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Amine oxidase [flavin-containing] B (EC 1.4.3.4) (Monoamine oxidase type B) (MAO-B)

 AOFB_HUMAN              Reviewed;         520 AA.
P27338; B2R6R3; B7Z5H3; D3DWC3; Q7Z6S2;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 186.
RecName: Full=Amine oxidase [flavin-containing] B;
EC=1.4.3.4;
AltName: Full=Monoamine oxidase type B;
Short=MAO-B;
Name=MAOB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2023912; DOI=10.1073/pnas.88.9.3637;
Grimsby J., Chen K., Wang L.J., Lan N.C., Shih J.C.;
"Human monoamine oxidase A and B genes exhibit identical exon-intron
organization.";
Proc. Natl. Acad. Sci. U.S.A. 88:3637-3641(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3387449; DOI=10.1073/pnas.85.13.4934;
Bach A.W.J., Lan N.C., Johnson D.L., Abell C.W., Bembenek M.E.,
Kwan S.W., Seeburg P.H., Shih J.C.;
"cDNA cloning of human liver monoamine oxidase A and B: molecular
basis of differences in enzymatic properties.";
Proc. Natl. Acad. Sci. U.S.A. 85:4934-4938(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8515265; DOI=10.1111/j.1471-4159.1993.tb03554.x;
Chen K., Wu H.F., Shih J.C.;
"The deduced amino acid sequences of human platelet and frontal cortex
monoamine oxidase B are identical.";
J. Neurochem. 61:187-190(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
PubMed=1432104;
Zhu Q.S., Grimsby J.S., Chen K., Shih J.C.;
"Promoter organization and activity of human monoamine oxidase (MAO) A
and B genes.";
J. Neurosci. 12:4437-4446(1992).
[8]
PROTEIN SEQUENCE OF 2-17, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
PubMed=11049757; DOI=10.1006/prep.2000.1309;
Newton-Vinson P., Hubalek F., Edmondson D.E.;
"High-level expression of human liver monoamine oxidase B in Pichia
pastoris.";
Protein Expr. Purif. 20:334-345(2000).
[9]
PROTEIN SEQUENCE OF 371-391, AND MUTAGENESIS OF THR-158; HIS-382;
LYS-386; CYS-389 AND SER-394.
PubMed=8665924; DOI=10.1111/j.1432-1033.1996.00996.x;
Cesura A.M., Gottowik J., Lahm H.-W., Lang G., Imhof R., Malherbe P.,
Roethlisberger U., Da Prada M.;
"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. 236:996-1002(1996).
[10]
MUTAGENESIS OF CYS-5; CYS-156; CYS-172; CYS-192; CYS-297; CYS-312;
CYS-365; CYS-389 AND CYS-397.
PubMed=8316221;
Wu H.F., Chen K., Shih J.C.;
"Site-directed mutagenesis of monoamine oxidase A and B: role of
cysteines.";
Mol. Pharmacol. 43:888-893(1993).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=11753429; DOI=10.1038/nsb732;
Binda C., Newton-Vinson P., Hubalek F., Edmondson D.E., Mattevi A.;
"Structure of human monoamine oxidase B, a drug target for the
treatment of neurological disorders.";
Nat. Struct. Biol. 9:22-26(2002).
[13]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
PubMed=12913124; DOI=10.1073/pnas.1633804100;
Binda C., Li M., Hubalek F., Restelli N., Edmondson D.E., Mattevi A.;
"Insights into the mode of inhibition of human mitochondrial monoamine
oxidase B from high-resolution crystal structures.";
Proc. Natl. Acad. Sci. U.S.A. 100:9750-9755(2003).
[14]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
PubMed=15027868; DOI=10.1021/jm031087c;
Binda C., Hubalek F., Li M., Herzig Y., Sterling J., Edmondson D.E.,
Mattevi A.;
"Crystal structures of monoamine oxidase B in complex with four
inhibitors of the N-propargylaminoindan class.";
J. Med. Chem. 47:1767-1774(2004).
[15]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT PHE-199 IN COMPLEXES
WITH INHIBITORS.
PubMed=15710600; DOI=10.1074/jbc.M500949200;
Hubalek F., Binda C., Khalil A., Li M., Mattevi A., Castagnoli N.,
Edmondson D.E.;
"Demonstration of isoleucine 199 as a structural determinant for the
selective inhibition of human monoamine oxidase B by specific
reversible inhibitors.";
J. Biol. Chem. 280:15761-15766(2005).
[16]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEXES WITH INHIBITORS.
PubMed=16366596; DOI=10.1021/jm0506266;
Binda C., Hubalek F., Li M., Herzig Y., Sterling J., Edmondson D.E.,
Mattevi A.;
"Binding of rasagiline-related inhibitors to human monoamine oxidases:
a kinetic and crystallographic analysis.";
J. Med. Chem. 48:8148-8154(2005).
-!- 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.
-!- CATALYTIC ACTIVITY: RCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) +
H(2)O(2).
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
-!- SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of
similar size). Each subunit contains a covalently bound flavin.
Enzymatically active as monomer (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
type IV membrane protein; Cytoplasmic side.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P27338-1; Sequence=Displayed;
Name=2;
IsoId=P27338-2; Sequence=VSP_057047, VSP_057048, VSP_057049;
Note=No experimental confirmation available.;
-!- MASS SPECTROMETRY: Mass=59474; Mass_error=14.0;
Method=Electrospray; Range=2-520;
Evidence={ECO:0000269|PubMed:11049757};
-!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=MAOB";
-!- WEB RESOURCE: Name=Wikipedia; Note=Monoamine oxidase entry;
URL="https://en.wikipedia.org/wiki/Monoamine_oxidase";
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EMBL; S62734; AAB27229.1; -; mRNA.
EMBL; M69135; AAA59551.1; -; Genomic_DNA.
EMBL; AK298942; BAH12909.1; -; mRNA.
EMBL; AK312679; BAG35560.1; -; mRNA.
EMBL; M69177; AAA59550.1; -; mRNA.
EMBL; M89637; AAB46386.1; -; Genomic_DNA.
EMBL; AL008709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL020990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX537148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z95125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471141; EAW59378.1; -; Genomic_DNA.
EMBL; CH471141; EAW59380.1; -; Genomic_DNA.
CCDS; CCDS14261.1; -. [P27338-1]
PIR; JH0817; JH0817.
RefSeq; NP_000889.3; NM_000898.4. [P27338-1]
UniGene; Hs.654473; -.
PDB; 1GOS; X-ray; 3.00 A; A/B=2-520.
PDB; 1H8R; Model; -; A=5-459.
PDB; 1OJ9; X-ray; 2.30 A; A/B=2-520.
PDB; 1OJA; X-ray; 1.70 A; A/B=2-520.
PDB; 1OJC; X-ray; 2.40 A; A/B=2-520.
PDB; 1OJD; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/L=2-520.
PDB; 1S2Q; X-ray; 2.07 A; A/B=1-520.
PDB; 1S2Y; X-ray; 2.12 A; A/B=1-520.
PDB; 1S3B; X-ray; 1.65 A; A/B=1-520.
PDB; 1S3E; X-ray; 1.60 A; A/B=1-520.
PDB; 2BK3; X-ray; 1.80 A; A/B=2-520.
PDB; 2BK4; X-ray; 1.90 A; A/B=2-520.
PDB; 2BK5; X-ray; 1.83 A; A/B=1-520.
PDB; 2BYB; X-ray; 2.20 A; A/B=2-520.
PDB; 2C64; X-ray; 2.20 A; A/B=2-520.
PDB; 2C65; X-ray; 1.70 A; A/B=2-520.
PDB; 2C66; X-ray; 2.50 A; A/B=2-520.
PDB; 2C67; X-ray; 1.70 A; A/B=2-520.
PDB; 2C70; X-ray; 2.06 A; A/B=2-520.
PDB; 2C72; X-ray; 2.00 A; A/B=2-520.
PDB; 2C73; X-ray; 2.20 A; A/B=2-520.
PDB; 2C75; X-ray; 1.70 A; A/B=2-520.
PDB; 2C76; X-ray; 1.70 A; A/B=2-520.
PDB; 2V5Z; X-ray; 1.60 A; A/B=2-520.
PDB; 2V60; X-ray; 2.00 A; A/B=2-520.
PDB; 2V61; X-ray; 1.70 A; A/B=2-520.
PDB; 2VRL; X-ray; 2.40 A; A/B=1-520.
PDB; 2VRM; X-ray; 2.30 A; A/B=1-520.
PDB; 2VZ2; X-ray; 2.30 A; A/B=1-520.
PDB; 2XCG; X-ray; 1.90 A; A/B=1-520.
PDB; 2XFN; X-ray; 1.60 A; A/B=1-520.
PDB; 2XFO; X-ray; 2.10 A; A/B=1-520.
PDB; 2XFP; X-ray; 1.66 A; A/B=1-520.
PDB; 2XFQ; X-ray; 2.20 A; A/B=1-520.
PDB; 2XFU; X-ray; 2.20 A; A/B=2-520.
PDB; 3PO7; X-ray; 1.80 A; A/B=1-520.
PDB; 3ZYX; X-ray; 2.20 A; A/B=2-520.
PDB; 4A79; X-ray; 1.89 A; A/B=1-520.
PDB; 4A7A; X-ray; 1.70 A; A/B=1-520.
PDB; 4CRT; X-ray; 1.80 A; A/B=1-520.
PDB; 5MRL; X-ray; 2.42 A; A/B=1-520.
PDBsum; 1GOS; -.
PDBsum; 1H8R; -.
PDBsum; 1OJ9; -.
PDBsum; 1OJA; -.
PDBsum; 1OJC; -.
PDBsum; 1OJD; -.
PDBsum; 1S2Q; -.
PDBsum; 1S2Y; -.
PDBsum; 1S3B; -.
PDBsum; 1S3E; -.
PDBsum; 2BK3; -.
PDBsum; 2BK4; -.
PDBsum; 2BK5; -.
PDBsum; 2BYB; -.
PDBsum; 2C64; -.
PDBsum; 2C65; -.
PDBsum; 2C66; -.
PDBsum; 2C67; -.
PDBsum; 2C70; -.
PDBsum; 2C72; -.
PDBsum; 2C73; -.
PDBsum; 2C75; -.
PDBsum; 2C76; -.
PDBsum; 2V5Z; -.
PDBsum; 2V60; -.
PDBsum; 2V61; -.
PDBsum; 2VRL; -.
PDBsum; 2VRM; -.
PDBsum; 2VZ2; -.
PDBsum; 2XCG; -.
PDBsum; 2XFN; -.
PDBsum; 2XFO; -.
PDBsum; 2XFP; -.
PDBsum; 2XFQ; -.
PDBsum; 2XFU; -.
PDBsum; 3PO7; -.
PDBsum; 3ZYX; -.
PDBsum; 4A79; -.
PDBsum; 4A7A; -.
PDBsum; 4CRT; -.
PDBsum; 5MRL; -.
ProteinModelPortal; P27338; -.
SMR; P27338; -.
BioGrid; 110302; 5.
IntAct; P27338; 3.
MINT; MINT-3010688; -.
STRING; 9606.ENSP00000367309; -.
BindingDB; P27338; -.
ChEMBL; CHEMBL2039; -.
DrugBank; DB08176; (1Z)-4-(4-FLUOROPHENYL)-2-METHYLIDENEBUTAN-1-IMINE.
DrugBank; DB08516; (S)-(+)-2-[4-(FLUOROBENZYLOXY-BENZYLAMINO)PROPIONAMIDE].
DrugBank; DB08480; 4-HYDROXY-N-PROPARGYL-1(R)-AMINOINDAN.
DrugBank; DB01472; 4-Methoxyamphetamine.
DrugBank; DB04307; 5-Hydroxy-N-Propargyl-1(R)-Aminoindan.
DrugBank; DB07512; 7-[(3-CHLOROBENZYL)OXY]-2-OXO-2H-CHROMENE-4-CARBALDEHYDE.
DrugBank; DB07513; 7-[(3-CHLOROBENZYL)OXY]-4-[(METHYLAMINO)METHYL]-2H-CHROMEN-2-ONE.
DrugBank; DB00915; Amantadine.
DrugBank; DB00182; Amphetamine.
DrugBank; DB04889; Bicifadine.
DrugBank; DB01445; Bufotenine.
DrugBank; DB00988; Dopamine.
DrugBank; DB01363; Ephedra.
DrugBank; DB02509; Farnesol.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB00614; Furazolidone.
DrugBank; DB04818; Iproniazid.
DrugBank; DB02095; Isatin.
DrugBank; DB01247; Isocarboxazid.
DrugBank; DB04147; Lauryl Dimethylamine-N-Oxide.
DrugBank; DB00601; Linezolid.
DrugBank; DB01577; Methamphetamine.
DrugBank; DB01442; MMDA.
DrugBank; DB01171; Moclobemide.
DrugBank; DB08082; N-(2-AMINOETHYL)-P-CHLOROBENZAMIDE.
DrugBank; DB04677; N-METHYL-N-[(1R)-1-METHYL-2-PHENYLETHYL]PROP-2-EN-1-AMINE.
DrugBank; DB02211; N-Methyl-N-Propargyl-1(R)-Aminoindan.
DrugBank; DB03894; N-Propargyl-1(S)-Aminoindan.
DrugBank; DB08804; Nandrolone decanoate.
DrugBank; DB04820; Nialamide.
DrugBank; DB00184; Nicotine.
DrugBank; DB04821; Nomifensine.
DrugBank; DB01626; Pargyline.
DrugBank; DB00780; Phenelzine.
DrugBank; DB00191; Phentermine.
DrugBank; DB00721; Procaine.
DrugBank; DB01168; Procarbazine.
DrugBank; DB01367; Rasagiline.
DrugBank; DB06654; Safinamide.
DrugBank; DB01037; Selegiline.
DrugBank; DB01104; Sertraline.
DrugBank; DB00752; Tranylcypromine.
DrugBank; DB04832; Zimelidine.
DrugBank; DB00909; Zonisamide.
GuidetoPHARMACOLOGY; 2490; -.
iPTMnet; P27338; -.
PhosphoSitePlus; P27338; -.
BioMuta; MAOB; -.
DMDM; 113980; -.
EPD; P27338; -.
MaxQB; P27338; -.
PaxDb; P27338; -.
PeptideAtlas; P27338; -.
PRIDE; P27338; -.
DNASU; 4129; -.
Ensembl; ENST00000378069; ENSP00000367309; ENSG00000069535. [P27338-1]
GeneID; 4129; -.
KEGG; hsa:4129; -.
UCSC; uc004dfz.5; human. [P27338-1]
CTD; 4129; -.
DisGeNET; 4129; -.
EuPathDB; HostDB:ENSG00000069535.13; -.
GeneCards; MAOB; -.
HGNC; HGNC:6834; MAOB.
HPA; CAB037200; -.
HPA; HPA002328; -.
MIM; 309860; gene.
neXtProt; NX_P27338; -.
OpenTargets; ENSG00000069535; -.
PharmGKB; PA237; -.
eggNOG; KOG0029; Eukaryota.
eggNOG; ENOG410XSNC; LUCA.
GeneTree; ENSGT00730000110903; -.
HOGENOM; HOG000221615; -.
HOVERGEN; HBG004255; -.
InParanoid; P27338; -.
KO; K00274; -.
OMA; PWKAPLA; -.
OrthoDB; EOG091G0G7P; -.
PhylomeDB; P27338; -.
TreeFam; TF313314; -.
BioCyc; MetaCyc:HS00966-MONOMER; -.
BRENDA; 1.4.3.4; 2681.
Reactome; R-HSA-141333; Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
SABIO-RK; P27338; -.
SIGNOR; P27338; -.
ChiTaRS; MAOB; human.
EvolutionaryTrace; P27338; -.
GeneWiki; Monoamine_oxidase_B; -.
GenomeRNAi; 4129; -.
PRO; PR:P27338; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000069535; -.
CleanEx; HS_MAOB; -.
Genevisible; P27338; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005740; C:mitochondrial envelope; TAS:ProtInc.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:ParkinsonsUK-UCL.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:Ensembl.
GO; GO:0008131; F:primary amine oxidase activity; TAS:Reactome.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0042420; P:dopamine catabolic process; TAS:ParkinsonsUK-UCL.
GO; GO:0050665; P:hydrogen peroxide biosynthetic process; NAS:ParkinsonsUK-UCL.
GO; GO:0014063; P:negative regulation of serotonin secretion; IEA:Ensembl.
GO; GO:0042135; P:neurotransmitter catabolic process; IEA:Ensembl.
GO; GO:0045964; P:positive regulation of dopamine metabolic process; IEA:Ensembl.
GO; GO:0010044; P:response to aluminum ion; IEA:Ensembl.
GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
Gene3D; 3.50.50.60; -; 2.
InterPro; IPR002937; Amino_oxidase.
InterPro; IPR036188; FAD/NAD-bd_sf.
InterPro; IPR001613; Flavin_amine_oxidase.
Pfam; PF01593; Amino_oxidase; 1.
PRINTS; PR00757; AMINEOXDASEF.
SUPFAM; SSF51905; SSF51905; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; FAD; Flavoprotein; Membrane; Mitochondrion;
Mitochondrion outer membrane; Oxidoreductase; Reference proteome;
Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11049757}.
CHAIN 2 520 Amine oxidase [flavin-containing] B.
/FTId=PRO_0000099859.
TOPO_DOM 2 489 Cytoplasmic.
TRANSMEM 490 516 Helical; Anchor for type IV membrane
protein.
TOPO_DOM 517 520 Mitochondrial intermembrane.
COMPBIAS 36 52 Arg/Lys-rich (basic).
SITE 156 156 Important for catalytic activity.
SITE 365 365 Important for catalytic activity.
SITE 382 382 Important for catalytic activity.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:11049757}.
MOD_RES 52 52 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8BW75}.
MOD_RES 397 397 S-8alpha-FAD cysteine.
VAR_SEQ 1 16 Missing (in isoform 2).
/FTId=VSP_057047.
VAR_SEQ 380 427 PVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDR
IYFAGTE -> GSTPASGQDLLCRHRDCHTLERLHGGGCRG
RGESSPRDPACHGEDSRG (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057048.
VAR_SEQ 428 520 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057049.
MUTAGEN 5 5 C->S: No loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 156 156 C->S: Complete loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 158 158 T->A: Dramatic loss of activity.
{ECO:0000269|PubMed:8665924}.
MUTAGEN 172 172 C->S: No loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 192 192 C->S: No loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 199 199 I->F: Alters specificity towards
synthetic inhibitors.
MUTAGEN 297 297 C->S: No loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 312 312 C->S: No loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 365 365 C->S: Complete loss of activity.
{ECO:0000269|PubMed:8316221}.
MUTAGEN 382 382 H->R: Significant loss of activity.
{ECO:0000269|PubMed:8665924}.
MUTAGEN 386 386 K->M: No loss of activity.
{ECO:0000269|PubMed:8665924}.
MUTAGEN 389 389 C->A: Complete loss of activity.
{ECO:0000269|PubMed:8316221,
ECO:0000269|PubMed:8665924}.
MUTAGEN 389 389 C->S: No loss of activity.
{ECO:0000269|PubMed:8316221,
ECO:0000269|PubMed:8665924}.
MUTAGEN 394 394 S->A: No loss of activity.
{ECO:0000269|PubMed:8665924}.
MUTAGEN 397 397 C->S: Complete loss of activity.
{ECO:0000269|PubMed:8316221}.
STRAND 6 10 {ECO:0000244|PDB:1S3E}.
HELIX 14 25 {ECO:0000244|PDB:1S3E}.
STRAND 30 33 {ECO:0000244|PDB:1S3E}.
STRAND 35 40 {ECO:0000244|PDB:1S3E}.
STRAND 45 48 {ECO:0000244|PDB:2XFN}.
TURN 49 51 {ECO:0000244|PDB:1S3E}.
STRAND 54 57 {ECO:0000244|PDB:1S3E}.
HELIX 66 74 {ECO:0000244|PDB:1S3E}.
STRAND 79 81 {ECO:0000244|PDB:1S3E}.
STRAND 85 92 {ECO:0000244|PDB:1S3E}.
STRAND 95 99 {ECO:0000244|PDB:1S3E}.
STRAND 101 103 {ECO:0000244|PDB:1S3E}.
HELIX 109 126 {ECO:0000244|PDB:1S3E}.
HELIX 134 136 {ECO:0000244|PDB:1S3E}.
HELIX 140 144 {ECO:0000244|PDB:1S3E}.
STRAND 145 147 {ECO:0000244|PDB:2BYB}.
HELIX 148 155 {ECO:0000244|PDB:1S3E}.
HELIX 159 173 {ECO:0000244|PDB:1S3E}.
TURN 177 179 {ECO:0000244|PDB:1S3E}.
HELIX 182 190 {ECO:0000244|PDB:1S3E}.
TURN 191 193 {ECO:0000244|PDB:1S3E}.
HELIX 195 199 {ECO:0000244|PDB:1S3E}.
STRAND 207 210 {ECO:0000244|PDB:1S3E}.
HELIX 215 225 {ECO:0000244|PDB:1S3E}.
HELIX 226 228 {ECO:0000244|PDB:1S3E}.
STRAND 229 232 {ECO:0000244|PDB:1S3E}.
STRAND 235 239 {ECO:0000244|PDB:1S3E}.
STRAND 241 249 {ECO:0000244|PDB:1S3E}.
STRAND 254 262 {ECO:0000244|PDB:1S3E}.
HELIX 266 271 {ECO:0000244|PDB:1S3E}.
STRAND 272 276 {ECO:0000244|PDB:1S3E}.
HELIX 280 285 {ECO:0000244|PDB:1S3E}.
STRAND 294 300 {ECO:0000244|PDB:1S3E}.
HELIX 305 309 {ECO:0000244|PDB:1S3E}.
STRAND 311 317 {ECO:0000244|PDB:1S3E}.
STRAND 319 321 {ECO:0000244|PDB:1S3B}.
STRAND 325 329 {ECO:0000244|PDB:1S3E}.
STRAND 339 345 {ECO:0000244|PDB:1S3E}.
HELIX 347 352 {ECO:0000244|PDB:1S3E}.
HELIX 357 372 {ECO:0000244|PDB:1S3E}.
HELIX 375 378 {ECO:0000244|PDB:1S3E}.
STRAND 381 387 {ECO:0000244|PDB:1S3E}.
HELIX 388 390 {ECO:0000244|PDB:1S3E}.
TURN 392 394 {ECO:0000244|PDB:1S3E}.
STRAND 396 398 {ECO:0000244|PDB:1S3E}.
HELIX 406 410 {ECO:0000244|PDB:1S3E}.
HELIX 411 413 {ECO:0000244|PDB:1S3E}.
STRAND 421 423 {ECO:0000244|PDB:1S3E}.
HELIX 426 428 {ECO:0000244|PDB:1S3E}.
STRAND 430 432 {ECO:0000244|PDB:1S3E}.
HELIX 436 453 {ECO:0000244|PDB:1S3E}.
HELIX 459 461 {ECO:0000244|PDB:1S3E}.
STRAND 470 472 {ECO:0000244|PDB:1S3E}.
HELIX 481 485 {ECO:0000244|PDB:1S3E}.
HELIX 489 500 {ECO:0000244|PDB:1S3E}.
SEQUENCE 520 AA; 58763 MW; 358D1025F5BCA604 CRC64;
MSNKCDVVVV GGGISGMAAA KLLHDSGLNV VVLEARDRVG GRTYTLRNQK VKYVDLGGSY
VGPTQNRILR LAKELGLETY KVNEVERLIH HVKGKSYPFR GPFPPVWNPI TYLDHNNFWR
TMDDMGREIP SDAPWKAPLA EEWDNMTMKE LLDKLCWTES AKQLATLFVN LCVTAETHEV
SALWFLWYVK QCGGTTRIIS TTNGGQERKF VGGSGQVSER IMDLLGDRVK LERPVIYIDQ
TRENVLVETL NHEMYEAKYV ISAIPPTLGM KIHFNPPLPM MRNQMITRVP LGSVIKCIVY
YKEPFWRKKD YCGTMIIDGE EAPVAYTLDD TKPEGNYAAI MGFILAHKAR KLARLTKEER
LKKLCELYAK VLGSLEALEP VHYEEKNWCE EQYSGGCYTT YFPPGILTQY GRVLRQPVDR
IYFAGTETAT HWSGYMEGAV EAGERAAREI LHAMGKIPED EIWQSEPESV DVPAQPITTT
FLERHLPSVP GLLRLIGLTT IFSATALGFL AHKRGLLVRV


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