Dipeptidase E | |||||||||
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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 | ||||||||
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Dipeptidase E | |||||||
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Identifiers | |||||||
Organism | Salmonella typhimurium | ||||||
Symbol | PepE | ||||||
UniProt | P36936 | ||||||
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Dipeptidase E (EC 3.4.13.21, aspartyl dipeptidase, peptidase E, PepE gene product (Salmonella typhimurium)) is an enzyme. 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)
Hydrolase: proteases (EC 3.4) | |||||||||||||||
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3.4.11-19: Exopeptidase |
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3.4.21-25: Endopeptidase | |||||||||||||||
3.4.99: Unknown |
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