The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

MAOB  -  monoamine oxidase B

Bos taurus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of MAOB

  • These data suggest that superoxide radicals are produced during the oxidation of MPTP by MAO-B and that the generation of H2O2 and .OH was secondary to the production of .O2-. It appears likely that the nigrostriatal toxicity of MPTP leading to Parkinson's disease-like syndrome may in part be mediated via these reactive oxygen species [1].
  • Although haloperidol and its 1,2,3,6-tetrahydropyridine dehydration product were not substrates for purified bovine liver MAO-B, both compounds were biotransformed to the pyridinium product by rat liver microsomal preparations [2].
  • The monoamine oxidase-B inhibitor L-deprenyl (Selegiline) is effective in treating Parkinson's disease and possibly Alzheimer's disease [3].
  • Our data also suggest that iron is capable of increasing the cytotoxicity of dopamine merely by increasing its rate of oxidation and without intervention of the monoamine oxidase B enzyme and, hence, both phenomenons may occur independently from each other in rat pheochromocytoma PC12 [4].

High impact information on MAOB


Biological context of MAOB


Anatomical context of MAOB

  • The corresponding kinetic values for this substrate in the retina and the choroid showed higher affinity for MAO A (Km 271 and 197 microM, respectively) than for MAO B (Km 861 and 404 microM, respectively) [12].
  • A new series of thirty derivatives of 2-(5-methoxy-1-methylindolyl)alkylamines has been synthesized and the compounds assayed as inhibitors of MAO-A and MAO-B from bovine brain mitochondria [13].
  • Monoamine oxidase B that has been synthesized by a reticulocyte lysate charged with bovine liver RNA will insert in a proteinase K-resistant form into isolated outer membranes from rat liver mitochondria [6].
  • Comparison of the decreases in apparent levels of MAO-B in rat liver mitochondrial membranes that were calculated from changes in relative catalytic activities with A and B specific substrates or changes in sensitivity to A-form specific reversible and irreversible inhibitors, all showed good quantitative correlation [14].

Associations of MAOB with chemical compounds

  • These results are discussed in terms of several mechanisms proposed for MAO catalysis and with previous structure-activity studies published with bovine liver MAO B [Walker, M. C., and Edmondson, D. E. (1994) Biochemistry 33, 7088-7098] [15].
  • All the compounds tested were substrates for ox liver monoamine oxidase-B (MAO-B), producing an aldehyde that could act as a substrate for ox liver aldehyde dehydrogenase and H2O2 as a result of oxidative cleavage which also released glycinamide, although their Michaelis-Menten parameters differed markedly [16].
  • [In a few samples we looked for but could not detect homovanillic acid or 3-methoxytyramine (O-methylated metabolites of DOPAC and DA respectively).] Deprenyl was about 44-72 times more potent an inhibitor of MAO than clorgyline when either DA or 5-HT was offered as substrate, suggesting that this MAO is of the MAOB type [17].
  • The contribution of monoamine oxidase (MAO) A, MAO B and semicarbazide-sensitive amine oxidase (SSAO) to the metabolism of dopamine in the bovine retina was studied [12].
  • The SSAO activities determined with 1 microM benzylamine were about half those determined for MAO-B [18].

Other interactions of MAOB


Analytical, diagnostic and therapeutic context of MAOB


  1. Generation of reactive oxygen species during the monoamine oxidase-catalyzed oxidation of the neurotoxicant, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine. Zang, L.Y., Misra, H.P. J. Biol. Chem. (1993) [Pubmed]
  2. Studies on the in vitro conversion of haloperidol to a potentially neurotoxic pyridinium metabolite. Subramanyam, B., Woolf, T., Castagnoli, N. Chem. Res. Toxicol. (1991) [Pubmed]
  3. L-deprenyl: nitric oxide production and dilation of cerebral blood vessels. Thomas, T., McLendon, C., Thomas, G. Neuroreport (1998) [Pubmed]
  4. Dopamine and iron induce apoptosis in PC12 cells. Velez-Pardo, C., Jimenez Del Rio, M., Verschueren, H., Ebinger, G., Vauquelin, G. Pharmacol. Toxicol. (1997) [Pubmed]
  5. Steroid regulation of monoamine oxidase activity in the adrenal medulla. Youdim, M.B., Banerjee, D.K., Kelner, K., Offutt, L., Pollard, H.B. FASEB J. (1989) [Pubmed]
  6. Ubiquitin is involved in the in vitro insertion of monoamine oxidase B into mitochondrial outer membranes. Zhaung, Z.P., McCauley, R. J. Biol. Chem. (1989) [Pubmed]
  7. Identification of imidazoline-receptor binding sites in cortex and medulla of the bovine adrenal gland. Colocalization with MAO-A and MAO-B. King, P.R., Gundlach, A.L., Louis, W.J. Ann. N. Y. Acad. Sci. (1999) [Pubmed]
  8. Selective inhibition of monoamine oxidase B by aminoethyl substituted benzyl ethers. Woodroofe, C.C., Mostashari, R., Lu, X., Ramsay, R.R., Silverman, R.B. J. Enzym. Inhib. (2000) [Pubmed]
  9. Structure-activity relationships in the oxidation of benzylamine analogues by bovine liver mitochondrial monoamine oxidase B. Walker, M.C., Edmondson, D.E. Biochemistry (1994) [Pubmed]
  10. Spectral and kinetic studies of imine product formation in the oxidation of p-(N,N-dimethylamino)benzylamine analogues by monoamine oxidase B. Edmondson, D.E., Bhattacharyya, A.K., Walker, M.C. Biochemistry (1993) [Pubmed]
  11. Stereoisomers of allenic amines as inactivators of monoamine oxidase type B. Stereochemical probes of the active site. Smith, R.A., White, R.L., Krantz, A. J. Med. Chem. (1988) [Pubmed]
  12. Contribution of different amine oxidases to the metabolism of dopamine in bovine retina. Fernández de Arriba, A., Lizcano, J.M., Balsa, D., Unzeta, M. Biochem. Pharmacol. (1991) [Pubmed]
  13. Acetylenic and allenic derivatives of 2-(5-methoxy-1-methylindolyl)alkylamines as selective inhibitors of MAO-A and MAO-B. Fernández García, C., Marco, J.L., Fernández-Alvarez, E. J. Neural Transm. Suppl. (1994) [Pubmed]
  14. Investigations of the mechanism of selective inhibition of type B mitochondrial monoamine oxidase by phosphatidylserine. Buckman, T.D., Eiduson, S., Boscia, R. Biochem. Pharmacol. (1983) [Pubmed]
  15. Structure-activity relationships in the oxidation of para-substituted benzylamine analogues by recombinant human liver monoamine oxidase A. Miller, J.R., Edmondson, D.E. Biochemistry (1999) [Pubmed]
  16. Interactions of some analogues of the anticonvulsant milacemide with monoamine oxidase. O'Brien, E.M., Dostert, P., Pevarello, P., Tipton, K.F. Biochem. Pharmacol. (1994) [Pubmed]
  17. Catabolism of dopamine and 5-hydroxytryptamine by monoamine oxidase in the ixodid tick, Amblyomma hebraeum. Kaufman, R., Sloley, D. Insect Biochem. Mol. Biol. (1996) [Pubmed]
  18. Monoamine oxidase and semicarbazide-sensitive amine oxidase activities in bovine eye. Fernandez de Arriba, A., Balsa, D., Tipton, K.F., Unzeta, M. J. Neural Transm. Suppl. (1990) [Pubmed]
  19. The primary structure of bovine monoamine oxidase type A. Comparison with peptide sequences of bovine monoamine oxidase type B and other flavoenzymes. Powell, J.F., Hsu, Y.P., Weyler, W., Chen, S.A., Salach, J., Andrikopoulos, K., Mallet, J., Breakefield, X.O. Biochem. J. (1989) [Pubmed]
  20. Studies on 4-benzyl-1-methyl-1,2,3,6-tetrahydropyridine, a nonneurotoxic analogue of the parkinsonian inducing agent 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine. Naiman, N., Rollema, H., Johnson, E., Castagnoli, N. Chem. Res. Toxicol. (1990) [Pubmed]
  21. Monoamine oxidase B isolated from bovine liver exists as large oligomeric complexes in vitro. Shiloff, B.A., Behrens, P.Q., Kwan, S.W., Lee, J.H., Abell, C.W. Eur. J. Biochem. (1996) [Pubmed]
  22. Secondary structure of monoamine oxidase by FTIR spectroscopy. Wouters, J., Ramsay, R., Goormaghtigh, E., Ruysschaert, J.M., Brasseur, R., Durant, F. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
WikiGenes - Universities