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ENZYME

ENZYME entry: EC 3.4.13.21

PURL: https://purl.expasy.org/enzyme/EC/3.4.13.21
Accepted Name
dipeptidase E
Alternative Name(s)
aspartyl dipeptidase
PepE gene product (Salmonella typhimurium)
peptidase E
Reaction catalysed
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
Comment(s)
  • A free carboxy group is not absolutely required in the substrate since Asp-Phe-NH2 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.
Cross-references
BRENDA3.4.13.21
EC2PDB3.4.13.21
ExplorEnz3.4.13.21
KEGG Ligand Database for Enzyme Nomenclature3.4.13.21
IUBMB Enzyme Nomenclature3.4.13.21
MEDLINEFind literature relating to 3.4.13.21
MetaCyc3.4.13.21
Rhea expert-curated reactions3.4.13.21
UniProtKB/Swiss-Prot
A3N0N1, PEPE_ACTP2B3H1L0, PEPE_ACTP7B0BPF6, PEPE_ACTPJ
A8ANB2, PEPE_CITK8Q9VYH3, PEPE_DROMEA7ZUN5, PEPE_ECO24
B7UPH5, PEPE_ECO27B7MJ04, PEPE_ECO45B7LAW3, PEPE_ECO55
P0A7C7, PEPE_ECO57B5Z0B3, PEPE_ECO5EB7NRV3, PEPE_ECO7I
B7MRE6, PEPE_ECO81B7M7S7, PEPE_ECO8AC5A0V8, PEPE_ECOBW
B1XC20, PEPE_ECODHA8A7B7, PEPE_ECOHSA1AIJ2, PEPE_ECOK1
Q0TA47, PEPE_ECOL5Q8FB55, PEPE_ECOL6B1IUN1, PEPE_ECOLC
P0A7C6, PEPE_ECOLIB7NFV7, PEPE_ECOLUB6I5M9, PEPE_ECOSE
B1LPH7, PEPE_ECOSMQ1R3S5, PEPE_ECOUTQ4QMU5, PEPE_HAEI8
A5UHB4, PEPE_HAEIGP44766, PEPE_HAEINP58493, PEPE_NOSS1
Q9CNH7, PEPE_PASMUB5F1K4, PEPE_SALA4A9MHB2, PEPE_SALAR
Q57H37, PEPE_SALCHB5R7Q9, PEPE_SALG2B4TDG7, PEPE_SALHS
B4T1N0, PEPE_SALNSQ5PKZ6, PEPE_SALPAA9N1I0, PEPE_SALPB
C0Q494, PEPE_SALPCB5BJT4, PEPE_SALPKB4TQM9, PEPE_SALSV
P58494, PEPE_SALTIP36936, PEPE_SALTYA1S5J3, PEPE_SHEAM
B8E718, PEPE_SHEB2A3D5N8, PEPE_SHEB5A6WPJ2, PEPE_SHEB8
A9L579, PEPE_SHEB9Q12MB3, PEPE_SHEDOQ8EDL3, PEPE_SHEON
A4Y7X3, PEPE_SHEPCA0KY73, PEPE_SHESAQ0HHP4, PEPE_SHESM
Q0HTZ6, PEPE_SHESRA1RIL5, PEPE_SHESWB2TX41, PEPE_SHIB3
Q31TY2, PEPE_SHIBSQ0SXY7, PEPE_SHIF8Q83PB5, PEPE_SHIFL
Q3YUW9, PEPE_SHISSQ93RZ5, PEPE_STRCOQ91642, PEPE_XENLA

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.13.-
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