CATH Classification
Level | CATH Code | Description |
---|---|---|
![]() |
2 | Mainly Beta |
![]() |
2.70 | Distorted Sandwich |
![]() |
2.70.98 | Beta-galactosidase; Chain A, domain 5 |
![]() |
2.70.98.20 | Copper amine oxidase, catalytic domain |
Domain Context
CATH Clusters
Superfamily | Copper amine oxidase, catalytic domain |
Functional Family | Amine oxidase |
Enzyme Information
1.4.3.21 |
Primary-amine oxidase.
based on mapping to UniProt P12807
RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2).
-!- A group of enzymes that oxidize primary monoamines but have little or no activity toward diamines, such as histamine, or toward secondary and tertiary amines. -!- They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and, unlike EC 1.4.3.4, are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. -!- In some mammalian tissues the enzyme also functions as a vascular- adhesion protein (VAP-1). -!- Formerly EC 1.4.3.6.
|
UniProtKB Entries (1)
P12807 |
AMO_PICAN
Ogataea angusta
Peroxisomal primary amine oxidase
|
PDB Structure
PDB | 3SX1 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with CuI and CoII.
Acta Crystallogr.,Sect.F
|