AOFB_RAT
ID AOFB_RAT Reviewed; 520 AA.
AC P19643; Q5EBB5;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Amine oxidase [flavin-containing] B {ECO:0000305};
DE EC=1.4.3.21 {ECO:0000269|PubMed:20493079, ECO:0000269|PubMed:4156831};
DE EC=1.4.3.4 {ECO:0000269|PubMed:20493079};
DE AltName: Full=Monoamine oxidase type B;
DE Short=MAO-B;
GN Name=Maob {ECO:0000312|RGD:3041};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2974701; DOI=10.1016/s0006-291x(88)80969-0;
RA Ito A., Kuwahara T., Inadome S., Sagara Y.;
RT "Molecular cloning of a cDNA for rat liver monoamine oxidase B.";
RL Biochem. Biophys. Res. Commun. 157:970-976(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=4156831; DOI=10.1042/bj1440029;
RA Seiler N., Al-Therib M.J.;
RT "Putrescine catabolism in mammalian brain.";
RL Biochem. J. 144:29-35(1974).
RN [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6428396; DOI=10.1016/0006-291x(84)91293-2;
RA Chiba K., Trevor A., Castagnoli N. Jr.;
RT "Metabolism of the neurotoxic tertiary amine, MPTP, by brain monoamine
RT oxidase.";
RL Biochem. Biophys. Res. Commun. 120:574-578(1984).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20493079; DOI=10.1016/0197-0186(86)90182-8;
RA O'Carroll A.M., Bardsley M.E., Tipton K.F.;
RT "The oxidation of adrenaline and noradrenaline by the two forms of
RT monoamine oxidase from human and rat brain.";
RL Neurochem. Int. 8:493-500(1986).
RN [6]
RP MUTAGENESIS OF ILE-199.
RX PubMed=9162023; DOI=10.1074/jbc.272.22.14033;
RA Tsugeno Y., Ito A.;
RT "A key amino acid responsible for substrate selectivity of monoamine
RT oxidase A and B.";
RL J. Biol. Chem. 272:14033-14036(1997).
CC -!- FUNCTION: Catalyzes the oxidative deamination of primary and some
CC secondary amines such as neurotransmitters, and exogenous amines
CC including the tertiary amine, neurotoxin 1-methyl-4-phenyl-1,2,3,6-
CC tetrahydropyridine (MPTP), with concomitant reduction of oxygen to
CC hydrogen peroxide and participates in the metabolism of neuroactive and
CC vasoactive amines in the central nervous system and peripheral tissues
CC (PubMed:20493079). Preferentially degrades benzylamine and
CC phenylethylamine (PubMed:20493079). {ECO:0000269|PubMed:20493079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary aliphatic amine + H2O + O2 = a primary amine + an
CC aldehyde + H2O2; Xref=Rhea:RHEA:26414, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:58855, ChEBI:CHEBI:65296; EC=1.4.3.4;
CC Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-adrenaline + H2O + O2 = (R)-3,4-dihydroxymandelaldehyde +
CC H2O2 + methylamine; Xref=Rhea:RHEA:51168, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:59338,
CC ChEBI:CHEBI:71406, ChEBI:CHEBI:180943;
CC Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21;
CC Evidence={ECO:0000269|PubMed:20493079, ECO:0000269|PubMed:4156831};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16154;
CC Evidence={ECO:0000305|PubMed:4156831};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dopamine + H2O + O2 = 3,4-dihydroxyphenylacetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:27946, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:27978, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:59905; Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + tyramine = (4-hydroxyphenyl)acetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:30591, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:15621, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:327995; Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-noradrenaline + H2O + O2 = (R)-3,4-dihydroxymandelaldehyde
CC + H2O2 + NH4(+); Xref=Rhea:RHEA:69076, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:72587, ChEBI:CHEBI:180943;
CC Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzylamine + H2O + O2 = benzaldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:59424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17169, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:225238; Evidence={ECO:0000250|UniProtKB:P27338};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59425;
CC Evidence={ECO:0000250|UniProtKB:P27338};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:25265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16424, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:225237; Evidence={ECO:0000269|PubMed:20493079};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetylputrescine + O2 = 4-acetamidobutanal + H2O2 +
CC NH4(+); Xref=Rhea:RHEA:70283, ChEBI:CHEBI:7386, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58263; Evidence={ECO:0000269|PubMed:4156831};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70284;
CC Evidence={ECO:0000269|PubMed:4156831};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P27338};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=840 uM for (R)-adrenaline {ECO:0000269|PubMed:20493079};
CC KM=290 uM for dopamine {ECO:0000269|PubMed:20493079};
CC KM=533 uM for serotonin {ECO:0000269|PubMed:20493079};
CC KM=1954 uM for (R)-noradrenaline {ECO:0000269|PubMed:20493079};
CC KM=5 uM for 2-phenylethylamine {ECO:0000269|PubMed:20493079};
CC KM=328 uM for tyramine {ECO:0000269|PubMed:20493079};
CC Vmax=531 pmol/min/mg enzyme toward (R)-adrenaline
CC {ECO:0000269|PubMed:20493079};
CC Vmax=396 pmol/min/mg enzyme toward dopamine
CC {ECO:0000269|PubMed:20493079};
CC Vmax=125 pmol/min/mg enzyme toward serotonin
CC {ECO:0000269|PubMed:20493079};
CC Vmax=383 pmol/min/mg enzyme toward (R)-noradrenaline
CC {ECO:0000269|PubMed:20493079};
CC Vmax=489 pmol/min/mg enzyme toward 2-phenylethylamine
CC {ECO:0000269|PubMed:20493079};
CC Vmax=687 pmol/min/mg enzyme toward tyramine
CC {ECO:0000269|PubMed:20493079};
CC -!- SUBUNIT: Monomer, homo- or heterodimer (containing two subunits of
CC similar size). Each subunit contains a covalently bound flavin.
CC Enzymatically active as monomer (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type IV
CC membrane protein; Cytoplasmic side.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000305}.
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DR EMBL; M23601; AAA41566.1; -; mRNA.
DR EMBL; BC089814; AAH89814.1; -; mRNA.
DR PIR; A31870; A31870.
DR RefSeq; NP_037330.1; NM_013198.1.
DR AlphaFoldDB; P19643; -.
DR SMR; P19643; -.
DR BioGRID; 247778; 1.
DR STRING; 10116.ENSRNOP00000043466; -.
DR BindingDB; P19643; -.
DR ChEMBL; CHEMBL2993; -.
DR DrugCentral; P19643; -.
DR GuidetoPHARMACOLOGY; 2490; -.
DR iPTMnet; P19643; -.
DR PhosphoSitePlus; P19643; -.
DR PaxDb; P19643; -.
DR PRIDE; P19643; -.
DR DNASU; 25750; -.
DR Ensembl; ENSRNOT00000044009; ENSRNOP00000043466; ENSRNOG00000029778.
DR GeneID; 25750; -.
DR KEGG; rno:25750; -.
DR UCSC; RGD:3041; rat.
DR CTD; 4129; -.
DR RGD; 3041; Maob.
DR eggNOG; KOG0029; Eukaryota.
DR GeneTree; ENSGT00940000161545; -.
DR HOGENOM; CLU_004498_0_1_1; -.
DR InParanoid; P19643; -.
DR OMA; PIHWAGT; -.
DR OrthoDB; 1151887at2759; -.
DR PhylomeDB; P19643; -.
DR BRENDA; 1.4.3.4; 5301.
DR Reactome; R-RNO-141333; Biogenic amines are oxidatively deaminated to aldehydes by MAOA and MAOB.
DR SABIO-RK; P19643; -.
DR PRO; PR:P19643; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000029778; Expressed in liver and 19 other tissues.
DR Genevisible; P19643; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:RHEA.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0097621; F:monoamine oxidase activity; IDA:UniProtKB.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:RHEA.
DR GO; GO:0008131; F:primary amine oxidase activity; IDA:UniProtKB.
DR GO; GO:0014063; P:negative regulation of serotonin secretion; IMP:RGD.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IDA:RGD.
DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; IMP:RGD.
DR GO; GO:0010044; P:response to aluminum ion; IEP:RGD.
DR GO; GO:0051412; P:response to corticosterone; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0010269; P:response to selenium ion; IEP:RGD.
DR GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW Acetylation; FAD; Flavoprotein; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Oxidoreductase; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P56560"
FT CHAIN 2..520
FT /note="Amine oxidase [flavin-containing] B"
FT /id="PRO_0000099863"
FT TOPO_DOM 2..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 490..516
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000250"
FT TOPO_DOM 517..520
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250"
FT SITE 156
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 365
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 382
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P56560"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BW75"
FT MOD_RES 397
FT /note="S-8alpha-FAD cysteine"
FT /evidence="ECO:0000250|UniProtKB:P27338"
FT MUTAGEN 139
FT /note="L->H: No change in substrate affinity."
FT MUTAGEN 199
FT /note="I->F: Increased affinity for serotonin and
FT tyramine."
FT /evidence="ECO:0000269|PubMed:9162023"
FT CONFLICT 38
FT /note="R -> C (in Ref. 1; AAA41566)"
FT /evidence="ECO:0000305"
FT CONFLICT 335..336
FT /note="GS -> AG (in Ref. 1; AAA41566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 58459 MW; F2C230BC6CDE5840 CRC64;
MSNKCDVIVV GGGISGMAAA KLLHDCGLSV VVLEARDRVG GRTYTIRNKN VKYVDLGGSY
VGPTQNRILR LAKELGLETY KVNEVERLIH FVKGKSYAFR GPFPPVWNPI TYLDYNNLWR
TMDEMGQEIP SDAPWKAPLA EEWDYMTMKE LLDKICWTNS TKQIATLFVN LCVTAETHEV
SALWFLWYVK QCGGTTRIIS TTNGGQERKF IGGSGQVSER IKDILGDRVK LERPVIHIDQ
TGENVVVKTL NHEIYEAKYV ISAIPPVLGM KIHHSPPLPI LRNQLITRVP LGSVIKCMVY
YKEPFWRKKD FCGTMVIEGE EAPIAYTLDD TKPDGSCAAI MGFILAHKAR KLVRLTKEER
LRKLCELYAK VLNSQEALQP VHYEEKNWCE EQYSGGCYTA YFPPGILTQY GRVLRQPVGK
IFFAGTETAS HWSGYMEGAV EAGERAAREI LHAIGKIPED EIWQPEPESV DVPARPITNT
FLERHLPSVP GLLKLLGLTT ILSATALGFL AHKKGLFVRF
