| Entry |
|
|---|
| Name |
monoamine oxidase;
adrenalin oxidase;
adrenaline oxidase;
amine oxidase (ambiguous);
amine oxidase (flavin-containing);
amine:oxygen oxidoreductase (deaminating) (flavin-containing);
epinephrine oxidase;
MAO;
MAO A;
MAO B;
MAO-A;
MAO-B;
monoamine oxidase A;
monoamine oxidase B;
monoamine:O2 oxidoreductase (deaminating);
polyamine oxidase (ambiguous);
serotonin deaminase;
spermidine oxidase (ambiguous);
spermine oxidase (ambiguous);
tyraminase;
tyramine oxidase |
|---|
| Class |
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With oxygen as acceptor
 |
|---|
| Sysname |
amine:oxygen oxidoreductase (deaminating) |
|---|
| Reaction(IUBMB) |
RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 [RN:R01853] |
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| Reaction(KEGG) |
R01853 > R02173 R02382 R02529 R02532 R02613 R02908 R04025 R04300
R04674 R04890 R04893 R08348;
(other) R02919 R04894 R04907 R04908 R06133 R08346 R08347
 |
|---|
| Substrate |
RCH2NHR';
H2O [CPD:C00001];
O2 [CPD:C00007] |
|---|
| Product |
RCHO [CPD:C00071];
R'NH2;
H2O2 [CPD:C00027] |
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| Cofactor |
FAD [CPD:C00016] |
|---|
| Comment |
A mitochondrial outer-membrane flavoprotein (FAD) that catalyses the
oxidative deamination of neurotransmitters and biogenic amines [3].
Acts on primary amines, and also on some secondary and tertiary
amines. It differs from EC 1.4.3.21, primary-amine oxidase as it can
oxidize secondary and tertiary amines but not methylamine. This
enzyme is inhibited by acetylenic compounds such as chlorgyline,
1-deprenyl and pargyline but, unlike EC 1.4.3.21 and EC 1.4.3.22
(diamine oxidase), it is not inhibited by semicarbazide. |
|---|
| Pathway |
PATH: ec00260 Glycine, serine and threonine metabolism
PATH: ec00330 Arginine and proline metabolism
PATH: ec00340 Histidine metabolism
PATH: ec00350 Tyrosine metabolism
PATH: ec00360 Phenylalanine metabolism
PATH: ec00380 Tryptophan metabolism
PATH: ec00950 Isoquinoline alkaloid biosynthesis
PATH: ec00982 Drug metabolism - cytochrome P450
PATH: ec01100 Metabolic pathways |
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| Orthology |
KO: K00274 monoamine oxidase |
|---|
| Genes |
HSA: 4128(MAOA) 4129(MAOB)
PTR: 740491(MAOA)
MCC: 708371(MAOA) 708468(MAOB)
MMU: 109731(Maob) 17161(Maoa)
RNO: 25750(Maob) 29253(Maoa)
CFA: 403450(MAOA) 403451(MAOB)
BTA: 281293(MAOA) 338445(MAOB)
SSC: 414424(MAOA) 414909(MAOB)
ECB: 100033867(MAOA) 100033868(MAOB)
MDO: 100027805
OAA: 100081953 100082010
GGA: 418561(MAOB)
TGU: 100223232
XLA: 495197
XTR: 100145726
DRE: 404730(mao)
BFO: BRAFLDRAFT_278561
CIN: 100178944
SPU: 583484 590198 760963
DPO: Dpse_GA12404
DAN: Dana_GF16121
DPE: Dper_GL23363
DGR: Dgri_GH14186
DMO: Dmoj_GI22096
AGA: AgaP_AGAP011321
AAG: AaeL_AAEL000542
CQU: CpipJ_CPIJ017420
AME: 551871
ISC: IscW_ISCW021957
NVE: NEMVE_v1g229539
CRE: CHLREDRAFT_187700
PAN: PODANSg2788
MGR: MGG_14365
FGR: FG05272.1
ANI: AN3291.2
AFM: AFUA_3G00100
AOR: AO090023000744 AO090103000118 AO090113000186
ANG: An01g01840 An12g05210 An12g10150 An13g03560
AFV: AFLA_011120 AFLA_096550 AFLA_111520
PCS: Pc16g03430
URE: UREG_02130 UREG_06244
CNE: CNL05890
CNB: CNBI0930
MBR: MONBRDRAFT_23499
DDI: DDB_0231707(maoA)
TET: TTHERM_00264690 TTHERM_00424660
XCC: XCC3278
XCB: XC_0886
XCA: xccb100_0906(lao)
XCV: XCV3541
XAC: XAC3426
XOM: XOO_1119
VFM: VFMJ11_A1186
PAE: PA0421
PAU: PA14_05480
PAP: PSPA7_0521
PAG: PLES_04191
PPU: PP_4983
PPF: Pput_4856
PPG: PputGB1_5032
PPW: PputW619_0482
PST: PSPTO_5074
PSB: Psyr_0455 Psyr_2888
PSP: PSPPH_0446
PFL: PFL_1384
PFO: Pfl01_2738 Pfl01_2742 Pfl01_5286
PFS: PFLU4065
PEN: PSEEN5045
PSA: PST_1610
AVN: Avin_03220
PAR: Psyc_1152
PCR: Pcryo_1131
PRW: PsycPRwf_2357
PAT: Patl_1720
PIN: Ping_1791
TTU: TERTU_3532
RPI: Rpic_4331
RPF: Rpic12D_4441 Rpic12D_4452
REU: Reut_C6401
REH: H16_A0831(maoB) H16_A0845(lao1)
BUR: Bcep18194_C6829 Bcep18194_C6833
BCN: Bcen_5037 Bcen_5048
BCH: Bcen2424_5812 Bcen2424_5823
BCM: Bcenmc03_4356 Bcenmc03_4367
BCJ: BCAM0112 BCAM0123
BXE: Bxe_B1535
BPT: Bpet4206
PNA: Pnap_1588
VEI: Veis_0808
CTT: CtCNB1_4355
LCH: Lcho_1418
AZO: azo2784
BBA: Bd2540
DOL: Dole_0266
DAT: HRM2_07830
MXA: MXAN_4930
SCL: sce9156
HOH: Hoch_5789
MLO: mll3668
PLA: Plav_2453
SME: SM_b21110
ARA: Arad_0120
AVI: Avi_2873
RET: RHE_PE00403(ype00210)
REC: RHECIAT_PA0000322
RLE: pRL110538 pRL120187
RLT: Rleg2_5659
RLG: Rleg_5306 Rleg_6595
BJA: blr0541
BRA: BRADO0266 BRADO1842 BRADO2376
BBT: BBta_0261 BBta_2164 BBta_2728
RPA: RPA0409
RPB: RPB_0104
RPC: RPC_0038
RPD: RPD_0698
RPE: RPE_0041
RPT: Rpal_0413
NWI: Nwi_0489
NHA: Nham_0613
OCA: OCAR_4306
XAU: Xaut_0102 Xaut_1419
AZC: AZC_3405 AZC_4484
MEX: Mext_4367
MEA: Mex_1p4817
MDI: METDI5413
MRD: Mrad2831_1384 Mrad2831_5276
MET: M446_3036
MPO: Mpop_0312
MCH: Mchl_4843
MNO: Mnod_4579
BID: Bind_1664 Bind_1769 Bind_3575
MSL: Msil_0744 Msil_1737
CCR: CC_2793
CCS: CCNA_02883
CAK: Caul_0148 Caul_1379
RDE: RD1_0535
MMR: Mmar10_0141
ACR: Acry_1970
GDI: GDI_2456
GDJ: Gdia_0704
RCE: RC1_3921
BAN: BA1924 BA2018
BAR: GBAA1924 GBAA2018
BAA: BA_2428 BA_2522
BAT: BAS1785 BAS1876
BAH: BAMEG_2568 BAMEG_2666
BAI: BAA_1994 BAA_2089
BCE: BC1925 BC2016
BCA: BCE_2008 BCE_2098
BCZ: BCZK1742 BCZK1830
BCR: BCAH187_A2029 BCAH187_A2131
BCB: BCB4264_A1928 BCB4264_A2020
BCU: BCAH820_1960 BCAH820_2053
BCG: BCG9842_B3289 BCG9842_B3414
BCQ: BCQ_1915 BCQ_2015
BCX: BCA_1990 BCA_2099
BTK: BT9727_1764 BT9727_1846
BTL: BALH_1703 BALH_1788
BWE: BcerKBAB4_1799 BcerKBAB4_1880
GTN: GTNG_0259
GYM: GYMC10_0703
GYC: GYMC61_1150
EAT: EAT1b_2144
BBE: BBR47_39680
PJD: Pjdr2_3197 Pjdr2_5155
CBO: CBO1197
CBA: CLB_1227
CBH: CLC_1239
CBY: CLM_1349
CBL: CLK_0635
CBK: CLL_A2339
CBB: CLD_3371
CBI: CLJ_B1237
CBF: CLI_1280
CBE: Cbei_2598 Cbei_4105
CPY: Cphy_2915
CCE: Ccel_1778
MTU: Rv3170(aofH)
MTC: MT3259
MRA: MRA_3203(aofH)
MTF: TBFG_13191
MTB: TBMG_03213(TBMG_03213.1)
MBO: Mb3195(aofH)
MBB: BCG_3194(aofH)
MBT: JTY_3189(aofH)
MPA: MAP3228
MAV: MAV_4062
MSM: MSMEG_2035
MUL: MUL_1281(aofH_1) MUL_2487(aofH)
MVA: Mvan_1178 Mvan_1866 Mvan_5578
MGI: Mflv_1230 Mflv_4501
MAB: MAB_2659
MMC: Mmcs_1556
MKM: Mkms_1580
MJL: Mjls_1526
MMI: MMAR_1389(aofH) MMAR_3362(aofH_1)
NFA: nfa26430 nfa30780
RHA: RHA1_ro01769 RHA1_ro05707
RER: RER_12600(lao) RER_44090(puo)
ROP: ROP_04530 ROP_14410 ROP_16910(lao) ROP_57750
GBR: Gbro_2005
ACH: Achl_0040
KRH: KRH_17330
MLU: Mlut_10320
XCE: Xcel_0068
NCA: Noca_4000
TCU: Tcur_3201
SRO: Sros_5603 Sros_8119
KRA: Krad_0085 Krad_2472
SEN: SACE_4116(aofH) SACE_4854
SAQ: Sare_2329
CAI: Caci_7142 Caci_7453
LBI: LEPBI_I1118
LBF: LBF_1077(aofA)
SRU: SRU_0427
DFE: Dfer_2278 Dfer_5079
CPI: Cpin_0081 Cpin_5972 Cpin_5977 Cpin_6047
GFO: GFO_1974
FJO: Fjoh_3835
OTE: Oter_1328 Oter_3468
SYN: slr0782
SYC: syc1144_c
SYF: Synpcc7942_0369
SYD: Syncc9605_0745 Syncc9605_1906
SYX: SynWH7803_0067
MAR: MAE_40250
CYP: PCC8801_0817 PCC8801_3473
CYN: Cyan7425_3896
CYH: Cyan8802_0846 Cyan8802_2643
NPU: Npun_R3302
TER: Tery_1366
RRS: RoseRS_2594 RoseRS_2925
RCA: Rcas_1864 Rcas_1963
CAU: Caur_1376
CAG: Cagg_2535
CHL: Chy400_1500
DRA: DR_A0274
DGE: Dgeo_1827
DDR: Deide_2p01780
 |
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| Structures |
PDB: 1DYU 1GOS 1JRQ 1O5W 1OJ9 1OJA 1OJB 1OJC 1OJD 1QAF
1QAK 1QAL 1S2Q 1S2Y 1S3B 1S3E 2BK3 2BK4 2BK5 2BXR
2BXS 2BYB 2C64 2C65 2C66 2C67 2C70 2C72 2C73 2C75
2C76 2V5Z 2V60 2V61 2VRL 2VRM 2VVL 2VVM 2VZ2 2W0Q
2Z5X 2Z5Y |
|---|
Reference
Authors
Title
Journal
|
1
Blaschko, H.
Amine oxidase.
In: Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd
ed., vol. 8, Academic Press, New York, 1963, p. 337-351. |
|---|
Reference
Authors
Title
Journal
|
2 [PMID:2644497]
Dostert PL, Strolin Benedetti M, Tipton KF.
Interactions of monoamine oxidase with substrates and inhibitors.
Med. Res. Rev. 9 (1989) 45-89. |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:15279562]
Edmondson DE, Mattevi A, Binda C, Li M, Hubalek F.
Structure and mechanism of monoamine oxidase.
Curr. Med. Chem. 11 (2004) 1983-93.
Homo sapiens [GN:hsa] |
|---|
Reference
Authors
Title
Journal
Organism
|
4 [PMID:15279563]
Shih JC, Chen K.
Regulation of MAO-A and MAO-B gene expression.
Curr. Med. Chem. 11 (2004) 1995-2005.
Homo sapiens [GN:hsa] |
|---|
Reference
Authors
Title
Journal
|
5 [PMID:15279561]
Tipton KF, Boyce S, O'Sullivan J, Davey GP, Healy J.
Monoamine oxidases: certainties and uncertainties.
Curr. Med. Chem. 11 (2004) 1965-82. |
|---|
Reference
Authors
Title
Journal
Organism
|
6 [PMID:16129825]
De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A.
Three-dimensional structure of human monoamine oxidase A (MAO A):
relation to the structures of rat MAO A and human MAO B.
Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 12684-9.
Homo sapiens [GN:hsa] |
|---|
Reference
Authors
Title
Journal
Organism
|
7 [PMID:16552415]
Youdim MB, Edmondson D, Tipton KF.
The therapeutic potential of monoamine oxidase inhibitors.
Nat. Rev. Neurosci. 7 (2006) 295-309.
Homo sapiens [GN:hsa] |
|---|
Reference
Authors
Title
Journal
Organism
|
8 [PMID:16402116]
Youdim MB, Bakhle YS.
Monoamine oxidase: isoforms and inhibitors in Parkinson's disease
and depressive illness.
Br. J. Pharmacol. 147 Suppl 1 (2006) S287-96.
Homo sapiens [GN:hsa] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 1.4.3.4
IUBMB Enzyme Nomenclature: 1.4.3.4
ExPASy - ENZYME nomenclature database: 1.4.3.4
UM-BBD (Biocatalysis/Biodegradation Database): 1.4.3.4
BRENDA, the Enzyme Database: 1.4.3.4
CAS: 9001-66-5 |
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