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Information on EC 3.4.15.5 - Peptidyl-dipeptidase Dcp and Organism(s) Escherichia coli and UniProt Accession P24171

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     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.15 Peptidyl-dipeptidases
                3.4.15.5 Peptidyl-dipeptidase Dcp
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Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P24171 not found.
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
dipeptidyl carboxypeptidase, dipeptidylcarboxypeptidase, lddcp, k-26-dcp, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DCP
292397
-
Dipeptidyl carboxypeptidase
dipeptidyl carboxypeptidase II
292397
-
additional information
292397
the enzyme belongs to the metallopeptidase family M3
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
0
CAS REGISTRY NUMBER
COMMENTARY hide
9015-82-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
angiotensin I + H2O
DRVYIHPF + His-Leu
show the reaction diagram
i.e. DRVYIHPFHL, hydrolysis at the F-H bond generating angiotensin II
-
-
?
bradykinin + H2O
RPPGF + Ser-Pro + Phe-Arg
show the reaction diagram
i.e. RPPGFSPFR, hydrolysis at at sequential cleavage sites releasing the C-terminal dipeptides F-R and S-P
-
-
?
o-aminobenzoyl-FRAK(2,4-dinitrophenyl)-OH + H2O
o-aminobenzoyl-FR + AK(2,4-dinitrophenyl)-OH
show the reaction diagram
an ACE substrate, Dcp hydrolyzes at the R-A bond
-
-
?
o-aminobenzoyl-FRK(2,4-dinitrophenyl)P-OH + H2O
o-aminobenzoyl-FR + K(2,4-dinitrophenyl)P-OH
show the reaction diagram
an ACE substrate, Dcp hydrolyzes at the R-K bond
-
-
?
o-aminobenzoyl-LFK(2,4-dinitrophenyl)-OH + H2O
o-aminobenzoyl-L + FK(2,4-dinitrophenyl)-OH
show the reaction diagram
an ACE substrate, Dcp hydrolyzes at the L-F bond
-
-
?
4-Nitrobenzyloxycarbonyl-Gly-(S-4-nitrobenzo-2-oxa-1,3-diazole)-Cys-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
4-Nitrobenzyloxycarbonyl-Gly-Phe-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
Acetyl-Ala-Ala-Ala + H2O
Acetyl-Ala + Ala-Ala
show the reaction diagram
-
-
-
?
Acetyl-Ala3 + H2O
?
show the reaction diagram
-
the enzyme is required for the utilization of acetyl-Ala3 as a sole nitrogen source
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
show the reaction diagram
-
-
-
?
Ala-Ala-Ala-Lys-Phe + H2O
Ala-Ala-Ala + Lys-Phe
show the reaction diagram
-
-
-
?
Ala-Ala-Phe-Ala + H2O
Ala-Ala + Phe-Ala
show the reaction diagram
-
-
-
-
?
Ala-Gly-Phe-Ala + H2O
Ala-Gly + Phe-Ala
show the reaction diagram
-
-
-
-
?
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg + H2O
?
show the reaction diagram
-
-
-
-
?
Benzyloxycarbonyl-Ala-Ala-Ala + H2O
Benzyloxycarbonyl-Ala + Ala-Ala
show the reaction diagram
-
-
-
?
Dinitrophenyl-poly-(Pro-Gly-Pro) + H2O
Gly-Pro + ?
show the reaction diagram
-
-
-
?
Gly-Ala-Phe-Ala + H2O
Gly-Ala + Phe-Ala
show the reaction diagram
-
-
-
-
?
Gly-Gly-Phe-Ala + H2O
Gly-Gly + Phe-Ala
show the reaction diagram
-
-
-
?
Hippuric acid-His-Leu + H2O
Hippuric acid + His-Leu
show the reaction diagram
-
-
-
?
Lys-Ala-Ala-Lys-Ala-Ala + H2O
Lys-Ala + Ala-Lys-Ala-Ala
show the reaction diagram
-
-
-
?
Lys-Lys-Lys-Lys + H2O
Lys-Lys + Lys-Lys
show the reaction diagram
-
-
-
?
tert-butyloxycarbonyl-Ala-Ala-Ala + H2O
tert-butyloxycarbonyl-Ala + Ala-Ala
show the reaction diagram
-
-
-
-
?
tert-Butyloxycarbonyl-Ala-Glu-Ala-Ala + H2O
tert-Butyloxycarbonyl-Ala-Glu + Ala-Ala
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Acetyl-Ala3 + H2O
?
show the reaction diagram
-
the enzyme is required for the utilization of acetyl-Ala3 as a sole nitrogen source
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates
Co2+
-
activates
Mn2+
-
activates
Zinc
-
metallopeptidase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
lisinopril-Trp
-
1,10-phenanthroline
-
-
captopril
-
-
chymostatin
-
-
pepstatin
-
-
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E-64
Trypsin inhibitor
-
from lima bean and from bovine pancreas
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00066
o-aminobenzoyl-FRAK(2,4-dinitrophenyl)-OH
pH 8.0, 37°C, recombinant enzyme
0.00029
o-aminobenzoyl-FRK(2,4-dinitrophenyl)P-OH
pH 8.0, 37°C, recombinant enzyme
0.00255
o-aminobenzoyl-LFK(2,4-dinitrophenyl)-OH
pH 8.0, 37°C, recombinant enzyme
1.27
Ala-Ala-Phe-Ala
-
-
0.61
Ala-Gly-Phe-Ala
-
-
0.44
Ala4
-
-
1.39
Gly-Ala-Phe-Ala
-
-
6.06
Gly-Gly-Phe-Ala
-
-
0.1
Lys4
-
-
0.71
tert-butyloxycarbonyl-Ala-Ala-Ala
-
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.1
o-aminobenzoyl-FRAK(2,4-dinitrophenyl)-OH
pH 8.0, 37°C, recombinant enzyme
0.81
o-aminobenzoyl-FRK(2,4-dinitrophenyl)P-OH
pH 8.0, 37°C, recombinant enzyme
1.4
o-aminobenzoyl-LFK(2,4-dinitrophenyl)-OH
pH 8.0, 37°C, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1667
o-aminobenzoyl-FRAK(2,4-dinitrophenyl)-OH
pH 8.0, 37°C, recombinant enzyme
2793
o-aminobenzoyl-FRK(2,4-dinitrophenyl)P-OH
pH 8.0, 37°C, recombinant enzyme
538
o-aminobenzoyl-LFK(2,4-dinitrophenyl)-OH
pH 8.0, 37°C, recombinant enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.022
(5S)-5-[(N-benzoyl)amino]-4-oxo-6-phenylhexanoyl-L-tryptophan
-
0.000003
captopril
-
0.0044
lisinopril
-
0.0008
lisinopril-Trp
-
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
Escherichia coli K-12
additional information
-
pI: 5.29, Escherichia coli, 5.06, Salmonella typhimurium
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
activity range, profile, overview
5 - 7.5
-
pH 5.0: 50% of activity maximum, pH 7.5: activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 42
-
37°C: 75% of activity maximum, 42°C: activity maximum
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
77500
-
E. coli, calculation from nucleotide sequence
78000
-
1 * 78000, SDS-PAGE
97000
-
E. coli B, gradient PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 78000, SDS-PAGE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization in presence of a octapeptide inhibitor, sitting-drop vapor-diffusion procedure, 2.0 A resolution, indication of a ligand-dependent hinge movement mechanism
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, retains 70% of the original activity after 5 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged Dcp from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
phylogenetic analysis, expression of His-tagged Dcp in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Conlin, C.A.; Miller, C.G.
Dipeptidyl carboxypeptidase and oligopeptidase A from Escherichia coli and Salmonella typhimurium
Methods Enzymol.
248
567-579
1995
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
Manually annotated by BRENDA team
Henrich, B.; Becker, S.; Schroeder, U.; Plapp, R.
Dcp gene of Escherichia coli: cloning, sequencing, transcript mapping, and characterization of the gene product
J. Bacteriol.
175
7290-7300
1993
Escherichia coli
Manually annotated by BRENDA team
Yaron, A.
Dipeptidyl carboxypeptidase from Escherichia coli
Methods Enzymol.
45
599-610
1976
Escherichia coli, Escherichia coli B / ATCC 11303
Manually annotated by BRENDA team
Comellas-Bigler, M.; Lang, R.; Bode, W.; Maskos, K.
Crystal structure of the E. coli dipeptidyl carboxypeptidase Dcp: further indication of a ligand-dependent hinge movement mechanism
J. Mol. Biol.
349
99-112
2005
Escherichia coli (P24171), Escherichia coli
Manually annotated by BRENDA team
Cunha, C.E.; Magliarelli, H.d.e..F.; Paschoalin, T.; Nchinda, A.T.; Lima, J.C.; Juliano, M.A.; Paiva, P.B.; Sturrock, E.D.; Travassos, L.R.; Carmona, A.K.
Catalytic properties of recombinant dipeptidyl carboxypeptidase from Escherichia coli: a comparative study with angiotensin I-converting enzyme
Biol. Chem.
390
931-940
2009
Escherichia coli (P24171), Escherichia coli
Manually annotated by BRENDA team
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