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Enzyme Nomenclature
Information on EC 3.4.13.21 - dipeptidase E
for references in articles please use BRENDA:EC3.4.13.21
Word Map on EC 3.4.13.21
- 3.4.13.21
- dipeptides
-
serovar
-
enterica
- cyanophycinase
- cyanobacteria
- synechocystis
-
cyanophycin
- ser
- eubacteria
- leucine
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.4.13.21
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RECOMMENDED NAME
GeneOntology No.
dipeptidase E
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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
hydrolysis of peptide bond
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-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
278616-03-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
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-
?
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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-
?
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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-
?
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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-
?
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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-
?
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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INHIBITORS
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
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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
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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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PDB
SCOP
CATH
ORGANISM
UNIPROT
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
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gel filtration, non-denaturing PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure at 1.2 A resolution
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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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ENGINEERING
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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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.13.21)
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