Information on EC 3.4.13.21 - dipeptidase E

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
3.4.13.21
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RECOMMENDED NAME
GeneOntology No.
dipeptidase E
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REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
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 hide
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY hide
278616-03-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-Asp-4-nitroanilide + H2O
L-Asp + 4-nitroaniline
show the reaction diagram
L-Asp-beta-Ala + H2O
L-Asp + beta-Ala
show the reaction diagram
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28% of the activity with L-Asp-L-Leu
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?
L-Asp-Gly + H2O
L-Asp + Gly
show the reaction diagram
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75% of the activity with L-Asp-L-Leu
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?
L-Asp-Gly-Gly + H2O
?
show the reaction diagram
L-Asp-L-Ala + H2O
L-Asp + L-Ala
show the reaction diagram
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153% of the activity with L-Asp-L-Leu
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?
L-Asp-L-Asp + H2O
L-Asp + L-Asp
show the reaction diagram
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49% of the activity with L-Asp-L-Leu
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?
L-Asp-L-His + H2O
L-Asp + L-His
show the reaction diagram
L-Asp-L-Leu + H2O
L-Asp + L-Leu
show the reaction diagram
L-Asp-L-Lys + H2O
L-Asp + L-Lys
show the reaction diagram
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168% of the activity with L-Asp-L-Leu
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?
L-Asp-L-Phe + H2O
L-Asp + L-Phe
show the reaction diagram
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162% of the activity with L-Asp-L-Leu
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?
L-Asp-L-Phe-methyl ester + H2O
L-Asp + L-Phe-methyl ester
show the reaction diagram
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14% of the activity with L-Asp-L-Leu
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?
L-Asp-L-Phe-NH2 + H2O
L-Asp + L-Phe-NH2
show the reaction diagram
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37% of the activity with L-Asp-L-Leu
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?
L-Asp-L-Ser + H2O
L-Asp + L-Ser
show the reaction diagram
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156% of the activity with L-Asp-L-Leu
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?
L-Asp-L-Val + H2O
L-Asp + L-Val
show the reaction diagram
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94% of the activity with L-Asp-L-Leu
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?
L-isoasparagine + L-phenylalanine methyl ester
N-(L-alpha-L-aspartyl)-L-phenylalanine methyl ester + ?
show the reaction diagram
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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the enzyme does not contain zinc or any other metals
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
iodoacetate
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inhibition of wild-type but not of S120C mutant
N-ethylmaleimide
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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
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not inhibited by EDTA, dipicolinic acid, DL-2-amino-2-methylpropanoate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.26 - 4.3
L-Asp-4-nitroanilide
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.22 - 39
L-Asp-4-nitroanilide
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0014
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substrate L-Asp-4-nitroanilide
3.39
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purified enzyme
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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 hide
LITERATURE
24770
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calculation from sequence of cDNA
25000
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SDS-PAGE
35000
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gel filtration, non-denaturing PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
60
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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
yield of 1.2% after 5-20% gradient acrylamide slab gel
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N89H/Q153E/L205R
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47fold increase in enzyme activity, increased stability
S120C
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not inhibited by iodoacetate, N-ethylmaleimide, trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
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Show AA Sequence (944 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 3.4.13.21)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)