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Information on EC 3.4.13.21 - dipeptidase E
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3.4.13.21 dipeptidase ESpecify your search results
Word Map
- 3.4.13.21
- dipeptides
-
enterica
-
serovar
- polymer
- hydrolases
- ser
- cyanobacteria
- synechocystis
- cyanophycinase
- eubacteria
-
cyanophycin
The enzyme appears in viruses and cellular organisms
Synonyms
asp-specific dipeptidase, aspartyl dipeptidase, dipeptidase e, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dipeptidase E
PepE
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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CAS REGISTRY NUMBER
COMMENTARY
278616-03-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-Asp-beta-Ala + H2O
L-Asp + beta-Ala
-
28% of the activity with L-Asp-L-Leu
-
?
L-Asp-Gly + H2O
L-Asp + Gly
-
75% of the activity with L-Asp-L-Leu
-
?
L-Asp-L-Ala + H2O
L-Asp + L-Ala
-
153% of the activity with L-Asp-L-Leu
-
?
L-Asp-L-Asp + H2O
L-Asp + L-Asp
-
49% of the activity with L-Asp-L-Leu
-
?
L-Asp-L-Lys + H2O
L-Asp + L-Lys
-
168% of the activity with L-Asp-L-Leu
-
?
L-Asp-L-Phe + H2O
L-Asp + L-Phe
-
162% of the activity with L-Asp-L-Leu
-
?
L-Asp-L-Phe-methyl ester + H2O
L-Asp + L-Phe-methyl ester
-
14% of the activity with L-Asp-L-Leu
-
?
L-Asp-L-Phe-NH2 + H2O
L-Asp + L-Phe-NH2
-
37% of the activity with L-Asp-L-Leu
-
?
L-Asp-L-Ser + H2O
L-Asp + L-Ser
-
156% of the activity with L-Asp-L-Leu
-
?
L-Asp-L-Val + H2O
L-Asp + L-Val
-
94% of the activity with L-Asp-L-Leu
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
?
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
-
-
-
?
L-Asp-L-His + H2O
L-Asp + L-His
-
-
-
?
L-Asp-L-His + H2O
L-Asp + L-His
-
200% of the activity with L-Asp-L-Leu
-
?
L-Asp-L-Leu + H2O
L-Asp + L-Leu
-
-
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
-
assay at 30°C, pH 10.0
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme does not contain zinc or any other metals
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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
-
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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
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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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GenBank accession number P36936
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-
brenda
GenBank accession number U01246
-
-
brenda
Show AA Sequence and Transmembrane Helices (2511 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.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24770
-
calculation from sequence of cDNA
35000
-
gel filtration, non-denaturing PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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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
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
-
30 min, 25% residual activity for wild-type, 80% residual activity for mutant N89H/Q153E/L205R
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Häkansson, 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
Klebsiella aerogenes, Escherichia coli, Hafnia alvei, Raoultella planticola, Morganella morganii, Rahnella aquatilis, Serratia marcescens, Yersinia aldovae, Cedecea lapagei, Klebsiella aerogenes TPU 6151, Yersinia aldovae TPU 7650, Rahnella aquatilis TPU 5901, Cedecea lapagei TPU 5750, Escherichia coli TPU 6303, Morganella morganii TPU 6501, Serratia marcescens TPU 7303, Hafnia alvei TPU 6440, Raoultella planticola TPU 6501
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), Salmonella enterica subsp. enterica serovar Typhimurium LT2 (P36936)
brenda
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