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News About Monoamine_oxidase_B

20-September-2008 09:55:50 - B Monoamine oxidase B PDB rendering based on 1gos. Available structures: 1gos, 1oj9, 1oja, 1ojb, 1ojc, 1ojd, 1s2q, 1s2y, 1s3b, 1s3e, 2bk3, 2bk4, 2bk5, 2byb, 2c64, 2c65, 2c66, 2c67, 2c70, 2c72, 2c73, 2c75, 2c76 Identifiers Symbols MAOB; MGC26382 External IDs OMIM: 309860 MGI: 96916 HomoloGene: 20251 Gene ontology Molecular function: amine oxidase activity electron carrier activity oxidoreductase activity Cellular component: mitochondrion mitochondrial envelope mitochondrial inner membrane membrane integral to membrane Biological process: electron transport RNA expression pattern More reference expression data Orthologs Human Mouse Entrez 4129 109731 Ensembl ENSG00000069535 ENSMUSG00000040147 Uniprot P27338 Q14CG9 Refseq NM_000898 mRNA NP_000889 protein NM_172778 mRNA NP_766366 protein Location Chr X: 43.51 - 43.63 Mb Chr X: 15.87 - 15.93 Mb Pubmed search 1 2 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 ^ 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/S0161-813X0300114-1. 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. This article on a gene on the X chromosome and/or its associated protein is a stub. Retrieved from http://en..org/wiki/Monoamine_oxidase_B Categories: Genes on chromosome X | Human proteins | Chromosome X gene stubs Views Article Discussion this page History Personal tools Log in / create account Navigation Main page Contents Featured content Current events Random article Search Go Search Interaction Community portal Recent changes Contact Donate to Help Toolbox What links here Related changes Upload file Special pages Printable version Permanent link Cite this page This page was last modified on 8 July 2008, at 07:41

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