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 | Primary amine oxidase |
Enzyme Information
| 1.4.3.21 |
Primary-amine oxidase.
based on mapping to UniProt P46883
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)
| P46883 |
AMO_ECOLI
Escherichia coli K-12
Primary amine oxidase
|
PDB Structure
| PDB | 1JRQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Conserved tyrosine-369 in the active site of Escherichia coli copper amine oxidase is not essential.
Biochemistry
|
