CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.800 | Arginase; Chain A |
|
3.40.800.20 | Histone deacetylase domain |
Domain Context
CATH Clusters
| Superfamily | Histone deacetylase domain |
| Functional Family |
Enzyme Information
| 3.5.1.62 |
Acetylputrescine deacetylase.
based on mapping to UniProt Q48935
N-acetylputrescine + H(2)O = acetate + putrescine.
-!- The enzyme from Micrococcus luteus also acts on N(8)-acetylspermidine and acetylcadaverine, but more slowly.
|
| 3.5.1.48 |
Acetylspermidine deacetylase.
based on mapping to UniProt Q48935
N(8)-acetylspermidine + H(2)O = acetate + spermidine.
-!- It was initially thought that N(1)-acetylspermidine was the substrate for this deacetylase reaction but this has since been disproved.
|
| 3.5.1.- |
In linear amides.
based on mapping to UniProt Q48935
|
UniProtKB Entries (1)
| Q48935 |
APAH_MYCRA
Mycoplana ramosa
Acetylpolyamine amidohydrolase
|
PDB Structure
| PDB | 3Q9E |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of prokaryotic polyamine deacetylase reveals evolutionary functional relationships with eukaryotic histone deacetylases .
Biochemistry
|
