTTCGGGGCGCCTTTCCACCAGTATGGAATCCCATTGCA
TATTTGGATTACAATAATCTGTGGAGGACAATAGATAACATGGGGAAGGAGATTCCAACT
GATGCACCCTGGGAGGCTCAACATGCTGACAAATGGGACAAAATGACCATGAAAGAGCTC
ATTGACAAAATCTGCTGGACAAAGACTGCTAGGCGGTTTGCTTATCTTTTTGTGAATATC
AATGTGACCTCTGAGCCTCACGAAGTGTCTGCCCTGTGGTTCTTGTGGTATGTGAAGCAG
TGCGGGGGCACCACTCGGATATTCTCTGTCACCAATGGTGGCCAGGAACGGAAGTTTGTA
GGTGGATCTGGTCAAGTGAGCGAACGGATAATGGACCTCCTCGGAGACCAAGTGAAGCTG
AACCATCCTGTCACTCACGTTGACCAGTCAAGTGACAACATCATCATAGAGACGCTGAAC
CATGAACATTATGAGTGCAAATACGTAATTAATGCGATCCCTCCGACCTTGACTGCCAAG
ATTCACTTCAGACCAGAGCTTCCAGCAGAGAGAAACCAGTTAATTCAGCGTCTTCCAATG
GGAGCTGTCATTAAGTGCATGATGTATTACAAGGAGGCCTTCTGGAAGAAGAAGGATTAC
TGTGGCTGCATGATCATTGAAGATGAAGATGCTCCAATTTCAATAACCTTGGATGACACC
AAGCCAGATGGGTCACTGCCTGCCATCATGGGCTTCATTCTTGCCCGGAAAGCTGATCGA
CTTGCTAAGCTACATAAGGAAATAAGGAAGAAGAAAATCTGTGAGCTCTATGCCAAAGTG
CTGGGATCCCAAGAAGCTTTACATCCAGTGCATTATGAAGAGAAGAACTGGTGTGAGGAG
CAGTACTCTGGGGGCTGCTACACGGCCTACTTCCCTCCTGGGATCATGACTCAATATGGA
AGGGTGATTCGTCAACCCGTGGGCAGGATTTTCTTTGCGGGCACAGAGACTGCCACAAAG
TGGAGCGGCTACATGGAAGGGGCAGTTGAGGCTGGAGAACGAGCAGCTAGGGAGGTCTTA
AATGGTCTCGGGAAGGTGACCGAGAAAGACATCTGGGTACAAGAACCTGAATCAAAGGAC
GTTCCAGCGGTAGAAATCACCCACACCTTCTGGGAAAGGAACCTGCCCTCTGTTTCTGGC
CTGCTGAAGATCATTGGATTTTCCACATCAGTAACTGCCCTGGGGTTTGTGCTGTACAAA
TACAAGCTCCTGCCACGGTCTTGA
Protein Properties
Number of Residues 527
Molecular Weight 59681.27
Theoretical pI 7.862
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Amine oxidase [flavin-containing] A
MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHV
DYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIA
YLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNI
NVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKL
NHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPM
GAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADR
LAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYG
RVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKD
VPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS
GenBank ID Protein 187355
UniProtKB/Swiss-Prot ID P21397
UniProtKB/Swiss-Prot Entry Name AOFA_HUMAN
PDB IDs
GenBank Gene ID M69226
GeneCard ID MAOA
GenAtlas ID MAOA
HGNC ID HGNC:6833
References
General References
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  4. Bach AW, Lan NC, Johnson DL, Abell CW, Bembenek ME, Kwan SW, Seeburg PH, Shih JC: cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4934-8. [PubMed:3387449 ]
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  6. Wu HF, Chen K, Shih JC: Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines. Mol Pharmacol. 1993 Jun;43(6):888-93. [PubMed:8316221 ]
  7. Hsu YP, Weyler W, Chen S, Sims KB, Rinehart WB, Utterback MC, Powell JF, Breakefield XO: Structural features of human monoamine oxidase A elucidated from cDNA and peptide sequences. J Neurochem. 1988 Oct;51(4):1321-4. [PubMed:3418353 ]
  8. Chen ZY, Hotamisligil GS, Huang JK, Wen L, Ezzeddine D, Aydin-Muderrisoglu N, Powell JF, Huang RH, Breakefield XO, Craig I, et al.: Structure of the human gene for monoamine oxidase type A. Nucleic Acids Res. 1991 Aug 25;19(16):4537-41. [PubMed:1886775 ]
  9. Denney RM: The promoter of the human monoamine oxidase A gene. Prog Brain Res. 1995;106:57-66. [PubMed:8584674 ]
  10. Denney RM, Sharma A, Dave SK, Waguespack A: A new look at the promoter of the human monoamine oxidase A gene: mapping transcription initiation sites and capacity to drive luciferase expression. J Neurochem. 1994 Sep;63(3):843-56. [PubMed:7519662 ]
  11. Chen SA, Weyler W: Partial amino acid sequence analysis of human placenta monoamine oxidase A and bovine liver monoamine oxidase B. Biochem Biophys Res Commun. 1988 Oct 14;156(1):445-50. [PubMed:3178846 ]
  12. Weyler W: Monoamine oxidase A from human placenta and monoamine oxidase B from bovine liver both have one FAD per subunit. Biochem J. 1989 Jun 15;260(3):725-9. [PubMed:2764901 ]
  13. Li M, Hubalek F, Newton-Vinson P, Edmondson DE: High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae. Protein Expr Purif. 2002 Feb;24(1):152-62. [PubMed:11812236 ]
  14. De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A: 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. 2005 Sep 6;102(36):12684-9. Epub 2005 Aug 29. [PubMed:16129825 ]
  15. Brunner HG, Nelen M, Breakefield XO, Ropers HH, van Oost BA: Abnormal behavior associated with a point mutation in the structural gene for monoamine oxidase A. Science. 1993 Oct 22;262(5133):578-80. [PubMed:8211186 ]
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