CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.880 | Class I glutamine amidotransferase (GATase) domain |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.880 |
| Functional Family | Peptidase E |
Enzyme Information
| 3.4.13.21 |
Dipeptidase E.
based on mapping to UniProt P36936
Dipeptidase E catalyzes the hydrolysis of dipeptides Asp-|-Xaa. It does not act on peptides with N-terminal Glu, Asn or Gln, nor does it cleave isoaspartyl peptides.
-!- A free carboxy group is not absolutely required in the substrate since Asp-Phe-NH(2) and Asp-Phe-OMe are hydrolyzed somewhat more slowly than dipeptides with free C-termini. -!- No peptide larger than a C-blocked dipeptide is known to be a substrate. -!- Asp-NH-Np is hydrolyzed and is a convenient substrate for routine assay. -!- The enzyme is most active near pH 7.0, and is not inhibited by di-isopropylfluorophosphate or phenylmethanesulfonyl fluoride. -!- Belongs to peptidase family S51.
|
UniProtKB Entries (1)
| P36936 |
PEPE_SALTY
Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Peptidase E
|
PDB Structure
| PDB | 1FY2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad.
Proc.Natl.Acad.Sci.USA
|
