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
| 3.4.11.5 |
Prolyl aminopeptidase.
based on mapping to UniProt Q10712
Release of N-terminal proline from a peptide.
-!- Present in the cytosol of mammalian and microbial cells. -!- In contrast to the mammalian form, the bacterial form of the enzyme hydrolyzes both polyproline and prolyl-2-naphthylamide. -!- The mammalian enzyme, which is not specific for prolyl bonds, is possibly identical with EC 3.4.11.1. -!- Belongs to peptidase family S33. -!- Formerly EC 3.4.1.4.
|
| 3.4.11.1 |
Leucyl aminopeptidase.
based on mapping to UniProt Q10712
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.
|
UniProtKB Entries (1)
| Q10712 |
AMPL1_SOLLC
Solanum lycopersicum
Leucine aminopeptidase 1, chloroplastic
|
PDB Structure
| PDB | 4KSI |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of tomato wound-induced leucine aminopeptidase sheds light on substrate specificity.
Acta Crystallogr.,Sect.D
|
