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Information on EC 3.4.14.4 - dipeptidyl-peptidase III and Organism(s) Homo sapiens and UniProt Accession Q9NY33
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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 taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dipeptidyl aminopeptidase III
dipeptidyl arylamidase III
dipeptidyl-peptide hydrolase
-
-
-
-
dipeptidylpeptidase III
-
-
-
-
enkephalinase B
peptidase, dipeptidyl, III
-
-
-
-
red cell angiotensinase
-
-
-
-
dipeptidyl aminopeptidase III
-
-
-
-
dipeptidyl arylamidase III
-
-
-
-
enkephalinase B
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY
77464-87-0
-
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-Arg-2-naphthylamide + H2O
Ala-Arg + 2-naphthylamine
poor substrate
-
-
?
Ala-Phe-2-naphthylamide + H2O
Ala-Phe + 2-naphtylamine
assay at 37°C, pH 8.0
-
-
?
Gly-Phe-2-naphthylamide + H2O
Gly-Phe + 2-naphthylamine
assay at 37°C, pH 8.0
-
-
?
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
-
-
?
Phe-Arg-2-naphthylamide + H2O
Phe-Arg + 2-naphthylamine
poor substrate
-
-
?
Arg-Arg-4-methoxy-2-naphthylamide + H2O
Arg-Arg + 4-methoxy-2-naphthylamine
-
-
-
-
?
Lys-Ala-4-methoxy-2-naphthylamide + H2O
Lys-Ala + 4-methoxy-2-naphthylamine
-
poor substrate
-
?
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
assay at 37°C, pH 8.0
-
-
?
Ala-Ala-2-naphthylamide + H2O
Ala-Ala + 2-naphthylamine
-
poor substrate
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
-
-
-
-
?
Arg-Arg-2-naphthylamide + H2O
Arg-Arg + 2-naphthylamine
-
substrate used in the activity assay
-
-
?
additional information
?
-
-
hydrolysis depending on type of amino acid and chain length
-
-
?
additional information
?
-
-
enzyme prefers a hydrophobic residue at P1 position
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Co2+
Zn2+
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-(4,5-dihydro-1H-imidazol-2-yl)-2-[(E)-2-phenylethenyl]-1H-benzimidazole
0.01 mM, 97.8% inhibition
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
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
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
-
-
p-hydroxymercuribenzoate
-
reactivation by reduced glutathione or mercaptoethanol
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
aFas
-
anti-fas antibody, aFas treated cells release lysosomal hydrolases into the culture medium
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
-
0.00015
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
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
8.6
-
assay condition with the synthetic substrate Arg-Arg-2-naphthylamide, determination of specific activity
7.4
-
physiological condition, determination of Ki values and kinetic parameters of the hydrolysis of endomorphin-1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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+
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). DPP3_HUMAN
737
0
82589
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
82000
80000 - 86000
82000
predicted, and verified by SDS-PAGE and Western Blot analysis, purified human erythtocyte DPP III and recombinant DPP III
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
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
S504G
-
mutation in S2 subsite, mutant does not show decreased binding of peptides with N-terminal arginine
additional information
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in human glioblastoma, ovarian carcinoma, pancreatic carcinoma and mouse fibroblast cells
into the pET21b vector for expression in Escherichia coli BL21DE3RIL+ cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased enzyme expression with recombinant constructs with Ets-1/Elk-1 proteins bind to binding motifs
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Abramic, M.; Zubanovic, M.; Vitale, L.
Dipeptidyl peptidase III from human erythrocytes
Biol. Chem. Hoppe-Seyler
369
29-38
1988
Homo sapiens
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
Jones, T.H.D.; Kapralou, A.
A rapid assay for dipeptidyl aminopeptidase III in human erythrocytes
Anal. Biochem.
119
418-423
1982
Homo sapiens
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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, Bacteroides thetaiotaomicron DSM 2079 (Q8A6N1), Homo sapiens (Q9NY33), Homo sapiens
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
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)
-
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)
-
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