Monoamine oxidase B

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Monoamine oxidase B
PDB rendering based on 1gos.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols MAOB ; MGC26382
External IDs Template:OMIM5 Template:MGI HomoloGene20251
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Monoamine oxidase B, also known as MAOB, is a human gene.

The protein encoded by this gene belongs to the flavin monoamine oxidase family. It is an enzyme located in the mitochondrial outer membrane. It catalyzes the oxidative deamination of biogenic and xenobiotic amines and plays an important role in the metabolism of neuroactive and vasoactive amines in the central nervous sysytem and peripheral tissues. This protein preferentially degrades benzylamine and phenylethylamine.[1]

References

  1. "Entrez Gene: MAOB monoamine oxidase B".

Further reading

  • Edmondson DE, Binda C, Mattevi A (2004). "The FAD binding sites of human monoamine oxidases A and B.". Neurotoxicology. 25 (1–2): 63–72. doi:10.1016/S0161-813X(03)00114-1. PMID 14697881.
  • Kumar MJ, Andersen JK (2004). "Perspectives on MAO-B in aging and neurological disease: where do we go from here?". Mol. Neurobiol. 30 (1): 77–89. PMID 15247489.
  • Ghozlan A, Munnich A (2004). "[MAOB: a modifier gene in phenylketonuria?]". Med Sci (Paris). 20 (10): 929–32. PMID 15461973.
  • Zhu QS, Grimsby J, Chen K, Shih JC (1992). "Promoter organization and activity of human monoamine oxidase (MAO) A and B genes". J. Neurosci. 12 (11): 4437–46. PMID 1432104.
  • Grimsby J, Chen K, Wang LJ; et al. (1991). "Human monoamine oxidase A and B genes exhibit identical exon-intron organization". Proc. Natl. Acad. Sci. U.S.A. 88 (9): 3637–41. PMID 2023912.
  • Bach AW, Lan NC, Johnson DL; et al. (1988). "cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties". Proc. Natl. Acad. Sci. U.S.A. 85 (13): 4934–8. PMID 3387449.
  • Kochersperger LM, Parker EL, Siciliano M; et al. (1987). "Assignment of genes for human monoamine oxidases A and B to the X chromosome". J. Neurosci. Res. 16 (4): 601–16. doi:10.1002/jnr.490160403. PMID 3540317.
  • Wyatt RJ, Murphy DL, Belmaker R; et al. (1973). "Reduced monoamine oxidase activity in platelets: a possible genetic marker for vulnerability to schizophrenia". Science. 179 (76): 916–8. PMID 4687789.
  • Goldin LR, Gershon ES, Lake CR; et al. (1982). "Segregation and linkage studies of plasma dopamine-beta-hydroxylase (DBH), erythrocyte catechol-O-methyltransferase (COMT), and platelet monoamine oxidase (MAO): possible linkage between the ABO locus and a gene controlling DBH activity". Am. J. Hum. Genet. 34 (2): 250–62. PMID 6951409.
  • Denney RM, Fritz RR, Patel NT, Abell CW (1982). "Human liver MAO-A and MAO-B separated by immunoaffinity chromatography with MAO-B-specific monoclonal antibody". Science. 215 (4538): 1400–3. PMID 7063850.
  • Raddatz R, Parini A, Lanier SM (1996). "Imidazoline/guanidinium binding domains on monoamine oxidases. Relationship to subtypes of imidazoline-binding proteins and tissue-specific interaction of imidazoline ligands with monoamine oxidase B.". J. Biol. Chem. 270 (46): 27961–8. PMID 7499273.
  • Woo JC, Silverman RB (1994). "Observation of two different chromophores in the resting state of monoamine oxidase B by fluorescence spectroscopy". Biochem. Biophys. Res. Commun. 202 (3): 1574–8. doi:10.1006/bbrc.1994.2111. PMID 8060341.
  • Wu HF, Chen K, Shih JC (1993). "Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines". Mol. Pharmacol. 43 (6): 888–93. PMID 8316221.
  • Chen K, Wu HF, Shih JC (1993). "The deduced amino acid sequences of human platelet and frontal cortex monoamine oxidase B are identical". J. Neurochem. 61 (1): 187–90. PMID 8515265.
  • Fowler JS, Volkow ND, Wang GJ; et al. (1996). "Inhibition of monoamine oxidase B in the brains of smokers". Nature. 379 (6567): 733–6. doi:10.1038/379733a0. PMID 8602220.
  • Lenders JW, Eisenhofer G, Abeling NG; et al. (1996). "Specific genetic deficiencies of the A and B isoenzymes of monoamine oxidase are characterized by distinct neurochemical and clinical phenotypes". J. Clin. Invest. 97 (4): 1010–9. PMID 8613523.
  • Cesura AM, Gottowik J, Lahm HW; et al. (1996). "Investigation on the structure of the active site of monoamine oxidase-B by affinity labeling with the selective inhibitor lazabemide and by site-directed mutagenesis". Eur. J. Biochem. 236 (3): 996–1002. PMID 8665924.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.
  • Saura J, Bleuel Z, Ulrich J; et al. (1997). "Molecular neuroanatomy of human monoamine oxidases A and B revealed by quantitative enzyme radioautography and in situ hybridization histochemistry". Neuroscience. 70 (3): 755–74. PMID 9045087.
  • Checkoway H, Franklin GM, Costa-Mallen P; et al. (1998). "A genetic polymorphism of MAO-B modifies the association of cigarette smoking and Parkinson's disease". Neurology. 50 (5): 1458–61. PMID 9596006.


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