_EC 1.4.3.4 Monoamine oxidase. 50 PDB entries  
EC 1.-.-.- Oxidoreductases. [8,609 PDB entries]
EC 1.4.-.- Acting on the CH-NH(2) group of donors. [358 PDB entries]
EC 1.4.3.- With oxygen as acceptor. [214 PDB entries]
EC 1.4.3.4 Monoamine oxidase. [50 PDB entries]    
1gos

Reaction: RCH(2)NHR' + H(2)O + O(2) = Rcho + R'NH(2) + H(2)O(2).
 

RCH(2)NHR'
+ H(2)O
+
O(2)
=
RCHO
+ R'NH(2)
+
H(2)O(2)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Adrenaline oxidase. Amine oxidase. Amine oxidase (flavin-containing). Tyraminase. Tyramine oxidase.
Cofactor(s): Fad.
 

FAD
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments: Catalyzes the oxidative deamination of neurotransmitters and biogenic amines. Acts on primary amines, and also on some secondary and tertiary amines. It differs from Ec 1.4.3.21, as it can oxidize secondary and tertiary amines but not methylamine. Inhibited by acetylenic compounds such as chlorgyline, 1-deprenyl and pargyline but, unlike Ec 1.4.3.21 and Ec 1.4.3.22, it is not inhibited by semicarbazide. Formerly Ec 1.4.3.9.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 50 PDB entries in enzyme class E.C.1.4.3.4

  PDB code Protein
1gos
Human monoamine oxidase b
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (497 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1h8q
Human monoamine oxidase type a (truncated)
Source: Homo sapiens. Human. Other_details: mitochondrial outer membrane
Chain: A (455 residues)
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1h8r
Human monoamine oxidase type b (truncated)
Source: Homo sapiens. Human. Other_details: mitochondrial outer membrane
Chain: A (455 residues)
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1o5w
The structure basis of specific recognitions for substrates and inhibitors of rat monoamine oxidase a
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
Chains: A, B, C, D (511 residues) CATH domain: 3.50.50.60
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1oj9
Human monoamine oxidase b in complex with 1,4-diphenyl-2-butene
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1oja
Human monoamine oxidase b in complex with isatin
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1ojb
Human monoamine oxidase b in complex with tranylcypromine
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1ojc
Human monoamine oxidase b in complex with n-(2-aminoethyl)-p-chlorobenzamide
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1ojd
Human monoamine oxidase b in complex with lauryldimethylamine-n-oxide (ldao)
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B, C, D, E, F, G, H, I, L (497 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1s2q
Crystal structure of maob in complex with n-propargyl-1(r)-a (rasagiline)
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1s2y
Crystal structure of maob in complex with n-propargyl-1(s)- aminoindan
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1s3b
Crystal structure of maob in complex with n-methyl-n- propargyl-1(r)-aminoindan
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
1s3e
Crystal structure of maob in complex with 6-hydroxy-n- propargyl-1(r)-aminoindan
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2bk3
Human monoamine oxidase b in complex with farnesol
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2bk4
Human monoamine oxidase b: i199f mutant in complex with rasagiline
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2bk5
Human monoamine oxidase b: i199f mutant in complex with isatin
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2bxr
Human monoamine oxidase a in complex with clorgyline, crystal form a
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (445 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2bxs
Human monoamine oxidase a in complex with clorgyline, crystal form b
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (490 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2byb
Human monoamine oxidase b in complex with deprenyl
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2c64
Mao inhibition by rasagiline analogues
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2c65
Mao inhibition by rasagiline analogues
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2c66
Mao inhibition by rasagiline analogues
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2c67
Mao inhibition by rasagiline analogues
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2c70
Functional role of the aromatic cage in human monoamine oxidase b: structures and catalytic properties of tyr435 mutant proteins
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2c72
Functional role of the aromatic cage in human monoamine oxidase b: structures and catalytic properties of tyr435 mutant proteins
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2c73
Functional role of the aromatic cage in human monoamine oxidase b: structures and catalytic properties of tyr435 mutant proteins
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2c75
Functional role of the aromatic cage in human monoamine oxidase b: structures and catalytic properties of tyr435 mutant proteins
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2c76
Functional role of the aromatic cage in human monoamine oxidase b: structures and catalytic properties of tyr435 mutant proteins
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2v5z
Structure of human mao b in complex with the selective inhibitor safinamide
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2v60
Structure of human mao b in complex with the selective inhibitor 7-(3-chlorobenzyloxy)-4-carboxaldehyde-coumarin
Source: Homo sapiens. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2v61
Structure of human mao b in complex with the selective inhibitor 7-(3-chlorobenzyloxy)-4-(methylamino)methyl- coumarin
Source: Homo sapiens. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2vrl
Structure of human mao b in complex with benzylhydrazine
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2vrm
Structure of human mao b in complex with phenyethylhydrazine
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2vvl
The structure of mao-n-d3, a variant of monoamine oxidase from aspergillus niger.
Source: Aspergillus niger. Organism_taxid: 5061. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H (478 residues) CATH domain: 3.50.50.60
Bound ligands:   Het Group EDO is 40.00% similar to enzyme product aldehyde
  Het Group FAD corresponds to enzyme cofactor FAD
2vvm
The structure of mao-n-d5, a variant of monoamine oxidase from aspergillus niger.
Source: Aspergillus niger. Organism_taxid: 5061. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (481 residues) CATH domain: 3.50.50.60
Bound ligands:   Het Group EDO is 40.00% similar to enzyme product aldehyde
  Het Group FAD corresponds to enzyme cofactor FAD
2vz2
Human mao b in complex with mofegiline
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2xcg
Tranylcypromine-inhibited human monoamine oxidase b in complex with 2-(2-benzofuranyl)-2-imidazoline
Source: Homo sapiens. Human. Organism_taxid: 9606
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FA8 corresponds to enzyme cofactor FAD
2xfn
Human monoamine oxidase b in complex with 2-(2-benzofuranyl) -2-imidazoline
Source: Homo sapiens. Human. Organism_taxid: 9606
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2xfo
Tranylcypromine-inhibited human monoamine oxidase b ile199ala mutant in complex with 2-(2-benzofuranyl)-2- imidazoline
Source: Homo sapiens. Human. Organism_taxid: 9606
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FA8 corresponds to enzyme cofactor FAD
2xfp
Isatin-inhibited human monoamine oxidase b in complex with 2-(2-benzofuranyl)-2-imidazoline
Source: Homo sapiens. Human. Organism_taxid: 9606
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2xfq
Rasagiline-inhibited human monoamine oxidase b in complex with 2-(2-benzofuranyl)-2-imidazoline
Source: Homo sapiens. Human. Organism_taxid: 9606
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2xfu
Human monoamine oxidase b with tranylcypromine
Source: Homo sapiens. Human. Organism_taxid: 9606
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FA8 corresponds to enzyme cofactor FAD
2z5x
Crystal structure of human monoamine oxidase a with harmine
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
Chain: A (513 residues) CATH domain: 3.50.50.60
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
2z5y
Crystal structure of human monoamine oxidase a (g110a) with harmine
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
Chain: A (513 residues) CATH domain: 3.50.50.60
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
3po7
Human monoamine oxidase b in complex with zonisamide
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: maob. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
3zdn
D11-c mutant of monoamine oxidase from aspergillus niger
Source: Aspergillus niger. Organism_taxid: 5061. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta.
Chains: A, B, C, D (478 residues) CATH domain: 3.50.50.60
Bound ligands:   Het Group EDO is 40.00% similar to enzyme product aldehyde
  Het Group FAD corresponds to enzyme cofactor FAD
3zyx
Crystal structure of human monoamine oxidase b in complex with methylene blue and bearing the double mutation i199a- y326a
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
4a79
Crystal structure of human monoamine oxidase b (mao b) in complex with pioglitazone
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
4a7a
Crystal structure of human monoamine oxidase b (mao b) in complex with rosiglitazone
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Chains: A, B (499 residues) CATH domains: 3.50.50.60 3.90.660.10 1.10.405.10
Bound ligand:   Het Group FAD corresponds to enzyme cofactor FAD
4ffu
Crystal structure of putative maoc-like (monoamine oxidase-l protein, similar to nodn from sinorhizo bium meliloti 1021
Source: Sinorhizobium meliloti. Ensifer meliloti. Organism_taxid: 266834. Strain: 1021. Gene: rb0689, sm_b21110. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H, I, J, K, L (155 residues) CATH domain: 3.10.129.10