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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-06-23 18:05:55
Primary Accession Number DB01367
Secondary Accession Number
  • EXPT02758
Name Rasagiline
Drug Type
  • Approved
  • Small Molecule
Description Rasagiline is an irreversible inhibitor of monoamine oxidase and is used as a monotherapy in early Parkinson's disease or as an adjunct therapy in more advanced cases.
Synonyms
  1. RAS
Brand Names
  1. Azilect
Brand Mixtures Not Available
Chemical IUPAC Name (1R)-N-prop-2-ynyl-2,3-dihydro-1H-inden-1-amine
Chemical Formula C12H13N
Chemical Structure Structure
CAS Registry Number 136236-51-6
InChI Identifier InChI=1/C12H13N/c1-2-9-13-12-8-7-10-5-3-4-6-11(10)12/h1,3-6,12-13H,7-9H2/t12-/m1/s1
InChI Key RUOKEQAAGRXIBM-GFCCVEGCBG
KEGG Drug D02562 Link Image
KEGG Compound Not Available
PubChem Compound 3052776 Link Image
PubChem Substance 10056118 Link Image
ChEBI ID Not Available
PharmGKB ID Not Available
HET ID RAS Link Image
GenBank ID Not Available
Drug ID Number [DIN] 02284642 Link Image
RxList Link http://www.rxlist.com/cgi/generic/azilect.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Rasagiline Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 171.2383
Monoisotopic Molecular Weight 171.1048
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.49e-02 mg/mL Calculated using ALOGPS
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP 2.26 Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS -3.84 Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Show Link Image | Download Link Image
SDF File Show Link Image | Download Link Image
PDB File Show Link Image | Download Link Image
2D Structure
3D Structure
Experimental PDB ID 1S2Q Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES C#CCN[C@@H]1CCC2=CC=CC=C12
Canonical SMILES C#CCNC1CCC2=CC=CC=C12
Drug Category
  • Monoamine Oxidase Inhibitors
  • Neuroprotective Agents
ATC Codes
AHFS Codes
  • 28:92.00
Indication For the treatment of the signs and symptoms of idiopathic Parkinsons disease as initial monotherapy and as adjunct therapy to levodopa.
Pharmacology Rasagiline, an irreversible inhibitor of monoamine oxidase (MAO). MAO, a flavin-containing enzyme, is classified into two major molecular species, A and B, and is localized in mitochondrial membranes throughout the body in nerve terminals, brain, liver and intestinal mucosa. MAO regulates the metabolic degradation of catecholamines and serotonin in the CNS and peripheral tissues. MAO-B is the major form in the human brain. In ex vivo animal studies in brain, liver and intestinal tissues rasagiline was shown to be a potent, irreversible monoamine oxidase type B (MAO-B) selective inhibitor. Rasagiline at the recommended therapeutic dose was also shown to be a potent and irreversible inhibitor of MAO-B in platelets. The selectivity of rasagiline for inhibiting only MAO-B (and not MAO-A) in humans and the sensitivity to tyramine during rasagiline treatment at any dose has not been sufficiently characterized to avoid restriction of dietary tyramine and amines contained in medications.
Mechanism of Action The precise mechanisms of action of rasagiline are unknown. One mechanism is believed to be related to its MAO-B inhibitory activity, which causes an increase in extracellular levels of dopamine in the striatum. The elevated dopamine level and subsequent increased dopaminergic activity are likely to mediate rasagilines beneficial effects seen in models of dopaminergic motor dysfunction.
Absorption Rasagiline is rapidly absorbed following oral administration. The absolute bioavailability of rasagiline is about 36%.
Toxicity Signs and symptoms of overdosage may include, alone or in combination, any of the following: drowsiness, dizziness, faintness, irritability, hyperactivity, agitation, severe headache, hallucinations, trismus, opisthotonos, convulsions, and coma; rapid and irregular pulse, hypertension, hypotension and vascular collapse; precordial pain, respiratory depression and failure, hyperpyrexia, diaphoresis, and cool, clammy skin.
Protein Binding Plasma protein binding ranges from 88-94% with mean extent of binding of 61-63% to human albumin over the concentration range of 1-100 ng/ml.
Biotransformation Rasagiline undergoes almost complete biotransformation in the liver prior to excretion. In vitro experiments indicate that both routes of rasagiline metabolism are dependent on the cytochrome P450 (CYP) system, with CYP 1A2 being the major isoenzyme involved in rasagiline metabolism.
Half Life Rasagiline has a mean steady-state half life of 3 hours but there is no correlation of pharmacokinetics with its pharmacological effect because of its irreversible inhibition of MAO-B.
Dosage Forms
Form Route
Tablet Oral
Tablet Oral
Tablet Oral
Patient Information Show Link Image
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions
Drug Interaction
Altretamine Risk of severe hypotension
Amitriptyline Possibility of severe adverse effects
Amoxapine Possibility of severe adverse effects
Amphetamine Possible hypertensive crisis
Atomoxetine Possible severe adverse reaction with this combination
Benzphetamine Possible hypertensive crisis
Bupropion Possible severe adverse reaction with this combination
Buspirone Possible blood pressure elevation
Ciprofloxacin Ciprofloxacin increases effect/toxicity of rasagiline
Citalopram Possible severe adverse reaction with this combination
Clomipramine Possibility of severe adverse effects
Cyclobenzaprine Increased risk of toxicity with this association
Desipramine Possibility of severe adverse effects
Dexfenfluramine Possible hypertensive crisis
Dextroamphetamine Possible hypertensive crisis
Dextromethorphan Possible severe adverse reaction
Diethylpropion Possible hypertensive crisis
Dobutamine Increased arterial pressure
Dopamine Increased arterial pressure
Doxepin Possibility of severe adverse effects
Duloxetine Possible severe adverse reaction with this combination
Ephedra Increased arterial pressure
Ephedrine Increased arterial pressure
Epinephrine Increased arterial pressure
Escitalopram Possible severe adverse reaction with this combination
Fenfluramine Possible hypertensive crisis
Fenoterol Increased arterial pressure
Fluoxetine Possible severe adverse reaction with this combination
Fluvoxamine Possible severe adverse reaction with this combination
Ginseng Ginseng increases the effect and toxicity of MAOI
Imipramine Possibility of severe adverse effects
Isoproterenol Increased arterial pressure
Mazindol Possible hypertensive crisis
Meperidine Potentiall fatal adverse effects
Mephentermine Increased arterial pressure
Metaraminol Increased arterial pressure
Methamphetamine Possible hypertensive crisis
Methoxamine Increased arterial pressure
Methylphenidate Possible severe adverse reaction with this combination
Midodrine Possible severe adverse reaction with this combination
Mirtazapine Possible severe adverse reaction with this combination
Nefazodone Possible severe adverse reaction with this combination
Norepinephrine Increased arterial pressure
Nortriptyline Possibility of severe adverse effects
Orciprenaline Increased arterial pressure
Paroxetine Possible severe adverse reaction with this combination
Phendimetrazine Possible hypertensive crisis
Phenmetrazine Possible hypertensive crisis
Phentermine Possible hypertensive crisis
Phenylephrine Increased arterial pressure
Phenylpropanolamine Increased arterial pressure
Pirbuterol Increased arterial pressure
Procaterol Increased arterial pressure
Protriptyline Possibility of severe adverse effects
Pseudoephedrine Increased arterial pressure
Salbutamol Increased arterial pressure
Sertraline Possible severe adverse reaction with this combination
Sibutramine Possible serotoninergic syndrome with this combination
St. John's Wort Increased risk of toxicity with this association
Terbutaline Increased arterial pressure
Tramadol Increased risk of seizures and serotonin syndrome
Trimipramine Possibility of severe adverse effects
Venlafaxine Possible severe adverse reaction with this combination
Food Interactions
  • Avoid alcohol and caffeine.
Pathways Not Available
General References
  1. Wikipedia Link Image
  2. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 1A2 (CYP1A2)
  2. Monoamine oxidase type A (MAO-A)
  3. Monoamine oxidase type B (MAO-B)
Targets
  1. Apoptosis regulator Bcl-2
  2. Amine oxidase [flavin-containing] B
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 1A2 (CYP1A2)
Enzyme 1 Gene Name CYP1A2
Enzyme 1 SwissProt ID P05177 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >P05177|CP1A2_HUMAN Cytochrome P450 1A2 - Homo sapiens (Human). 
MALSQSVPFSATELLLASAIFCLVFWVLKGLRPRVPKGLKSPPEPWGWPLLGHVLTLGKN
PHLALSRMSQRYGDVLQIRIGSTPVLVLSRLDTIRQALVRQGDDFKGRPDLYTSTLITDG
QSLTFSTDSGPVWAARRRLAQNALNTFSIASDPASSSSCYLEEHVSKEAKALISRLQELM
AGPGHFDPYNQVVVSVANVIGAMCFGQHFPESSDEMLSLVKNTHEFVETASSGNPLDFFP
ILRYLPNPALQRFKAFNQRFLWFLQKTVQEHYQDFDKNSVRDITGALFKHSKKGPRASGN
LIPQEKIVNLVNDIFGAGFDTVTTAISWSLMYLVTKPEIQRKIQKELDTVIGRERRPRLS
DRPQLPYLEAFILETFRHSSFLPFTIPHSTTRDTTLNGFYIPKKCCVFVNQWQVNHDPEL
WEDPSEFRPERFLTADGTAINKPLSEKMMLFGMGKRRCIGEVLAKWEIFLFLAILLQQLE
FSVPPGVKVDLTPIYGLTMKHARCEHVQARRFSIN
Phase 1 Metabolizing Enzyme 2 [top]
Enzyme 2 Name Monoamine oxidase type A (MAO-A)
Enzyme 2 Gene Name MAOA
Enzyme 2 SwissProt ID P21397 Link Image
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 Protein Sequence >sp|P21397|AOFA_HUMAN Amine oxidase [flavin-containing] 
MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHV
DYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIA
YLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNI
NVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKL
NHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPM
GAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADR
LAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYG
RVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKD
VPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS
Phase 1 Metabolizing Enzyme 3 [top]
Enzyme 3 Name Monoamine oxidase type B (MAO-B)
Enzyme 3 Gene Name MAOB
Enzyme 3 SwissProt ID P27338 Link Image
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 Protein Sequence >sp|P27338|AOFB_HUMAN Amine oxidase B 
SNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSYV
GPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWRT
MDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEVS
ALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQT
RENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYY
KEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEERL
KKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRI
YFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTTF
LERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV
Drug Target 1 [top]
Target 1 ID 273
Target 1 Name Apoptosis regulator Bcl-2
Target 1 Synonyms Not Available
Target 1 Gene Name BCL2
Target 1 Protein Sequence >Apoptosis regulator Bcl-2 
MAHAGRTGYDNREIVMKYIHYKLSQRGYEWDAGDVGAAPPGAAPAPGIFSSQPGHTPHPA
ASRDPVARTSPLQTPAAPGAAAGPALSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLH
LTPFTARGRFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDNIALWMTEY
LNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKTLLSLALVGACITLGAYLGHK
Target 1 Number of Residues 242
Target 1 Molecular Weight 26266
Target 1 Theoretical pI 7.32
Target 1 GO Classification
Function
Not Available
Process
regulation of biological process
regulation of physiological process
regulation of cellular physiological process
regulation of programmed cell death
regulation of apoptosis
Component
cell
membrane
Target 1 General Function Involved in BH3 domain binding
Target 1 Specific Function Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1)
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • None
Target 1 Transmembrane Regions
  • 212-233
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 179367 Link Image
Target 1 UniProtKB/Swiss-Prot ID P10415 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name BCL2_HUMAN Link Image
Target 1 PDB ID Not Available
Target 1 Cellular Location
  • Mitochondrion
  • mitochondrial outer membrane
  • nuclear membrane
  • single-pass membrane protein. Nucleus
Target 1 Gene Sequence >720 bp 
ATGGCGCACGCTGGGAGAACGGGGTACGACAACCGGGAGATAGTGATGAAGTACATCCAT
TATAAGCTGTCGCAGAGGGGCTACGAGTGGGATGCGGGAGATGTGGGCGCCGCGCCCCCG
GGGGCCGCCCCCGCACCGGGCATCTTCTCCTCCCAGCCCGGGCACACGCCCCATCCAGCC
GCATCCCGCGACCCGGTCGCCAGGACCTCGCCGCTGCAGACCCCGGCTGCCCCCGGCGCC
GCCGCGGGGCCTGCGCTCAGCCCGGTGCCACCTGTGGTCCACCTGGCCCTCCGCCAAGCC
GGCGACGACTTCTCCCGCCGCTACCGCGGCGACTTCGCCGAGATGTCCAGCCAGCTGCAC
CTGACGCCCTTCACCGCGCGGGGACGCTTTGCCACGGTGGTGGAGGAGCTCTTCAGGGAC
GGGGTGAACTGGGGGAGGATTGTGGCCTTCTTTGAGTTCGGTGGGGTCATGTGTGTGGAG
AGCGTCAACCGGGAGATGTCGCCCCTGGTGGACAACATCGCCCTGTGGATGACTGAGTAC
CTGAACCGGCACCTGCACACCTGGATCCAGGATAACGGAGGCTGGGATGCCTTTGTGGAA
CTGTACGGCCCCAGCATGCGGCCTCTGTTTGATTTCTCCTGGCTGTCTCTGAAGACTCTG
CTCAGTTTGGCCCTGGTGGGAGCTTGCATCACCCTGGGTGCCTATCTGAGCCACAAGTGA
Target 1 GenBank Gene ID
Target 1 GeneCard ID BCL2 Link Image
Target 1 GenAtlas ID BCL2 Link Image
Target 1 HGNC ID HGNC:990 Link Image
Target 1 Chromosome Location 18
Target 1 Locus 18q21.33|18q21.3
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Yamamoto K, Ichijo H, Korsmeyer SJ: BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M. Mol Cell Biol. 1999 Dec;19(12):8469-78. [PubMed Link Image]
  2. Ruvolo PP, Deng X, May WS: Phosphorylation of Bcl2 and regulation of apoptosis. Leukemia. 2001 Apr;15(4):515-22. [PubMed Link Image]
  3. Yu J, Zhang L, Hwang PM, Kinzler KW, Vogelstein B: PUMA induces the rapid apoptosis of colorectal cancer cells. Mol Cell. 2001 Mar;7(3):673-82. [PubMed Link Image]
  4. Qin W, Hu J, Guo M, Xu J, Li J, Yao G, Zhou X, Jiang H, Zhang P, Shen L, Wan D, Gu J: BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis. Biochem Biophys Res Commun. 2003 Aug 22;308(2):379-85. [PubMed Link Image]
  5. Tanaka S, Louie DC, Kant JA, Reed JC: Frequent incidence of somatic mutations in translocated BCL2 oncogenes of non-Hodgkin's lymphomas. Blood. 1992 Jan 1;79(1):229-37. [PubMed Link Image]
  6. Eguchi Y, Ewert DL, Tsujimoto Y: Isolation and characterization of the chicken bcl-2 gene: expression in a variety of tissues including lymphoid and neuronal organs in adult and embryo. Nucleic Acids Res. 1992 Aug 25;20(16):4187-92. [PubMed Link Image]
  7. Hockenbery D, Nunez G, Milliman C, Schreiber RD, Korsmeyer SJ: Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature. 1990 Nov 22;348(6299):334-6. [PubMed Link Image]
  8. Seto M, Jaeger U, Hockett RD, Graninger W, Bennett S, Goldman P, Korsmeyer SJ: Alternative promoters and exons, somatic mutation and deregulation of the Bcl-2-Ig fusion gene in lymphoma. EMBO J. 1988 Jan;7(1):123-31. [PubMed Link Image]
  9. Cleary ML, Smith SD, Sklar J: Cloning and structural analysis of cDNAs for bcl-2 and a hybrid bcl-2/immunoglobulin transcript resulting from the t(14;18) translocation. Cell. 1986 Oct 10;47(1):19-28. [PubMed Link Image]
  10. Hua C, Zorn S, Jensen JP, Coupland RW, Ko HS, Wright JJ, Bakhshi A: Consequences of the t(14;18) chromosomal translocation in follicular lymphoma: deregulated expression of a chimeric and mutated BCL-2 gene. Oncogene Res. 1988 Feb;2(3):263-75. [PubMed Link Image]
  11. 3523487 Tsujimoto Y, Croce CM: Analysis of the structure, transcripts, and protein products of bcl-2, the gene involved in human follicular lymphoma. Proc Natl Acad Sci U S A. 1986 Jul;83(14):5214-8.
  12. 8183370 Yin XM, Oltvai ZN, Korsmeyer SJ: BH1 and BH2 domains of Bcl-2 are required for inhibition of apoptosis and heterodimerization with Bax. Nature. 1994 May 26;369(6478):321-3.
  13. 8668206 Naumovski L, Cleary ML: The p53-binding protein 53BP2 also interacts with Bc12 and impedes cell cycle progression at G2/M. Mol Cell Biol. 1996 Jul;16(7):3884-92.
  14. 9395403 Cheng EH, Kirsch DG, Clem RJ, Ravi R, Kastan MB, Bedi A, Ueno K, Hardwick JM: Conversion of Bcl-2 to a Bax-like death effector by caspases. Science. 1997 Dec 12;278(5345):1966-8.
Target 1 Drug References
  1. Youdim MB, Weinstock M: Molecular basis of neuroprotective activities of rasagiline and the anti-Alzheimer drug TV3326 [(N-propargyl-(3R)aminoindan-5-YL)-ethyl methyl carbamate]. Cell Mol Neurobiol. 2001 Dec;21(6):555-73. [PubMed Link Image]
  2. Akao Y, Maruyama W, Yi H, Shamoto-Nagai M, Youdim MB, Naoi M: An anti-Parkinson's disease drug, N-propargyl-1(R)-aminoindan (rasagiline), enhances expression of anti-apoptotic bcl-2 in human dopaminergic SH-SY5Y cells. Neurosci Lett. 2002 Jun 28;326(2):105-8. [PubMed Link Image]
  3. Maruyama W, Akao Y, Carrillo MC, Kitani K, Youdium MB, Naoi M: Neuroprotection by propargylamines in Parkinson's disease: suppression of apoptosis and induction of prosurvival genes. Neurotoxicol Teratol. 2002 Sep-Oct;24(5):675-82. [PubMed Link Image]
  4. Youdim MB, Amit T, Falach-Yogev M, Am OB, Maruyama W, Naoi M: The essentiality of Bcl-2, PKC and proteasome-ubiquitin complex activations in the neuroprotective-antiapoptotic action of the anti-Parkinson drug, rasagiline. Biochem Pharmacol. 2003 Oct 15;66(8):1635-41. [PubMed Link Image]
  5. Bar-Am O, Weinreb O, Amit T, Youdim MB: Regulation of Bcl-2 family proteins, neurotrophic factors, and APP processing in the neurorescue activity of propargylamine. FASEB J. 2005 Nov;19(13):1899-901. Epub 2005 Sep 7. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 3939
Target 2 Name Amine oxidase [flavin-containing] B
Target 2 Synonyms
  1. EC 1.4.3.4
  2. MAO-B
  3. Monoamine oxidase type B
Target 2 Gene Name MAOB
Target 2 Protein Sequence >Amine oxidase [flavin-containing] B 
MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSY
VGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWR
TMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEV
SALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQ
TRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVY
YKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEER
LKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDR
IYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTT
FLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV
Target 2 Number of Residues 528
Target 2 Molecular Weight 58764
Target 2 Theoretical pI 7.55
Target 2 GO Classification
Function
catalytic activity
oxidoreductase activity
Process
physiological process
metabolism
cellular metabolism
generation of precursor metabolites and energy
electron transport
Component
Not Available
Target 2 General Function Amino acid transport and metabolism
Target 2 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. MAOB preferentially degrades benzylamine and phenylethylamine
Target 2 Pathways
Name SMPDB Link KEGG Link
Tryptophan metabolism map00220 Link Image
Target 2 Reactions
  • RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2
Target 2 Pfam Domain Function
Target 2 Signals
  • None
Target 2 Transmembrane Regions
  • 490-516
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 398415 Link Image
Target 2 UniProtKB/Swiss-Prot ID P27338 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name AOFB_HUMAN Link Image
Target 2 PDB ID 2BK3 Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Mitochondrion
Target 2 Gene Sequence >1560 bp 
ATGAGCAACAAATGCGACGTGGTCGTGGTGGGGGGCGGCATCTCAGGTATGGCAGCAGCC
AAACTTCTGCATGACTCTGGACTGAATGTGGTTGTTCTGGAAGCCCGGGACCGTGTGGGA
GGCAGGACTTACACTCTTAGGAACCAAAAGGTTAAATATGTGGACCTTGGAGGATCCTAT
GTTGGACCAACCCAGAATCGTATCTTGAGATTAGCCAAGGAGCTAGGATTGGAGACCTAC
AAAGTGAATGAGGTTGAGCGTCTGATCCACCATGTAAAGGGCAAATCATACCCCTTCAGG
GGGCCATTCCCACCTGTATGGAATCCAATTACCTACTTAGATCATAACAACTTTTGGAGG
ACAATGGATGACATGGGGCGAGAGATTCCGAGTGATGCCCCATGGAAGGCTCCCCTTGCA
GAAGAGTGGGACAACATGACAATGAAGGAGCTACTGGACAAGCTCTGCTGGACTGAATCT
GCAAAGCAGCTTGCCACTCTCTTTGTGAACCTGTGTGTCACTGCAGAGACCCATGAGGTC
TCTGCTCTCTGGTTCCTGTGGTATGTGAAGCAGTGTGGAGGCACAACAAGAATCATCTCG
ACAACAAATGGAGGACAGGAGAGGAAATTTGTGGGCGGATCTGGTCAAGTGAGTGAGCGG
ATAATGGACCTCCTTGGAGACCGAGTGAAGCTGGAGAGGCCTGTGATCTACATTGACCAG
ACAAGAGAAAATGTCCTTGTGGAGACCCTAAACCATGAGATGTATGAGGCTAAATATGTG
ATTAGTGCTATTCCTCCTACTCTGGGCATGAAGATTCACTTCAATCCCCCTCTGCCAATG
ATGAGAAACCAGATGATCACTCGTGTGCCTTTGGGTTCAGTCATCAAGTGTATAGTTTAT
TATAAAGAGCCTTTCTGGAGGAAAAAGGATTACTGTGGAACCATGATTATTGATGGAGAA
GAAGCTCCAGTTGCCTACACGTTGGATGATACCAAACCTGAAGGCAACTATGCTGCCATA
ATGGGATTTATCCTGGCCCACAAAGCCAGAAAACTGGCACGTCTTACCAAAGAGGAAAGG
TTGAAGAAACTTTGTGAACTCTATGCCAAGGTTCTGGGTTCCCTAGAAGCTCTGGAGCCA
GTGCATTATGAAGAAAAGAACTGGTGTGAGGAGCAGTACTCTGGGGGCTGCTACACAACT
TATTTCCCCCCTGGGATCCTGACTCAATATGGAAGGGTTCTACGCCAGCCAGTGGACAGG
ATTTACTTTGCAGGCACCGAGACTGCCACACACTGGAGCGGCTACATGGAGGGGGCTGTA
GAGGCCGGGGAGAGAGCAGCCCGAGAGATCCTGCATGCCATGGGGAAGATTCCAGAGGAT
GAAATCTGGCAGTCAGAACCAGAGTCTGTGGATGTCCCTGCACAGCCCATCACCACCACC
TTTTTGGAGAGACATTTGCCCTCCGTGCCAGGCCTGCTCAGGCTGATTGGATTGACCACC
ATCTTTTCAGCAACGGCTCTTGGCTTCCTGGCCCACAAAAGGGGGCTACTTGTGAGAGTC
Target 2 GenBank Gene ID
Target 2 GeneCard ID MAOB Link Image
Target 2 GenAtlas ID MAOB Link Image
Target 2 HGNC ID HGNC:6834 Link Image
Target 2 Chromosome Location X
Target 2 Locus Xp11.23
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. Newton-Vinson P, Hubalek F, Edmondson DE: High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr Purif. 2000 Nov;20(2):334-45. [PubMed Link Image]
  2. Binda C, Newton-Vinson P, Hubalek F, Edmondson DE, Mattevi A: Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat Struct Biol. 2002 Jan;9(1):22-6. [PubMed Link Image]
  3. Zhu QS, Grimsby J, Chen K, Shih JC: Promoter organization and activity of human monoamine oxidase (MAO) A and B genes. J Neurosci. 1992 Nov;12(11):4437-46. [PubMed Link Image]
  4. Grimsby J, Chen K, Wang LJ, Lan NC, Shih JC: Human monoamine oxidase A and B genes exhibit identical exon-intron organization. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3637-41. [PubMed Link Image]
  5. 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 Link Image]
  6. Chen K, Wu HF, Shih JC: The deduced amino acid sequences of human platelet and frontal cortex monoamine oxidase B are identical. J Neurochem. 1993 Jul;61(1):187-90. [PubMed Link Image]
Target 2 Drug References Not Available

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.