CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.50 | FAD/NAD(P)-binding domain |
|
3.50.50.60 | FAD/NAD(P)-binding domain |
Domain Context
CATH Clusters
| Superfamily | FAD/NAD(P)-binding domain |
| Functional Family |
Enzyme Information
| 1.4.3.4 |
Monoamine oxidase.
based on mapping to UniProt P46882
RCH(2)NHR' + H(2)O + O(2) = RCHO + R'NH(2) + H(2)O(2).
-!- 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.
|
UniProtKB Entries (1)
| P46882 |
AOFN_ASPNG
Aspergillus niger
Monoamine oxidase N
|
PDB Structure
| PDB | 2VVM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Structure of Monoamine Oxidase from Aspergillus Niger Provides a Molecular Context for Improvements in Activity Obtained by Directed Evolution.
J.Mol.Biol.
|
