Any feedback?
No. of entries
Information on EC 3.4.13.21 - dipeptidase E
for references in articles please use BRENDA:EC3.4.13.21
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.13 Dipeptidases
3.4.13.21 dipeptidase E
IUBMB Comments
A free carboxy group is not absolutely required in the substrate since Asp-Phe-NH2 and Asp-Phe-OMe are hydrolysed 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 hydrolysed 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 in peptidase family S51.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 3.4.13.21
- dipeptide
-
enterica
-
serovar
- hydrolases
- synechocystis
- cyanobacteria
- cyanophycinase
- eubacteria
-
xenopus
- ser
-
cyanophycin
Reaction Schemes
showdipeptidase 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
Synonyms
aspartyl dipeptidase, asp-specific dipeptidase, dipeptidase e, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-aspartyl dipeptidase
-
-
-
-
Asp-specific dipeptidase
-
-
-
-
aspartyl dipeptidase
-
-
-
-
dipeptidase E
PepE
PepE gene product, Salmonella typhimurium
-
-
-
-
peptidase E
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 since Asp-Phe-NH2 and Asp-Phe-OMe are hydrolysed 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 hydrolysed 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 in peptidase family S51
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
278616-03-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Asp-beta-Ala + H2O
L-Asp + beta-Ala
-
Substrates: 28% of the activity with L-Asp-L-Leu
Products: -
Products: -
?
L-Asp-Gly + H2O
L-Asp + Gly
-
Substrates: 75% of the activity with L-Asp-L-Leu
Products: -
Products: -
?
L-Asp-L-Ala + H2O
L-Asp + L-Ala
-
Substrates: 153% of the activity with L-Asp-L-Leu
Products: -
Products: -
?
L-Asp-L-Asp + H2O
L-Asp + L-Asp
-
Substrates: 49% of the activity with L-Asp-L-Leu
Products: -
Products: -
?
L-Asp-L-Lys + H2O
L-Asp + L-Lys
-
Substrates: 168% of the activity with L-Asp-L-Leu
Products: -
Products: -
?
L-Asp-L-Phe + H2O
L-Asp + L-Phe
-
Substrates: 162% of the activity with L-Asp-L-Leu
Products: -
Products: -
?
L-Asp-L-Phe-methyl ester + H2O
L-Asp + L-Phe-methyl ester
-
Substrates: 14% of the activity with L-Asp-L-Leu
Products: -
Products: -
?
L-Asp-L-Phe-NH2 + H2O
L-Asp + L-Phe-NH2
-
Substrates: 37% of the activity with L-Asp-L-Leu
Products: -
Products: -
?
L-Asp-L-Ser + H2O
L-Asp + L-Ser
-
Substrates: 156% of the activity with L-Asp-L-Leu
Products: -
Products: -
?
L-Asp-L-Val + H2O
L-Asp + L-Val
-
Substrates: 94% of the activity with L-Asp-L-Leu
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
Substrates: -
Products: -
Products: -
?
L-Asp-Gly-Gly + H2O
?
-
Substrates: -
Products: -
Products: -
?
L-Asp-L-His + H2O
L-Asp + L-His
-
Substrates: -
Products: -
Products: -
?
L-Asp-L-His + H2O
L-Asp + L-His
-
Substrates: 200% of the activity with L-Asp-L-Leu
Products: -
Products: -
?
L-Asp-L-Leu + H2O
L-Asp + L-Leu
-
Substrates: -
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
Substrates: assay at 30°C, pH 10.0
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme does not contain zinc or any other metals
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetate
-
inhibition of wild-type but not of S120C mutant
N-ethylmaleimide
-
inhibition of wild-type but not of S120C mutant
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E-64, inhibition of wild-type but not of S120C mutant
additional information
-
not inhibited by EDTA, dipicolinic acid, DL-2-amino-2-methylpropanoate
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.26
L-Asp-4-nitroanilide
-
mutant N89H/Q153E/L205R
3.98
L-Asp-4-nitroanilide
-
wild-type
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.22
L-Asp-4-nitroanilide
-
wild-type
5.83
L-Asp-4-nitroanilide
-
mutant N89H/Q153E/L205R
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GenBank accession number P36936
-
-
brenda
GenBank accession number U01246
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (2074 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24770
-
calculation from sequence of cDNA
35000
-
gel filtration, non-denaturing PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
aspartate-bound structure at 1.83 A resolution. The enzyme forms a dimer, and the active site is located at the dimer interface. The stringent aspartate specificity of the enzyme is due to electrostatics and molecular complementarity in the active site
crystal structure at 1.2 A resolution
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N89H/Q153E/L205R
-
47fold increase in enzyme activity, increased stability
S120C
-
not inhibited by iodoacetate, N-ethylmaleimide, trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
30 min, 25% residual activity for wild-type, 80% residual activity for mutant N89H/Q153E/L205R
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
-
pepE in Lactococcus lactis has a significant effect on the hardness of fermented milk
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hkansson, K.; Wang, A.H.J.; Miller, C.G.
The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad
Proc. Natl. Acad. Sci. USA
97
14097-14102
2000
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Lassy, R.A.L.; Miller, C.G.
Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase
J. Bacteriol.
182
2536-2543
2000
Salmonella enterica subsp. enterica serovar Typhimurium, Xenopus laevis
brenda
Carter, T.H.; Miller, C.G.
Aspartate-specific peptidases in Salmonella typhimurium: mutants deficient in peptidase E
J. Bacteriol.
159
453-459
1984
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Conlin, C.A.; Hakensson, K.; Liljas, A.; Miller, C.G.
Cloning and nucleotide sequence of the cyclic AMP receptor protein-regulated Salmonella typhimurium pepE gene and crystallization of its product, an alpha-aspartyl dipeptidase
J. Bacteriol.
176
166-172
1994
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Ang, H.H.; Chan, K.L.; Mak, J.W.
Electrophoretic variations of peptidase E (PEPE) in characterizing clones and isolates of Plasmodium falciparum from different geographical areas
Folia Parasitol.
44
128-130
1997
Plasmodium falciparum
brenda
Kong, X.; Liu, Y.; Gou, X.; Zhu, S.; Zhang, H.; Wang, X.; Zhang, J.
Directed evolution of alpha-aspartyl dipeptidase from Salmonella typhimurium
Biochem. Biophys. Res. Commun.
289
137-142
2001
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kira, I.; Asano, Y.; Yokozeki, K.
Screening, purification, and identification of the enzyme producing N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester from l-isoasparagine and L-phenylalanine methyl ester
J. Biosci. Bioeng.
108
190-193
2009
Cedecea lapagei, Cedecea lapagei TPU 5750, Escherichia coli, Escherichia coli TPU 6303, Hafnia alvei, Hafnia alvei TPU 6440, Klebsiella aerogenes, Klebsiella aerogenes TPU 6151, Morganella morganii, Morganella morganii TPU 6501, Rahnella aquatilis, Rahnella aquatilis TPU 5901, Raoultella planticola, Raoultella planticola TPU 6501, Serratia marcescens, Serratia marcescens TPU 7303, Yersinia aldovae, Yersinia aldovae TPU 7650
brenda
Yadav, P.; Goyal, V.D.; Gaur, N.K.; Kumar, A.; Gokhale, S.M.; Makde, R.D.
Structure of Asp-bound peptidase E from Salmonella enterica Active site at dimer interface illuminates Asp recognition
FEBS Lett.
592
3346-3354
2018
Salmonella enterica subsp. enterica serovar Typhimurium (P36936)
brenda
Kuerman, M.; Wang, R.; Zhou, Y.; Tian, X.; Cui, Q.; Yi, H.; Gong, P.; Zhang, Z.; Lin, K.; Liu, T.; Zhang, L.
Metagenomic insights into bacterial communities and functional genes associated with texture characteristics of Kazakh artisanal fermented milk Ayran in Xinjiang, China
Food Res. Int.
164
112414
2023
Lactococcus lactis
brenda
EXTERNAL LINKS (specific for EC-Number 3.4.13.21)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
