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Information on EC 3.4.14.4 - dipeptidyl-peptidase III
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3.4.14.4 dipeptidyl-peptidase IIISpecify your search results
Word Map
- 3.4.14.4
-
exopeptidase
- tynorphin
-
enkephalin-degrading
- leu-enkephalin
-
nudix
- spinorphin
-
hexxh
-
map2k5
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
Synonyms
dpp iii, dipeptidyl peptidase iii, nudt3, enkephalinase b, dppiii, dpp-iii, dipeptidyl aminopeptidase iii, dipeptidyl-peptidase iii, dipeptidylpeptidase iii, dipeptidyl-peptide hydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BT_1846
Cabys_2252
dipeptdiyl peptidase III
dipeptidyl aminopeptidase III
dipeptidyl arylamidase III
dipeptidyl peptidase III
dipeptidyl-peptidase III
dipeptidyl-peptide hydrolase
-
-
-
-
dipeptidylpeptidase III
DPP III
DPP-3
enkephalinase B
peptidase, dipeptidyl, III
-
-
-
-
red cell angiotensinase
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-
-
-
dipeptidyl aminopeptidase III
-
-
-
-
dipeptidyl arylamidase III
-
-
-
-
dipeptidylpeptidase III
-
-
-
-
enkephalinase B
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
exopeptidase, N-terminus, dipeptide
-
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CAS REGISTRY NUMBER
COMMENTARY
77464-87-0
-
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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
Ala-Ala-2-naphthylamide + H2O
Ala-Ala + 2-naphtylamine
assay at 37°C, pH 8.0
-
-
?
Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala
-
action of goat brain DPP-III on the peptide is investigated, substrate is hydrolyzed
-
-
?
Ala-Ala-beta-naphthylamide + H2O
Ala-Ala + beta-naphthylamine
-
10.0% activity
-
-
?
Ala-Phe-2-naphthylamide + H2O
Ala-Phe + 2-naphthylamine
-
-
-
?
Ala-Phe-2-naphthylamide + H2O
Ala-Phe + 2-naphtylamine
assay at 37°C, pH 8.0
-
-
?
Arg-Arg-4-methoxy-beta-naphthylamide + H2O
Arg-Arg + 4-methoxy-beta-naphthylamine
-
activity assay, 100% activity
-
-
?
Arg-Arg-4-methylcoumarin 7-amide + H2O
Arg-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Arg-Arg-7-amido-4-methylcoumarin + H2O
Arg-Arg + 7-amino-4-methylcoumarin
-
assay at 37°C
-
-
?
Arg-Arg-beta-naphthylamide + H2O
Arg-Arg + beta-naphthylamine
-
-
-
-
?
Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu + H2O
?
-
angiotensin III, action of goat brain DPP-III on the peptide is investigated, substrate is hydrolyzed
-
-
?
arginyl-arginyl-4-methoxy-beta-naphthylamide + H2O
Arg-Arg + 4-methoxy-beta-naphthylamine
-
substrate used in the activity assay
-
-
?
Asp-Ala-beta-naphthylamide + H2O
Asp-Ala + beta-naphthylamine
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0% activity
-
-
?
Asp-Arg-beta-naphthylamide + H2O
Asp-Arg + beta-naphthylamine
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1.5% activity
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-
?
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe + H2O
?
-
angiotensin II, action of goat brain DPP-III on the peptide is investigated, substrate is hydrolyzed
-
-
?
Gly-Ala-beta-naphthylamide + H2O
Gly-Ala + beta-naphthylamine
-
3.2% activity
-
-
?
Gly-Phe-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
assay at 37°C, pH 8.0
-
-
?
Gly-Phe-beta-naphthylamide + H2O
Gly-Phe + beta-naphthylamine
-
2.4% activity
-
-
?
Gly-Pro-4-methoxy-beta-naphthylamide + H2O
Gly-Pro + 4-methoxy-beta-naphthylamine
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0% activity
-
-
?
His-Phe-beta-naphthylamide + H2O
His-Phe + beta-naphthylamine
-
0% activity
-
-
?
His-Ser-2-naphthylamide + H2O
His-Ser + 2-naphthylamine
-
-
-
?
His-Ser-beta-naphthylamide + H2O
His-Ser + beta-naphthylamine
-
0% activity
-
-
?
L-Ala-L-Ala 2-naphthylamide + H2O
L-Ala-L-Ala + 2-naphthylamine
-
-
-
?
L-Ala-L-Ala-2-naphthylamide + H2O
L-Ala-L-Ala + 2-naphthylamine
-
36.64% of the activiy with L-Arg-L-Arg-4-methoxy-2-naphthylamide
-
-
?
L-Arg-L-Arg 2-naphthylamide + H2O
L-Arg-L-Arg + 2-naphthylamine
-
-
-
?
L-Asp-L-Ala-2-naphthylamide + H2O
L-Asp-L-Ala + 2-naphthylamine
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8.67% of the activiy with L-Arg-L-Arg-4-methoxy-2-naphthylamide
-
-
?
L-Asp-L-Arg-2-naphthylamide + H2O
L-Asp-L-Arg + 2-naphthylamine
-
9.8% of the activiy with L-Arg-L-Arg-4-methoxy-2-naphthylamide
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-
?
L-His-L-Ser-4-methoxy-2-naphthylamide + H2O
L-His-L-Ser + 4-methoxy-2-naphthylamine
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58.46% of the activiy with L-Arg-L-Arg-4-methoxy-2-naphthylamide
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-
?
L-Lys-L-Ala-2-naphthylamide + H2O
L-Lys-L-Ala + 2-naphthylamine
-
activity of the cupric derivative for Lys-Ala-beta-naphthylamide is about 30% of that of the wild-type enzyme
-
-
?
L-Ser-L-Tyr-2-naphthylamide + H2O
L-Ser-L-Tyr + 2-naphthylamine
-
7.35% of the activiy with L-Arg-L-Arg-4-methoxy-2-naphthylamide
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-
?
Leu-Ala-beta-naphthylamide + H2O
Leu-Ala + beta-naphthylamine
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5.0% activity
-
-
?
Lys-Ala-4-methoxy-beta-naphthylamide + H2O
Lys-Ala + 4-methoxy-beta-naphthylamine
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5.0% activity
-
-
?
Lys-Arg-2-naphtylamide + H2O
Lys-Arg + 2-naphthylamine
-
-
-
-
?
Lys-Arg-beta-naphthylamide + H2O
Lys-Arg + beta-naphthylamine
-
8% of the activity with Arg-Arg-beta-naphthylamide
-
-
?
Phe-Arg-beta-naphthylamide + H2O
Phe-Arg + beta-naphthylamine
-
17.6% activity
-
-
?
Pro-Arg-2-naphtylamide + H2O
Pro-Arg + 2-naphthylamine
143% of the activity with Arg-Arg-2-naphtylamide
-
-
?
Ser-Met-beta-naphthylamide + H2O
Ser-Met + beta-naphthylamine
-
0% activity
-
-
?
Ser-Tyr-beta-naphthylamide + H2O
Ser-Tyr + beta-naphthylamine
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0% activity
-
-
?
Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly + H2O
?
-
ACTH, action of goat brain DPP-III on the peptide is investigated, substrate is hydrolyzed
-
-
?
Trp-Met-Asp-Phe-NH2 + H2O
Trp-Met + Asp-Phe-NH2
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gastrin tetrapeptide amide, action of goat brain DPP-III on the peptide is investigated, substrate is hydrolyzed
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-
?
Ala-Ala-2-naphthylamide + H2O
Ala-Ala + 2-naphthylamine
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poor substrate
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?
Ala-Ala-2-naphthylamide + H2O
Ala-Ala + 2-naphthylamine
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poor substrate
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?
Ala-Ala-2-naphthylamide + H2O
Ala-Ala + 2-naphthylamine
-
-
-
?
Ala-Ala-2-naphtylamide + H2O
Ala-Ala + 2-naphthylamine
103% of the activity with Arg-Arg-2-naphtylamide
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-
?
Ala-Ala-2-naphtylamide + H2O
Ala-Ala + 2-naphthylamine
103% of the activity with Arg-Arg-2-naphtylamide
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?
Ala-Arg-2-naphthylamide + H2O
Ala-Arg + 2-naphthylamine
poor substrate
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-
?
Ala-Arg-2-naphthylamide + H2O
Ala-Arg + 2-naphthylamine
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-
-
?
Ala-Arg-2-naphtylamide + H2O
Ala-Arg + 2-naphthylamine
65% of the activity with Arg-Arg-2-naphtylamide
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?
Ala-Arg-2-naphtylamide + H2O
Ala-Arg + 2-naphthylamine
65% of the activity with Arg-Arg-2-naphtylamide
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?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
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-
-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
-
-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
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-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
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-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
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-
-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
preferred substrate
-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
-
substrate used in the activity assay
-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
substrate used in the activity assay
-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
assay at 37°C, pH 8.0
-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
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-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
assay at pH 8.0, 37°C
-
-
?
Arg-Arg-2-naphtylamide + H2O
Arg-Arg + 2-naphthylamine
-
-
-
?
Arg-Arg-4-methoxy-2-naphthylamide + H2O
Arg-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
Arg-Arg-4-methoxy-2-naphthylamide + H2O
Arg-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
Arg-Arg-4-methoxy-2-naphthylamide + H2O
Arg-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
Arg-Tyr-Leu-Pro-Thr + H2O
Arg-Tyr + Leu-Pro-Thr
-
i.e. proctolin
-
?
Gly-Arg-2-naphtylamide + H2O
Gly-Arg + 2-naphthylamine
167% of the activity with Arg-Arg-2-naphtylamide
-
-
?
Gly-Arg-2-naphtylamide + H2O
Gly-Arg + 2-naphthylamine
167% of the activity with Arg-Arg-2-naphtylamide
-
-
?
Gly-Arg-beta-naphthylamide + H2O
Gly-Arg + beta-naphthylamine
-
11.8% activity
-
-
?
Gly-Arg-beta-naphthylamide + H2O
Gly-Arg + beta-naphthylamine
-
6.1% of the activity with Arg-Arg-beta-naphthylamide
-
-
?
L-Arg-L-Arg-2-naphthylamide + H2O
L-Arg-L-Arg + 2-naphthylamine
binding free energy calculations reveal tighter binding of the preferred synthetic substrate Arg-Arg-2-naphtylamide to the closed than to the open enzyme conformation. The electrostatic component of the free energy of solvation is higher for the closed protein than for its less compact form
-
-
?
L-Arg-L-Arg-4-methoxy-2-naphthylamide + H2O
L-Arg-L-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
L-Arg-L-Arg-4-methoxy-2-naphthylamide + H2O
L-Arg-L-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
Leu-Gly-2-naphthylamide + H2O
Leu-Gly + 2-naphthylamine
-
no reaction
-
-
?
Lys-Ala-4-methoxy-2-naphthylamide + H2O
Lys-Ala + 4-methoxy-2-naphthylamine
-
poor substrate
-
?
Lys-Ala-4-methoxy-2-naphthylamide + H2O
Lys-Ala + 4-methoxy-2-naphthylamine
-
-
-
-
?
Lys-Ala-4-methoxy-2-naphthylamide + H2O
Lys-Ala + 4-methoxy-2-naphthylamine
-
poor substrate
-
?
Phe-Arg-2-naphthylamide + H2O
Phe-Arg + 2-naphthylamine
poor substrate
-
-
?
Phe-Arg-2-naphthylamide + H2O
Phe-Arg + 2-naphthylamine
-
-
-
?
Phe-Arg-2-naphtylamide + H2O
Phe-Arg + 2-naphthylamine
129% of the activity with Arg-Arg-2-naphtylamide
-
-
?
Phe-Arg-2-naphtylamide + H2O
Phe-Arg + 2-naphthylamine
129% of the activity with Arg-Arg-2-naphtylamide
-
-
?
Tyr-Gly-Gly-Phe + H2O
Tyr-Gly + Gly-Phe
-
enkephalin, action of goat brain DPP-III on the peptide is investigated, substrate is hydrolyzed
-
-
?
Tyr-Gly-Gly-Phe-Leu + H2O
Tyr-Gly + Gly-Phe-Leu
-
Leu-enkephalin, action of goat brain DPP-III on the peptide is investigated, substrate is hydrolyzed
-
-
?
additional information
?
-
enzyme additionally hydrolyzes isopentenyl diphosphate and dephosphorylates purine nucleotides ADP, dGDP, dGTP, and 8-oxo-dATP with strong preference for oxidized dATP
-
-
?
additional information
?
-
-
enzyme additionally hydrolyzes isopentenyl diphosphate and dephosphorylates purine nucleotides ADP, dGDP, dGTP, and 8-oxo-dATP with strong preference for oxidized dATP
-
-
?
additional information
?
-
-
polypeptides having unsubstituted N-termini, Gly4, Glu4, tripeptides and bonds involving proline are resistant
-
-
?
additional information
?
-
-
polypeptides having unsubstituted N-termini, Gly4, Glu4, tripeptides and bonds involving proline are resistant
-
-
?
additional information
?
-
-
Ala-Ala-Ala, action of goat brain DPP-III on the peptide is investigated, substrate is not hydrolyzed
no activity
-
?
additional information
?
-
-
Gly-Phe-Leu, action of goat brain DPP-III on the peptide is investigated, substrate is not hydrolyzed
no activity
-
?
additional information
?
-
-
hydrolysis depending on type of amino acid and chain length
-
-
?
additional information
?
-
-
enzyme prefers a hydrophobic residue at P1 position
-
?
additional information
?
-
-
no substrates: Arg-4-methyl-beta-naphthylamide, Ser-beta-naphthylamide, Leu-beta-naphthylamide, Pro-beta-naphthylamide, Val-beta-naphthylamide, Asp-beta-naphthylamide, Ile-beta-naphthylamide, Phe-beta-naphthylamide, Tyr-beta-naphthylamide, Trp-beta-naphthylamide, Gly-beta-naphthylamide, Arg-Phe-Ala-beta-naphthylamide, Gly-Pro-Leu-beta-naphthylamide, benzyloxycarbonyl-Phe-Arg-4-methyl-beta-naphthylamide, N-benzoyl-DL-Arg-beta-naphthylamide
-
-
?
additional information
?
-
enzyme additionally hydrolyzes isopentenyl diphosphate and dephosphorylates purine nucleotides ADP, dGDP, dGTP, and 8-oxo-dATP with strong preference for oxidized dATP
-
-
?
additional information
?
-
-
enzyme additionally hydrolyzes isopentenyl diphosphate and dephosphorylates purine nucleotides ADP, dGDP, dGTP, and 8-oxo-dATP with strong preference for oxidized dATP
-
-
?
additional information
?
-
-
hydrolysis depending on type of amino acid and chain length
-
-
?
additional information
?
-
-
hydrolysis depending on type of amino acid and chain length
-
-
?
additional information
?
-
-
enzyme prefers a hydrophobic residue at P1 position
-
?
additional information
?
-
-
no or very poor substrates: Gly-Phe-naphthylamide, Leu-Ala-2-naphthylamide, Ser-Met-2-naphthylamide, Gly-Ala-2-naphthylamide, Phe-Arg-2-naphthylamide, His-Phe-naphthylamide, Arg-4-methoxy-2-naphthylamide, Ser-2-naphthylamide, Leu-2-naphthylamide, Pro-2-naphthylamide, Val-2-naphthylamide, M-Gly-Arg-2-naphthylamide, Gly-Pro-Leu-2-naphthylamide, Val-Lys-Lys-Arg-4-methoxy-2-naphthylamide, benzoyl-DL-Arg-2-naphthylamide, Z-Arg-Arg-4-methoxy-2-naphthylamide
-
-
?
additional information
additional information
-
-
Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu, angiotensin I, action of goat brain DPP-III on the peptide is investigated, substrate is not hydrolyzed
no activity
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Cu2+
Zinc
Zn2+
additional information
Co2+
516% activity in the presence of 0.1 mM Co2+, 758% activity in the presence of 1 mM Co2+
Cu2+
-
activity of the cupric derivative for Lys-Ala-beta-naphthylamide is about 30% of that of the wild-type zinc enzyme. The enzyme activity of mutant Cu(II)-del-DPP III, in which Leu453 is deleted from the metal-binding motif, is only 1-2% of the enzyme activity of del-DPP III. The EPR spectra of Cu(II) del-DPP III do not change in the presence of excess Lys-Ala-beta-naphthylamide. The deletion of Leu453 from the HELLGH motif of rat DPP III leads to a complete loss of flexibility in the ligand geometry around the cupric ions
Zinc
the zinc ion is essential for the enzyme activity. It is positioned in the lower part of the upper domain where it is pentacoordinated by two histidines
Zn2+
QM/MM calculations reveal that the 5-coordinated metal ion is more favourable than the 6-coordinated one in only the most compact DPP III form. In this structure E451 is H-bonded to the metal ion coordinating water. Constraints for the broad substrate specificity of DPP III are the possibility of the substrate adopting the beta-strand shape and its charged N-terminus. The active conformation of the enzyme is the most compact form
additional information
-
spectral analysis of Zn2+-, Ni2+-, Cu2+-, Co2+-substituted enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,3-di-[5-(2-imidazolinyl)-2-benzimidazolyl]-2,4-di-o-chlorophenyl-cyclobutane dihydrochloride
-
-
1,3-di-[5-(2-imidazolinyl)-2-benzimidazolyl]-2,4-di-phenyl-cyclobutane dihydrochloride
-
-
1,3-di-[5-(2-imidazolinyl)-2-benzoimidazolyl]-2,4-di-(2-furyl)-cyclobutane dihydrochloride
-
-
1,3-di-[5-(2-imidazolinyl)-2-benzoimidazolyl]-2,4-di-(2-thienyl)-cyclobutane dihydrochloride
-
-
1,3-di-[5-(2-imidazolinyl)-2-benzoimidazolyl]-2,4-di-(2-thienyl)-cyclobutanedihydrochloride
-
-
1,3-di-[5-(N-amidino)-2-benzimidazolyl]-2,4-di-o-chlorophenyl-cyclobutane dihydrochloride
-
-
1,3-di-[5-(N-amidino)-2-benzimidazolyl]-2,4-di-phenyl-cyclobutane dihydrochloride
-
-
1,3-di-[5-(N-isopropylamidino)-2-benzimidazolyl]-2,4-di-o-chlorophenyl-cyclobutane dihydrochloride
-
-
1,3-di-[5-(N-isopropylamidino)-2-benzimidazolyl]-2,4-di-o-chlorophenylcyclobutane dihydrochloride
-
-
1,3-di-[5-(N-isopropylamidino)-2-benzimidazolyl]-2,4-di-phenyl-cyclobutane dihydrochloride
-
-
1-ethyl-3(3-dimethyl-amino-propyl)-carbodiimide*HCl
-
1.0 mM inhibitor, 29% inhibition, 5.0 mM inhibitor, 64% inhibition
2,2'-dithiodipyridine
-
1.0 mM inhibitor, 32% inhibition, 2.5 mM inhibitor, 98% inhibition
2,4,6-trinitrobenzene sufonic acid trihydrate
-
1.0 mM inhibitor, 52% inhibition, 2.5 mM inhibitor, 89% inhibition
2-(3H-imidazol-4-yl)-1H-benzoimidazole-5-carboxamidine hydrochloride
-
complete inhibition at 0.1 mM
2-(3H-imidazol-4-yl)-1H-benzoimidazole-5-imidazolinylamidine hydrochloride
-
complete inhibition at 0.1 mM
3,3'-dithiobis(6-nitrobenzoic acid)
-
13% residual activity at 2.5 mM, beta-mercaptoethanol and dithiothreitlol completely restores enzyme activity
4,4'-dithiodipyridine
inactivation of wild-type dipeptidyl peptidase III after incubation at pH 8.0 at 25°C, after 5 min incubation loss of 30% enzyme activity, after 15 min incubation loss of 62% enzyme activity
amino([(5-([(2R)-1-methoxy-3-(6-methylphenanthridin-8-yl)-1-oxopropan-2-yl]carbamoyl)-1H-pyrrol-2-yl)carbonyl]amino)methaniminium chloride
0.035 mM, 45% inhibition
amino[((5-[(2-([(2R)-1-methoxy-3-(6-methylphenanthridin-8-yl)-1-oxopropan-2-yl]amino)-2-oxoethyl)carbamoyl]-1H-pyrrol-2-yl)carbonyl)amino]methaniminium chloride
0.06 mM, 33% inhibition
benzamidine HCl
-
1.0 mM inhibitor, 29% inhibition, 5.0 mM inhibitor, 61% inhibition
dimethyl sulfoxide
-
inhibitory effect with more than 5% (v/v) dimethyl sulfoxide
E-64
-
i.e. L-trans-epoxysuccinyl-leucylamido(4-guanidino)butane, 10% inhibition at 0.1 mM
EGTA
96% inhibition in the presence of 1 mM EGTA, but 110% activity in the presence of the two inhibitors 1 mM EGTA and 1 mM Zn2+
iodoacetic acid
-
1.0 mM inhibitor, 25% inhibition, 5.0 mM inhibitor, 48% inhibition
L-Leu-L-Trp-L-Met-L-Arg-L-Phe-L-Ala
-
competitive inhibitor, complete inhibition at 1 mM
L-tryptophyl-L-methionyl-L-alpha-aspartyl-L-phenylalaninamide
-
competitive inhibition
Leu-enkephalin
-
i.e. L-Tyr-Gly-Gly-L-Phe-L-Leu, 92% inhibition at 1 mM, competitive inhibitor
Met-enkephalin
-
i.e. L-Tyr-Gly-Gly-L-Phe-L-Met, 61% inhibition at 0.5 mM, competitive inhibitor
methyl N-[5-(carbamimidoylcarbamoyl)-1H-pyrrole-2-carbonyl]-3-[[(pyren-1-yl)methyl]amino]-D-alaninate
0.01 mM, 36% inhibition. Compound is not hydrolysed by enzyme, although the binding affinity is comparable with that of Arg-Arg-2-naphthylamide
N-hydroxy-succinimide
-
1.0 mM inhibitor, 30% inhibition, 5.0 mM inhibitor, 51% inhibition
p-aminophenyl mercuric acetate
-
1.0 mM inhibitor, 42% inhibition, 2.5 mM inhibitor, 94% inhibition
p-hydroxymercuriphenyl-sulfonic acid
-
1.0 mM inhibitor, 22% inhibition, 2.5 mM inhibitor, 96% inhibition
p-nitrocatecholsulfate
-
1.0 mM inhibitor, 37% inhibition, 5.0 mM inhibitor, 58% inhibition
Pb(CH3COO)2
-
1.0 mM inhibitor, 53% inhibition, 2.5 mM inhibitor, 97% inhibition
Soybean trypsin inhibitor
-
1.0 mM inhibitor, 64% inhibition, 2.5 mM inhibitor, 76% inhibition
-
6-(4,5-dihydro-1H-imidazol-2-yl)-2-[(E)-2-phenylethenyl]-1H-benzimidazole
0.01 mM, 97.8% inhibition
iodoacetamide
-
1.0 mM inhibitor, 27% inhibition, 5.0 mM inhibitor, 42% inhibition
N-ethylmaleimide
-
1.0 mM inhibitor, 29% inhibition, 2.5 mM inhibitor, 88% inhibition, 5.0 mM inhibitor, 96% inhibition
o-phenanthroline
-
1.0 mM inhibitor, 46% inhibition, 2.5 mM inhibitor, 85% inhibition, 5.0 mM inhibitor, 96% inhibition
p-hydroxymercuribenzoate
-
reactivation by reduced glutathione or mercaptoethanol
Zn2+
19% inhibition in the presence of 0.1 mM Zn2+, 99.8% inhibition in the presence of 1 mM Zn2+
additional information
activities in phosphate buffers are singnificantly lower than in Tris-Hcl buffer
-
additional information
-
activities in phosphate buffers are singnificantly lower than in Tris-Hcl buffer
-
additional information
-
structural requirements for inhibition by hemorphin-like peptides
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aFas
-
anti-fas antibody, aFas treated cells release lysosomal hydrolases into the culture medium
-
dimethyl sulfoxide
-
the activity progressively increases with increase in dimethyl sulfoxide concentration up to 5% (v/v)
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
Tumor cytosol dipeptidyl peptidase III activity is increased with histological aggressiveness of ovarian primary carcinomas.
Cataract
Peptidases play an important role in cataractogenesis: an immunohistochemical study on lenses derived from Shumiya cataract rats.
Endometrial Neoplasms
Dipeptidyl peptidase III in malignant and non-malignant gynaecological tissue.
Endometrial Neoplasms
Tumor cytosol dipeptidyl peptidase III activity is increased with histological aggressiveness of ovarian primary carcinomas.
Glioblastoma
Ets-1/Elk-1 is a critical mediator of dipeptidyl-peptidase III transcription in human glioblastoma cells.
Glioblastoma
Transcription factor C/EBP-? mediates downregulation of dipeptidyl-peptidase III expression by interleukin-6 in human glioblastoma cells.
Hypertension
Novel Therapeutic Role for Dipeptidyl Peptidase III in the Treatment of Hypertension.
Hypertension
On Endogenous Angiotensin II Antagonism in Hypertension: The Role of Dipeptidyl Peptidase III.
Leishmaniasis
Dipeptidyl peptidase III as a DNA marker to investigate epidemiology and taxonomy of Old World Leishmania species.
Leukemia, Lymphocytic, Chronic, B-Cell
Enzymecytochemical heterogeneity of human chronic T-lymphocytic leukemia as demonstrated by reactivity to dipeptidylaminopeptidase IV (DAP IV; EC 3.4.14.4).
Leukemia, T-Cell
Enzymecytochemical heterogeneity of human chronic T-lymphocytic leukemia as demonstrated by reactivity to dipeptidylaminopeptidase IV (DAP IV; EC 3.4.14.4).
Neoplasms
Coumarin Derivatives Act as Novel Inhibitors of Human Dipeptidyl Peptidase III: Combined In Vitro and In Silico Study.
Neoplasms
Human dipeptidyl peptidase III mRNA variant I and II are expressed concurrently in multiple tumor derived cell lines and translated at comparable efficiency in vitro.
Neoplasms
The first structure of dipeptidyl-peptidase III provides insight into the catalytic mechanism and mode of substrate binding.
Neoplasms
Transcription factor C/EBP-? mediates downregulation of dipeptidyl-peptidase III expression by interleukin-6 in human glioblastoma cells.
Neoplasms
Tumor cytosol dipeptidyl peptidase III activity is increased with histological aggressiveness of ovarian primary carcinomas.
Obesity
DNA methylation signature in blood mirrors successful weight-loss during lifestyle interventions: the CENTRAL trial.
Obesity
The Obesity-Linked Gene Nudt3 Drosophila Homolog Aps Is Associated With Insulin Signaling.
Obesity
What model organisms and interactomics can reveal about the genetics of human obesity.
Sarcopenia
Disentangling the genetics of sarcopenia: prioritization of NUDT3 and KLF5 as genes for lean mass & HLA-DQB1-AS1 for hand grip strength with the associated enhancing SNPs & a scoring system.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.01518
Arg-Arg-2-naphthylamide
wild type, with His-tag, pH 8.0, 37°C
0.0945
L-Ala-L-Ala 2-naphthylamide
mutant R582Q, pH 8.0, 25°C, presence of CoCl2
0.1643
L-Ala-L-Ala 2-naphthylamide
mutant K638L, pH 8.0, 25°C, presence of CoCl2
0.2316
L-Ala-L-Ala 2-naphthylamide
wild-type, pH 8.0, 25°C, presence of CoCl2
0.0026
L-Arg-L-Arg 2-naphthylamide
mutant R582Q, pH 8.0, 25°C, presence of CoCl2
0.0032
L-Arg-L-Arg 2-naphthylamide
mutant R582Q, pH 8.0, 25°C, absence of CoCl2
0.004
L-Arg-L-Arg 2-naphthylamide
mutant K638L, pH 8.0, 25°C, absence of CoCl2
0.0051
L-Arg-L-Arg 2-naphthylamide
mutant K638L, pH 8.0, 25°C, presence of CoCl2
0.0143
L-Arg-L-Arg 2-naphthylamide
wild-type, pH 8.0, 25°C, absence of CoCl2
0.0152
L-Arg-L-Arg 2-naphthylamide
wild-type, pH 8.0, 25°C, presence of CoCl2
0.0251
L-Arg-L-Arg 2-naphthylamide
mutant H578N, pH 8.0, 25°C, presence of CoCl2
0.07
L-Lys-L-Ala-2-naphthylamide
-
wild-type in presence of Cu2+, pH 7.4, 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.249
Arg-Arg-2-naphthylamide
wild-type, with His-tag, pH 8.0, 37°C
0.002
L-Ala-L-Ala 2-naphthylamide
mutant K638L, pH 8.0, 25°C, presence of CoCl2
0.777
L-Ala-L-Ala 2-naphthylamide
wild-type, pH 8.0, 25°C, presence of CoCl2
7.25
L-Ala-L-Ala 2-naphthylamide
mutant R582Q, pH 8.0, 25°C, presence of CoCl2
0.003
L-Arg-L-Arg 2-naphthylamide
mutant H578N, pH 8.0, 25°C, presence of CoCl2
0.022
L-Arg-L-Arg 2-naphthylamide
mutant K638L, pH 8.0, 25°C, absence of CoCl2
0.028
L-Arg-L-Arg 2-naphthylamide
wild-type, pH 8.0, 25°C, absence of CoCl2
0.163
L-Arg-L-Arg 2-naphthylamide
mutant K638L, pH 8.0, 25°C, presence of CoCl2
0.248
L-Arg-L-Arg 2-naphthylamide
wild-type, pH 8.0, 25°C, presence of CoCl2
0.74
L-Arg-L-Arg 2-naphthylamide
mutant R582Q, pH 8.0, 25°C, absence of CoCl2
0.953
L-Arg-L-Arg 2-naphthylamide
mutant R582Q, pH 8.0, 25°C, presence of CoCl2
0.4
L-Lys-L-Ala-2-naphthylamide
-
wild-type in presence of Cu2+, pH 7.4, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
16.74
Arg-Arg-2-naphthylamide
wild type, with His-tag, pH 8.0, 37°C
0.012
L-Ala-L-Ala 2-naphthylamide
mutant K638L, pH 8.0, 25°C, presence of CoCl2
3.26
L-Ala-L-Ala 2-naphthylamide
wild-type, pH 8.0, 25°C, presence of CoCl2
76.7
L-Ala-L-Ala 2-naphthylamide
mutant R582Q, pH 8.0, 25°C, presence of CoCl2
0.133
L-Arg-L-Arg 2-naphthylamide
mutant H578N, pH 8.0, 25°C, presence of CoCl2
1.982
L-Arg-L-Arg 2-naphthylamide
wild-type, pH 8.0, 25°C, absence of CoCl2
5.42
L-Arg-L-Arg 2-naphthylamide
mutant K638L, pH 8.0, 25°C, absence of CoCl2
16.34
L-Arg-L-Arg 2-naphthylamide
wild-type, pH 8.0, 25°C, presence of CoCl2
231
L-Arg-L-Arg 2-naphthylamide
mutant R582Q, pH 8.0, 25°C, absence of CoCl2
366.7
L-Arg-L-Arg 2-naphthylamide
mutant R582Q, pH 8.0, 25°C, presence of CoCl2
3202
L-Arg-L-Arg 2-naphthylamide
mutant K638L, pH 8.0, 25°C, presence of CoCl2
5.7
L-Lys-L-Ala-2-naphthylamide
-
wild-type in presence of Cu2+, pH 7.4, 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0002
1,3-di-[5-(2-imidazolinyl)-2-benzimidazolyl]-2,4-di-phenyl-cyclobutane dihydrochloride
-
-
0.015
Gly-L-Phe-L-Leu
-
in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C
0.004
L-Arg-L-Phe-L-Ala
-
in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C
0.039
L-Leu-L-Trp
-
in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C
0.031
L-Leu-L-Trp-L-Met
-
in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C
0.007
L-Leu-L-Trp-L-Met-L-Arg-L-Phe-L-Ala
-
in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C
0.38
L-Trp-L-Met
-
in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C
0.055
L-tryptophyl-L-methionyl-L-alpha-aspartyl-L-phenylalaninamide
-
in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C
0.25
L-Val-L-Tyr
-
in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C
0.09
Leu-enkephalin
-
in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C
0.13
Met-enkephalin
-
in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C
0.00015
L-tyrosyl-L-phenylalanine hydroxamic acid
wild-type, pH 8.0, 37°C
0.00092
L-tyrosyl-L-phenylalanine hydroxamic acid
mutant W300F, pH 8.0, 37°C
0.00427
L-tyrosyl-L-phenylalanine hydroxamic acid
mutant W300L, pH 8.0, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
1,3-di-[5-(2-imidazolinyl)-2-benzimidazolyl]-2,4-di-o-chlorophenyl-cyclobutane dihydrochloride
0.0028
1,3-di-[5-(2-imidazolinyl)-2-benzimidazolyl]-2,4-di-phenyl-cyclobutane dihydrochloride
0.008
1,3-di-[5-(2-imidazolinyl)-2-benzoimidazolyl]-2,4-di-(2-furyl)-cyclobutane dihydrochloride
0.001
1,3-di-[5-(2-imidazolinyl)-2-benzoimidazolyl]-2,4-di-(2-thienyl)-cyclobutane dihydrochloride
Homo sapiens
-
-
0.01
1,3-di-[5-(2-imidazolinyl)-2-benzoimidazolyl]-2,4-di-(2-thienyl)-cyclobutanedihydrochloride
Homo sapiens
-
at pH 7.4 for 10 min at 25°C
0.007
1,3-di-[5-(N-amidino)-2-benzimidazolyl]-2,4-di-o-chlorophenyl-cyclobutane dihydrochloride
0.006
1,3-di-[5-(N-isopropylamidino)-2-benzimidazolyl]-2,4-di-o-chlorophenyl-cyclobutane dihydrochloride
Homo sapiens
-
-
0.006
1,3-di-[5-(N-isopropylamidino)-2-benzimidazolyl]-2,4-di-o-chlorophenylcyclobutane dihydrochloride
Homo sapiens
-
at pH 7.4 for 10 min at 25°C
0.01
1,3-di-[5-(N-isopropylamidino)-2-benzimidazolyl]-2,4-di-phenyl-cyclobutane dihydrochloride
0.01
6-(4,5-dihydro-1H-imidazol-2-yl)-2-[(E)-2-phenylethenyl]-1H-benzimidazole
Homo sapiens
-
-
0.0017
1,3-di-[5-(2-imidazolinyl)-2-benzimidazolyl]-2,4-di-o-chlorophenyl-cyclobutane dihydrochloride
Homo sapiens
-
-
0.0017
1,3-di-[5-(2-imidazolinyl)-2-benzimidazolyl]-2,4-di-o-chlorophenyl-cyclobutane dihydrochloride
Homo sapiens
-
at pH 7.4 for 10 min at 25°C
0.0028
1,3-di-[5-(2-imidazolinyl)-2-benzimidazolyl]-2,4-di-phenyl-cyclobutane dihydrochloride
Homo sapiens
-
-
0.0028
1,3-di-[5-(2-imidazolinyl)-2-benzimidazolyl]-2,4-di-phenyl-cyclobutane dihydrochloride
Homo sapiens
-
at pH 7.4 for 10 min at 25°C
0.008
1,3-di-[5-(2-imidazolinyl)-2-benzoimidazolyl]-2,4-di-(2-furyl)-cyclobutane dihydrochloride
Homo sapiens
-
-
0.008
1,3-di-[5-(2-imidazolinyl)-2-benzoimidazolyl]-2,4-di-(2-furyl)-cyclobutane dihydrochloride
Homo sapiens
-
at pH 7.4 for 10 min at 25°C
0.007
1,3-di-[5-(N-amidino)-2-benzimidazolyl]-2,4-di-o-chlorophenyl-cyclobutane dihydrochloride
Homo sapiens
-
-
0.007
1,3-di-[5-(N-amidino)-2-benzimidazolyl]-2,4-di-o-chlorophenyl-cyclobutane dihydrochloride
Homo sapiens
-
at pH 7.4 for 10 min at 25°C
0.0056
1,3-di-[5-(N-amidino)-2-benzimidazolyl]-2,4-di-phenyl-cyclobutane dihydrochloride
Homo sapiens
-
-
0.0056
1,3-di-[5-(N-amidino)-2-benzimidazolyl]-2,4-di-phenyl-cyclobutane dihydrochloride
Homo sapiens
-
at pH 7.4 for 10 min at 25°C
0.01
1,3-di-[5-(N-isopropylamidino)-2-benzimidazolyl]-2,4-di-phenyl-cyclobutane dihydrochloride
Homo sapiens
-
-
0.01
1,3-di-[5-(N-isopropylamidino)-2-benzimidazolyl]-2,4-di-phenyl-cyclobutane dihydrochloride
Homo sapiens
-
at pH 7.4 for 10 min at 25°C, IC50 above 0.01 mM
0.053
2-(3H-imidazol-4-yl)-1H-benzoimidazole-5-carboxamidine hydrochloride
Homo sapiens
-
at pH 7.4 for 10 min at 25°C
0.018
2-(3H-imidazol-4-yl)-1H-benzoimidazole-5-imidazolinylamidine hydrochloride
Homo sapiens
-
-
0.018
2-(3H-imidazol-4-yl)-1H-benzoimidazole-5-imidazolinylamidine hydrochloride
Homo sapiens
-
at pH 7.4 for 10 min at 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0092
-
purification step, gel filtration chromatography on a Sephadex G-100 column
0.0126
-
purification step, cation exchange chromatography on a CM Sephadex A-50 column
0.0652
-
purification step, anion exchange chromatography on a DEAE Sephadex A-50 column
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
8.5
8.6
8.8
7.4
-
physiological condition, determination of Ki values and kinetic parameters of the hydrolysis of endomorphin-1
8.6
-
assay condition with the synthetic substrate Arg-Arg-2-naphthylamide, determination of specific activity
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
-
the enzyme has 50% activity at pH 6 in the lower range and at pH 11 in the higher range
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
40
-
the enzyme shows a considerable heat stability up to 40°C, 30% activity is lost at 45°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
sequence contains a pentapeptide HEXXH, and at the N-terminus, a Nudix box
UniProt
brenda
sequence contains a pentapeptide HEXXH, and at the N-terminus, a Nudix box
UniProt
brenda
-
-
-
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
concurrent expression of mRNA variants DPP III V-I and V-II
brenda
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
DPP III overexpression and angiotensin II stimulation in angiotensin II type 1 receptor expressing HEK293T cells leads to a significant decrease in intracellular Ca2+
physiological function
the enzyme possesses a C-terminal extension containing an Armadillo type fold similar to the AlkD family of bacterial DNA glycosylases. The Km values for both Arg-Arg substrates are increased by 4fold when the C-terminal domain is removed. kcat values are reduced 120fold in the case of Arg-Arg-4-methylcoumarin 7-amide, and 250fold in the case of Arg-Arg-2-naphthylamide, resulting in a 470fold and 1050fold reduction in the catalytic efficiency, respectively. Complementation assays in a DNA repair-deficient Escherichia coli strain indicate the absence of alkylation repair function
Show AA Sequence and Transmembrane Helices (2426 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
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000 - 86000
82000
88000
89000
82000
predicted, and verified by SDS-PAGE and Western Blot analysis, purified human erythtocyte DPP III and recombinant DPP III
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
dimer
-
the protein exists in a mono- and dimeric form, X-ray crystallography
dimer
-
the protein exists in a mono- and dimeric form, X-ray crystallography
-
monomer
-
the protein exists in a mono- and dimeric form, X-ray crystallography
monomer
-
the protein exists in a mono- and dimeric form, X-ray crystallography
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
-
six potential glycosylation sites, but no glycosylation detectable
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modelling study of wild-type and its C450S mutant, as well as their complexes with substrates Arg-Arg-2-naphthylamide and Lys-Ala-2-naphtylamide
-
the ligand-free structure (refined to 2.4 A) is in the open conformation, while in the presence of the inhibitor Tyr-Phe-NHOH, the closed form (refined to 3.3 A) is observed. Compared to the closed form, the two domains of the open form are rotated away from each other by about 28 degrees
molecular dynamics simulations of the complex with luteolin. The 3' and 4' hydroxyl group on B-ring as well as 5 and 7 hydroxyl group on A-ring helps luteolin to interact with the Asn391, Asn406, Tyr417, His450, Glu451, Val447, Glu512, Asn545, Gln566, and Arg572 residues
molecular modeling of docking. Aprotinin interacts by its canonical binding epitope with the substrate binding cleft of DPP III. Thereby, free N-terminus of aprotinin is distant from the active-site zinc. The enzyme-inhibitor complex is stabilized by intermolecular hydrogen bonding network, electrostatic and hydrophobic interactions which mostly involve constituent amino acid residues of the DPP III substrate binding subsites S1, S1', S2, S2' and S3'
QSAR and molecular dynamics simulation of inhibitor binding. Compounds that contain two imidazolinyl groups, with only one sp3-hybridized nitrogen atom each, are potent inhibitors. Most of the interactions of imidazolinyl groups are achieved by electrostatic forces with the residuals Ser108, Gly110, Tyr318, and Ala416 of the lower domain, and with the residuals Tyr417, Asn545, and Glu667 of the upper domain. The phenyl groups of compound 6-(4,5-dihydro-1H-imidazol-2-yl)-2-[(E)-2-phenylethenyl]-1H-benzimidazole interact mainly by means of van der Waals and electrostatic forces with the residuals Ile386, Pro387, Ala388, Phe556, Gln566, and Met569, as well as the cyclobutane ring with His568
structures of human DPP III and its complex with the opioid peptide tynorphin, to 1.8 A and 2.4 and.0 A resolution, respectively. Structures rationalize the enzymes substrate specificity and reveal an exceptionally large domain motion upon ligand binding. Microcalorimetric analyses point at an entropy-dominated process, with the release of water molecules from the binding cleft as the major thermodynamic driving force
the C130S mutant is crystallized by sitting drop vapour diffusion method, in 20% (w/v) polyethylene glycol 3350 and 900 mM MgCl2 in 100 mM Tris-HCl (pH 7.0)
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C450S
-
residues Gly383 and Glu320 form significantly less hydrogen bonds with substrate Arg-Arg-2-naphthylamide than in the wild type enzyme
D372A
residue Asp372 plays a crucial role in the large scale interdomain closure. During the MD simulation time, the variant remains more open than the wild type protein. Apparently, Ala is not as efficient as Asp in establishing the interdomain interactions
D496G
-
mutation in S2 subsite, mutant has lost selectivity due to the increase of the Km value. Mutant shows significantly decreased binding of peptides with N-terminal arginine, and of tynorphin
G313A
mutation detected in human cancer, strong decrease in activity. Mutation significantly increases the enzyme flexibility, particularly that of the binding site including the H450ELLGH455 motif, and influences the substrate interactions with the catalytic His568
R510K
mutation detected in human cancer, substitution mildly decreases enzyme activity for Arg-Arg-2-naphtylamide substrate
R510W
mutation detected in human cancer, almost abolishes activity. Mutation significantly increases the enzyme flexibility, particularly that of the binding site including the H450ELLGH455 motif, and influences the substrate interactions with the catalytic His568
S504G
-
mutation in S2 subsite, mutant does not show decreased binding of peptides with N-terminal arginine
W300F
mutant with slight increase in activity compared to wild-type enzyme
Y318F
the potential functional role of the well-conserved tyrosine 318 residue in the active center of human DPP III is investigated
Y395F
the potential functional role of the well-conserved tyrosine 395 residue in the active center of human DPP III is investigated
Y644F
the potential functional role of the well-conserved tyrosine 644 residue in the active center of human DPP III is investigated
C176A
-
25-35% of wild type activity, resistant against p-chloro-mercuri-benzoate and N-ethylmaleimide
Leu453del
-
activity of mutant Cu(II)-del-DPP III, in which Leu453 is deleted from the metal-binding motif, is only 1-2% of the enzyme activity of del-DPP. The EPR spectra of Cu(II) del-DPP III do not change in the presence of excess Lys-Ala-beta-naphthylamide. The deletion of Leu453 from the HELLGH motif of rat DPP III leads to a complete loss of flexibility in the ligand geometry around the cupric ions
C130S
H578D
mutation 122fold lowers the catalytic efficiency for Arg-Arg 2-naphthylamide hydrolysis, and 14fold decreases affinity for hydroxamate inhibitor Tyr-Phe-NHOH
K638L
mutation slightly increases the specificity constant for Arg-Arg 2-naphthylamide hydrolysis. The affinity for Tyr-Phe-NHOH, and activity for the substrates with uncharged P2 side chains such as Ala-Ala-, Ala-Arg- and Phe-Arg 2-naphthylamide are dramatically reduced
R582Q
mutant exhibits an order of magnitude higher activity with all four dipeptide derivatives examined, compared to the wild type, due to a change in the H-bond networking in the R582Q variant active-site region
C130S
-
the mutant exhibits comparable enzymatic activity to the wild type protein
-
additional information
C130S
-
the mutant exhibits comparable enzymatic activity to the wild type protein
additional information
design of recombinant enzymes withh binding of Ets-1/Elk-1 proteins to binding motifs, increased enzyme expression
additional information
-
design of recombinant enzymes withh binding of Ets-1/Elk-1 proteins to binding motifs, increased enzyme expression
additional information
DPPIII6His, construct with hexahistidine
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 9.5
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
55
50
50% enzyme inactivation at 50°C for wild-type enzyme and mutant W300F and mutant W300L
55
wild-type enzyme and mutant W300F and mutant W300L completely inactivated
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
4,4'-dithiodipyridine, inactivation of wild-type dipeptidyl peptidase III after incubation at pH 8.0 at 25°C, after 5 min incubation loss of 30% enzyme activity, after 15 min incubation loss of 62% enzyme activity
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C, 50 mM sodium phosphate buffer, pH 6.8, 1 mM mercaptoethanol, 0.5 M NaCl, 40% glycerol, 1 year
-
-20°C, in 50 mM Tris-HCl, pH 7.5, 1 and 6 months, 38.15% and 99.75% loss of activity
-
-20°C, in 50 mM Tris-HCl, pH 7.5, in the presence of 10% (v/v) glycerol, 1 and 6 months, 26.5% and 92% loss of activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by gel filtration on a Sephacryl S-200 column, followed by FPLC on a Mono Q column, recombinant and human erythtocyte DPP III is purified
DPP from goat brain is purified by several steps, including acid precipitation, ammonium sulfate fractionation, chromatography on a Sephadex G-100 column, cation, anion and adsorption chromatography
-
partial
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli BL21
expression in human glioblastoma, ovarian carcinoma, pancreatic carcinoma and mouse fibroblast cells
into the pET21b vector for expression in Escherichia coli BL21DE3RIL+ cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased enzyme expression with recombinant constructs with Ets-1/Elk-1 proteins bind to binding motifs
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
incubation of apo-enzyme with Zn2+, Co2+, Ni2+ or Cu2+ completely recovers enzymic activity
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
knowing whether lysosomal enzymes are involved in vivo in the Fas apoptotic pathway may be of some help to explore specific therapeutic targets for cell death inhibition in several severe liver pathologies
medicine
-
multiple tumor derived cell lines show concurrent expression and a comparable in vitro translational efficiency for mRNA variants DPP III V-I and II
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McDonald, J.K.; Schwabe, C.
Dipeptidyl aminopeptidase III (EC 3.4.14.-)
Proteinases in Mammalian Cells and Tissues (Barrett, A. J. , ed. )
361-364
1977
Bos taurus, Rattus norvegicus
-
brenda
Alba, F.; Arenas, J.C.; Lopez, M.A.
Properties of rat brain dipeptidyl aminopeptidases in the presence of detergents
Peptides
16
325-329
1995
Rattus norvegicus
brenda
Shimamori, Y.; Watanabe, Y.; Fujimoto, Y.
Human placental dipeptidyl aminopeptidase III: Hydrolysis of enkephalins and its stimulation by cobaltus ions
Biochem. Med. Metab. Biol.
40
305-310
1988
Homo sapiens
brenda
Vanha-Perttula, T.
Dipeptidyl peptidase III and alanyl aminopeptidase in the human seminal plasma: Origin and biochemical properties
Clin. Chim. Acta
177
179-196
1988
Homo sapiens
brenda
Abramic, M.; Zubanovic, M.; Vitale, L.
Dipeptidyl peptidase III from human erythrocytes
Biol. Chem. Hoppe-Seyler
369
29-38
1988
Homo sapiens
brenda
Inaoka, Y.; Tamaoki, H.
Purification and characterization of enkephalinase B from rat brain membrane
Biochim. Biophys. Acta
925
27-35
1987
Rattus norvegicus
brenda
Chan., S.A.T.; Jones, T.H.D.; Sweeney, J.P.; Toursarkissian, K.
Partial purification and characterization of dipeptidyl-aminopeptidase III from Dictostelium discoideum
Exp. Mycol.
11
27-35
1987
Dictyostelium discoideum
-
brenda
Shimamori, Y.; Watanabe, Y.; Fujimoto, Y.
Purification and characterization of dipeptidyl aminopeptidase III from human placenta
Chem. Pharm. Bull.
34
3333-3340
1986
Homo sapiens
brenda
Nishikiori, T.; Kawahara, F.; Naganawa, H.; Muraoka, Y.; Aoyagi, T.; Umezawa, H.
Production of acetyl-L-leucyl-L-argininal, inhibitor of dipeptidyl aminopeptidase III by bacteria
J. Antibiot.
37
680-681
1984
Rattus norvegicus
brenda
Lee, C.M.; Snyder, S.H.
Dipeptidyl-aminopeptidase III of rat brain. Selective affinity for enkephalin and angiotensin
J. Biol. Chem.
257
12043-12050
1982
Rattus norvegicus
brenda
Jones, T.H.D.; Kapralou, A.
A rapid assay for dipeptidyl aminopeptidase III in human erythrocytes
Anal. Biochem.
119
418-423
1982
Homo sapiens
brenda
Swanson, A.A; Albers-Jackson, B.; McDonald, J.K.
Mammalian lens dipeptidyl aminopeptidase III
Biochem. Biophys. Res. Commun.
84
1151-1159
1978
Bos taurus
brenda
Fukasawa, K.; Fukasawa, K.M.; Kanai, M.; Fujii, S.; Hirose, J.; Harada, M.
Dipeptidyl peptidase III is a zinc metallo-exopeptidase
Biochem. J.
329
275-282
1998
Homo sapiens
brenda
Fukasawa, K.; Fukasawa, K.M.; Iwamoto, G.; Hirose, J.; Harada, M.
The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme
Biochemistry
38
8299-8303
1999
Rattus norvegicus
brenda
Huang, J.; Kim, J.; Ramamurthy, P.; Jones, T.H.D.
The purification, specificity, and role of dipeptidyl peptidase III in Dictostelium discoideum
Exp. Mycol.
16
102-109
1992
Dictyostelium discoideum
-
brenda
Simaga, S.; Babic, D.; Osmak, M.; Ilic-Forko, J.; Vitale, L.; Milicic, D.; Abramic, M.
Dipeptidyl peptidase III in malignant and non-malignant gynaecological tissue
Eur. J. Cancer
34
399-405
1998
Homo sapiens
brenda
Mazzocco, C.; Fukasawa, K.M.; Auguste, P.; Puiroux J.
Characterization of a functionally expressed dipeptidyl aminopeptidase III from Drosophila melanogaster
Eur. J. Biochem.
270
3074-3082
2003
Drosophila melanogaster
brenda
Smyth, M.; O'Cuinn, G.
Dipeptidyl aminopeptidase activities of guinea-pig brain
Int. J. Biochem.
26
913-921
1994
Cavia porcellus
brenda
Lynn, K.R.
The isolation and some properties of dipeptidyl peptidases II and III from porcine spleen
Int. J. Biochem.
23
47-50
1991
Sus scrofa
brenda
Hola-Jamriska, L.; Dalton, J.P.; Aaskow, J.; Brindley, P.J.
Dipeptidyl peptidase I and III activities of adult schistosomes
Parasitology
118
275-282
1999
Schistosoma sp.
brenda
Sentrandreu, M.A.; Toldra, F.
Biochemical properties of dipeptidyl peptidase III purified from porcine skeletal muscle.
J. Agric. Food Chem.
46
3977-3984
1998
Sus scrofa
brenda
Smyth, M.; O'Cuinn, G.
Dipeptidyl aminopeptidase III of guinea-pig brain: Specificity for short oligopeptide sequences
J. Neurochem.
63
1439-1445
1994
Cavia porcellus
brenda
Watanabe, Y.; Kumagai, Y.; Fujimoto, Y.
Presence of a dipeptidyl aminopeptidase III in Saccharomyces cerevisiae
Chem. Pharm. Bull.
38
246-248
1990
Saccharomyces cerevisiae
brenda
Li, Y.H.; Maeda, T.; Yamane, T.; Ohkubo, I.
Alteration of rat dipeptidyl peptidase III by site-directed mutagenesis: Cysteine176 is a regulatory residue for the enzyme activity
Biochem. Biophys. Res. Commun.
276
553-558
2000
Rattus norvegicus
brenda
Hirose, J.; Iwamoto, H.; Nagao, I.; Enmyo, K.; Sugao, H.; Kanemitu, N.; Ikeda, K.; Takeda, M.; Inoue, M.; Ikeda, T.; Matsuura, F.; Fukasawa, K.M.; Fukasawa, K.
Characterization of the metal-substituted dipeptidyl peptidase III (rat liver)
Biochemistry
40
11860-11865
2001
Rattus norvegicus
brenda
Abramic, M.; Schleuder, D.; Dolovcak, L.; Schroder, W.; Strupat, K.; Sagi, D.; Peter-Katalini, J.; Vitale, L.
Human and rat dipeptidyl peptidase III: biochemical and mass spectrometric arguments for similarities and differences
Biol. Chem.
381
1233-1243
2000
Homo sapiens, Rattus norvegicus
brenda
Yamamoto, Y.; Hashimoto, J.i.; Shimamura, M.; Yamaguchi, T.; Hazato, T.
Characterization of tynorphin, a potent endogenous inhibitor of dipeptidyl peptidaseIII
Peptides
21
503-508
2000
Platyrrhini
brenda
Chiba, T.; Li, Y.H.; Yamane, T.; Ogikubo, O.; Fukuoka, M.; Arai, R.; Takahashi, S.; Ohtsuka, T.; Ohkubo, I.; Matsui, N.
Inhibition of recombinant dipeptidyl peptidase III by synthetic hemorphin-like peptides
Peptides
24
773-778
2003
Platyrrhini
brenda
Mazzocco, C.; Gillibert-Duplantier, J.; Neaud, V.; Fukasawa, K.M.; Claverol, S.; Bonneu, M.; Puiroux, J.
Identification and characterization of two dipeptidyl-peptidase III isoforms in Drosophila melanogaster
FEBS J.
273
1056-1064
2006
Drosophila melanogaster (Q9VHR8), Drosophila melanogaster
brenda
Agic, D.; Hranjec, M.; Jajcanin, N.; Starcevic, K.; Karminski-Zamola, G.; Abramic, M.
Novel amidino-substituted benzimidazoles: synthesis of compounds and inhibition of dipeptidyl peptidase III
Bioorg. Chem.
35
153-169
2007
Homo sapiens
brenda
Wattiaux, R.; Wattiaux-de Coninck, S.; Thirion, J.; Gasingirwa, M.C.; Jadot, M.
Lysosomes and Fas-mediated liver cell death
Biochem. J.
403
89-95
2007
Homo sapiens
brenda
Barsun, M.; Jajcanin, N.; Vukeli?, B.; Spoljari?, J.; Abrami?, M.
Human dipeptidyl peptidase III acts as a post-proline-cleaving enzyme on endomorphins
Biol. Chem.
388
343-348
2007
Homo sapiens
brenda
Salopek-Sondi, B.; Vukelic, B.; Spoljaric, J.; Simaga, S.; Vujaklija, D.; Makarevic, J.; Jajcanin, N.; Abramic, M.
Functional tyrosine residue in the active center of human dipeptidyl peptidase III
Biol. Chem.
389
163-167
2008
Homo sapiens (Q9NY33), Homo sapiens
brenda
Dhanda, S.; Singh, J.; Singh, H.
Hydrolysis of various bioactive peptides by goat brain dipeptidylpeptidase-III homologue
Cell Biochem. Funct.
26
339-345
2007
Capra hircus
brenda
Simaga, S.; Abramic, M.; Osmak, M.; Babic, D.; Ilic-Forko, J.
Total tissue lactate dehydrogenase activity in endometrial carcinoma
Int. J. Gynecol. Cancer
18
1272-1278
2008
Homo sapiens
brenda
Dhanda, S.; Singh, H.; Singh, J.; Singh, T.P.
Isolation, purification and characterization of a DPP-III homologue from goat brain
Protein Expr. Purif.
52
297-305
2007
Capra hircus
brenda
Tye, C.E.; Lorenz, R.L.; Bartlett, J.D.
Lysosomal protease expression in mature enamel
Cells Tissues Organs
189
111-114
2009
Mus musculus
brenda
Baral, P.K.; Jajcanin-Jozic, N.; Deller, S.; Macheroux, P.; Abramic, M.; Gruber, K.
The first structure of dipeptidyl-peptidase III provides insight into the catalytic mechanism and mode of substrate binding
J. Biol. Chem.
283
22316-22324
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Dhanda, S.; Singh, H.; Singh, J.; Singh, T.P.
Functional characterization and specific effects of various peptides on enzymatic activity of a DPP-III homologue from goat brain
J. Enzyme Inhib. Med. Chem.
23
174-181
2008
Capra hircus
brenda
Cicin-Sain, L.; Simaga, S.; Froebe, A.; Abramic, M.
Central aminopeptidase and serotonin system activities: possible relationship
Neuropeptides
42
435-440
2008
Rattus norvegicus
brenda
Jajcanin-Jozic, N.; Deller, S.; Pavkov, T.; Macheroux, P.; Abramic, M.
Identification of the reactive cysteine residues in yeast dipeptidyl peptidase III
Biochimie
92
89-96
2010
Saccharomyces cerevisiae (Q08225), Saccharomyces cerevisiae
brenda
Spoljaric, J.; Salopek-Sondi, B.; Makarevic, J.; Vukelic, B.; Agic, D.; Simaga, S.; Jajcanin-Jozic, N.; Abramic, M.
Absolutely conserved tryptophan in M49 family of peptidases contributes to catalysis and binding of competitive inhibitors
Bioorg. Chem.
37
70-76
2009
Homo sapiens (Q9NY33), Homo sapiens
brenda
Casewell, N.R.; Harrison, R.A.; Wuester, W.; Wagstaff, S.C.
Comparative venom gland transcriptome surveys of the saw-scaled vipers (Viperidae: Echis) reveal substantial intra-family gene diversity and novel venom transcripts
BMC Genomics
10
564
2009
Echis pyramidum leakeyi, Echis carinatus sochureki, Echis coloratus
brenda
Shukla, A.A.; Jain, M.; Chauhan, S.S.
Ets-1/Elk-1 is a critical mediator of dipeptidyl-peptidase III transcription in human glioblastoma cells
FEBS J.
277
1861-1875
2010
Homo sapiens (Q9NY33), Homo sapiens
brenda
Isaac, R.; Bland, N.; Shirras, A.
Neuropeptidases and the metabolic inactivation of insect neuropeptides
Gen. Comp. Endocrinol.
162
8-17
2009
Blaberus craniifer, Drosophila melanogaster (Q9VHR8)
brenda
Flores, M.; Aristoy, M.C.; Antequera, T.; Barat, J.M.; Toldra, F.
Effect of prefreezing hams on endogenous enzyme activity during the processing of Iberian dry-cured hams
Meat Sci.
82
241-246
2009
Sus scrofa domesticus
brenda
Hirose, J.; Hata, T.; Kawaoka, C.; Ikeura, T.; Kitahara, S.; Horii, K.; Tomida, H.; Iwamoto, H.; Ono, Y.; Fukasawa, K.M.
Flexibility of the coordination geometry around the cupric ions in Cu(II)-rat dipeptidyl peptidase III is important for the expression of enzyme activity
Arch. Biochem. Biophys.
525
71-81
2012
Rattus norvegicus
brenda
Abramic, M.; Karacic, Z.; Semanjski, M.; Vukelic, B.; Jajcanin-Jozic, N.
Aspartate 496 from the subsite S2 drives specificity of human dipeptidyl peptidase III
Biol. Chem.
396
359-366
2015
Homo sapiens
brenda
Tomic, A.; Tomic, S.
Hunting the human DPP III active conformation: combined thermodynamic and QM/MM calculations
Dalton Trans.
43
15503-15514
2014
Homo sapiens (Q9NY33), Homo sapiens
brenda
Jajcanin-Jozic, N.; Tomic, S.; Abramic, M.
Importance of the three basic residues in the vicinity of the zinc-binding motifs for the activity of the yeast dipeptidyl peptidase III
J. Biochem.
155
43-50
2014
Saccharomyces cerevisiae (Q08225), Saccharomyces cerevisiae
brenda
Tomic, A.; Gonzalez, M.; Tomic, S.
The large scale conformational change of the human DPP III-substrate prefers the "closed" form
J. Chem. Inf. Model.
52
1583-1594
2012
Homo sapiens (Q9NY33), Homo sapiens
brenda
Bezerra, G.A.; Dobrovetsky, E.; Viertlmayr, R.; Dong, A.; Binter, A.; Abramic, M.; Macheroux, P.; Dhe-Paganon, S.; Gruber, K.
Entropy-driven binding of opioid peptides induces a large domain motion in human dipeptidyl peptidase III
Proc. Natl. Acad. Sci. USA
109
6525-6530
2012
Homo sapiens (Q9NY33), Homo sapiens
brenda
Jodha, D.; Attri, P.; Khaket, T.; Singh, J.
Isolation, purification and biochemical characterization of dipeptidyl peptidase-III from germinated Vigna radiata seeds
Process Biochem.
48
730-737
2013
Vigna radiata
-
brenda
Rastija, V.; Agic, D.; Tomic, S.; Nikolic, S.; Hranjec, M.; Grace, K.Z.; Abramic, M.
Synthesis, QSAR, and molecular dynamics simulation of amidino-substituted benzimidazoles as dipeptidyl peptidase III inhibitors
Acta Chim. Slov.
62
867-878
2015
Homo sapiens (Q9NY33), Homo sapiens
brenda
Karacic, Z.; Vukelic, B.; Ho, G.; Jozic, I.; Sucec, I.; Salopek-Sondi, B.; Kozlovic, M.; Brenner, S.; Ludwig-Mueller, J.; Abramic, M.
A novel plant enzyme with dual activity An atypical Nudix hydrolase and a dipeptidyl peptidase III
Biol. Chem.
398
101-112
2017
Physcomitrium patens (A9TLP4), Physcomitrium patens, Arabidopsis thaliana (Q8L831), Arabidopsis thaliana
brenda
Agic, D.; Brkic, H.; Tomic, S.; Karacic, Z.; Spoljarevic, M.; Lisjak, M.; Beslo, D.; Abramic, M.
Validation of flavonoids as potential dipeptidyl peptidase III inhibitors Experimental and computational approach
Chem. Biol. Drug Des.
89
619-627
2017
Homo sapiens (Q9NY33), Homo sapiens
brenda
Agic, D.; Brkic, H.; Kazazic, S.; Tomic, A.; Abramic, M.
Aprotinin interacts with substrate-binding site of human dipeptidyl peptidase III
J. Biomol. Struct. Dyn.
37
3596-3606
2018
Homo sapiens (Q9NY33), Homo sapiens
brenda
Cvitesic, A.; Sabljic, I.; Makarevic, J.; Abramic, M.
Novel dipeptidyl hydroxamic acids that inhibit human and bacterial dipeptidyl peptidase III
J. Enzyme Inhib. Med. Chem.
31
40-45
2016
Bacteroides thetaiotaomicron (Q8A6N1), Bacteroides thetaiotaomicron, Homo sapiens (Q9NY33), Homo sapiens, Bacteroides thetaiotaomicron DSM 2079 (Q8A6N1)
brenda
Prajapati, S.C.; Chauhan, S.S.
Human dipeptidyl peptidase III mRNA variant I and II are expressed concurrently in multiple tumor derived cell lines and translated at comparable efficiency in vitro
Mol. Biol. Rep.
43
457-462
2016
Homo sapiens
brenda
Attri, P.; Jodha, D.; Singh, J.; Dhanda, S.
Purification, kinetic and functional characterization of membrane bound dipeptidyl peptidase-III from NCDC 252 a probiotic lactic acid bacteria
Mol. Biol. Rep.
45
973-986
2018
Pediococcus acidilactici
brenda
Tomin, M.; Tomic, S.
Dynamic properties of dipeptidyl peptidase III from Bacteroides thetaiotaomicron and the structural basis for its substrate specificity - a computational study
Mol. Biosyst.
13
2407-2417
2017
Bacteroides thetaiotaomicron
brenda
Sabljic, I.; Mestrovic, N.; Vukelic, B.; Macheroux, P.; Gruber, K.; Luic, M.; Abramic, M.
Crystal structure of dipeptidyl peptidase III from the human gut symbiont Bacteroides thetaiotaomicron
PLoS ONE
12
e0187295
2017
Bacteroides thetaiotaomicron (Q8A6N1), Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron DSM 2079 (Q8A6N1)
brenda
Hromic-Jahjefendic, A.; Jajcanin Jozic, N.; Kazazic, S.; Grabar Branilovic, M.; Karacic, Z.; Schrittwieser, J.H.; Das, K.M.P.; Tomin, M.; Oberer, M.; Gruber, K.; Abramic, M.; Tomic, S.
A novel Porphyromonas gingivalis enzyme An atypical dipeptidyl peptidase III with an ARM repeat domain
PLoS ONE
12
e0188915
2017
Porphyromonas gingivalis (Q7MX92), Porphyromonas gingivalis
brenda
Sabljic, I.; Tomin, M.; Matovina, M.; Sucec, I.; Tomacic Paic, A.; Tomic, A.; Abramic, M.; Tomic, S.
The first dipeptidyl peptidase III from a thermophile Structural basis for thermal stability and reduced activity
PLoS ONE
13
e0192488
2018
Caldithrix abyssi (H1XW48), Caldithrix abyssi, Caldithrix abyssi DSM 13497 (H1XW48)
brenda
Matic, J.; Supljika, F.; Tir, N.; Piotrowski, P.; Schmuck, C.; Abramic, M.; Piantanida, I.; Tomic, S.
Guanidiniocarbonyl-pyrrole-aryl conjugates as inhibitors of human dipeptidyl peptidase III Combined experimental and computational study
RSC Adv.
6
83044-83052
2016
Homo sapiens (Q9NY33)
-
brenda
Matovina, M.; Agic, D.; Abramic, M.; Matic, S.; Karacic, Z.; Tomic, S.
New findings about human dipeptidyl peptidase III based on mutations found in cancer
RSC Adv.
7
36326-36334
2017
Homo sapiens (Q9NY33)
-
brenda
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