CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.220 | Leucine Aminopeptidase, subunit E; domain 1 |
|
3.40.220.10 | Leucine Aminopeptidase, subunit E, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Leucine Aminopeptidase, subunit E, domain 1 |
| Functional Family |
Enzyme Information
| 3.4.11.1 |
Leucyl aminopeptidase.
based on mapping to UniProt O86436
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
-!- Is activated by heavy metal ions. -!- Belongs to peptidase family M17. -!- Formerly EC 3.4.1.1.
|
| 3.4.11.10 |
Bacterial leucyl aminopeptidase.
based on mapping to UniProt O86436
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
-!- Similar aminopeptidases were isolated from Escherichia coli and Staphylococcus thermophilus. -!- Belongs to peptidase families M17 and M28.
|
UniProtKB Entries (1)
| O86436 |
AMPA_PSEPU
Pseudomonas putida
Cytosol aminopeptidase
|
PDB Structure
| PDB | 3H8E |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of the leucine aminopeptidase from Pseudomonas putida reveals the molecular basis for its enantioselectivity and broad substrate specificity.
J.Mol.Biol.
|
