| Dipeptidase E | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.13.21 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
| Dipeptidase E | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | PepE | ||||||
| UniProt | P36936 | ||||||
| |||||||
Dipeptidase E (EC 3.4.13.21, aspartyl dipeptidase, peptidase E, PepE gene product (Salmonella typhimurium)) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Dipeptidase E catalyses 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.
References
- ↑ Håkansson K, Wang AH, Miller CG (December 2000). "The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad". Proceedings of the National Academy of Sciences of the United States of America. 97 (26): 14097–102. Bibcode:2000PNAS...9714097H. doi:10.1073/pnas.260376797. PMC 18877. PMID 11106384.
- ↑ Lassy RA, Miller CG (May 2000). "Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase". Journal of Bacteriology. 182 (9): 2536–43. doi:10.1128/jb.182.9.2536-2543.2000. PMC 111318. PMID 10762256.
External links
- Dipeptidase+E at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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