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Information on EC 3.4.14.5 - dipeptidyl-peptidase IV and Organism(s) Sus scrofa and UniProt Accession P22411
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- 3.4.14.5
- mellitus
- glp-1
- peptide-1
- agonist
- cardiovascular
- sitagliptin
- metformin
-
antidiabetic
- incretins
-
glycemic
- sulfonylurea
- hypoglycemia
- vildagliptin
-
monotherapy
- hemoglobin
-
placebo
- pancreatic
-
glucose-lowering
-
glucose-dependent
-
sodium-glucose
- thiazolidinediones
-
insulinotropic
-
postprandial
-
glycated
-
incretin-based
- gip
- liraglutide
-
add-on
-
double-blind
- beta-cell
-
cotransporter
-
antihyperglycemic
-
exenatide
-
excursion
-
open-label
-
placebo-controlled
- pioglitazone
-
sulphonylureas
- pemphigoid
-
long-acting
-
bullous
- exendin-4
- mers-cov
-
real-world
- biguanides
-
once-daily
- medicine
-
macrovascular
-
once-weekly
- drug development
- veterinary medicine
- analysis
- pharmacology
- glargine
- food industry
-
enteroendocrine
- diagnostics
The taxonomic range for the selected organisms is: Sus scrofa
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, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
Synonyms
dpp-4, dipeptidyl peptidase-4, dpp-iv, dipeptidyl peptidase iv, dpp iv, dppiv, dipeptidyl peptidase 4, dipeptidyl peptidase-iv, dp iv, dipeptidylpeptidase iv, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACT3
-
-
-
-
ADABP
-
-
-
-
Adenosine deaminase complexing protein
-
-
-
-
amino acyl-prolyl dipeptidyl aminopeptidase
-
-
-
-
aminopeptidase, glycylproline
-
-
-
-
Bile canaliculus domain-specific membrane glycoprotein
-
-
-
-
dipeptidyl aminopeptidase IV
-
-
-
-
dipeptidyl-aminopeptidase IV
-
-
-
-
dipeptidyl-peptidase IV (CD26)
-
-
-
-
dipeptidyl-peptide hydrolase
-
-
-
-
DPP IV/CD26
-
-
-
-
Gly-Pro-naphthylamidase
-
-
-
-
glycoprotein GP110
-
-
-
-
glycylproline aminopeptidase
-
-
-
-
glycylproline-dipeptidyl-aminopeptidase
-
-
-
-
glycylprolyl aminopeptidase
-
-
-
-
glycylprolyl dipeptidylaminopeptidase
-
-
-
-
GP110 glycoprotein
-
-
-
-
leukocyte antigen CD26
-
-
-
-
lymphocyte, antigen CD26
-
-
-
-
Pep X
-
-
-
-
peptidase, dipeptidyl, IV
-
-
-
-
postproline dipeptidyl aminopeptidase IV
-
-
-
-
T cell triggering molecule Tp103
-
-
-
-
T-cell activation antigen CD26
-
-
-
-
THAM
-
-
-
-
Thymocyte-activating molecule
-
-
-
-
TP103
-
-
-
-
WC10
-
-
-
-
X-PDAP
-
-
-
-
X-prolyl dipeptidyl aminopeptidase
-
-
-
-
Xaa-Pro-dipeptidyl-aminopeptidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
catalytic domain structure, active site and substrate recognition study
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
cleaves dipeptides containing proline or alanine or one of several other amino acids at the penultimate position from the amino termini of substrates, contains a Ser-His-Asp catalytic triad, active site structure, the Glu-Glu motif is necessary for amino dipeptide selection
-
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
enzyme is an ectopeptidase
-
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
proline specific serine protease
-
CAS REGISTRY NUMBER
COMMENTARY
54249-88-6
-
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-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala-Ala
-
-
with traces of Ala4 and Ala after 2.5 h incubation
?
benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Gly-Gly-Pro + Gly-Gly-Pro-Ala + Ala + Gly-Pro + Gly-Pro-Ala + ?
-
-
-
?
Gly-L-Pro-rhodamine 110-(N-pentyl)maleimide + H2O
Gly-L-Pro + rhodamine 110-(N-pentyl)maleimide
-
-
-
-
?
Gly-Pro-2-naphthylamide + H2O
Gly-Pro + 2-naphthylamine
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Ala-4-methylcoumarin 7-amide + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Pro-4-nitroanilide + H2O
Lys-Pro + 4-nitroaniline
-
34% of the activity with Gly-Pro-4-nitroanilide
-
-
?
N-(Ala-Pro)-N'-6-(3,4-dichloromaleimidyl)-hexanoyl-rhodamine 110 + H2O
Ala-Pro + N-6-(3,4-dichloromaleimidyl)-hexanoyl-rhodamine 110
N-(Gly-Pro)-N'-(4-chlorobutanoyl)-rhodamine 110 + H2O
Gly-Pro + N-(4-chlorobutanoyl)-rhodamine 110
N-(Gly-Pro)-N'-(4-chloromethyl)benzoyl-rhodamine 110 + H2O
Gly-Pro + N-(4-chloromethyl)benzoyl-rhodamine 110
N-(Gly-Pro)-N'-(5-bromopentanoyl)-rhodamine 110 + H2O
Gly-Pro + N-(5-bromopentanoyl)-rhodamine 110
N-(Gly-Pro)-N'-(5-chloropentanoyl)-rhodamine 110 + H2O
Gly-Pro + N-(5-chloropentanoyl)-rhodamine 110
N-(Gly-Pro)-N'-4-(maleimidyl)butanoyl-rhodamine 110 + H2O
Gly-Pro + N-4-(maleimidyl)butanoyl-rhodamine 110
N-(Gly-Pro)-N'-6-(maleimidyl)hexanoyl-rhodamine 110 + H2O
Gly-Pro + N-6-(maleimidyl)hexanoyl-rhodamine 110
pituitary adenylate cyclase-activating polypeptide + H2O
?
-
pituitary adenylate cyclase-activating polypeptide (PACAP) is a neuropeptide with promising therapeutic applications for the treatment of several pathophysiological states related to neurodegenerative diseases. However, its use for therapeutic applications is actually limited by its restricted bioavailability and rapid degradation. N-terminal modifications confer resistance to dipeptidyl peptidase IV, a major proteolytic process involved in PACAP degradation
-
-
?
glucagon-like peptide-1 + H2O
?
-
dipeptidyl peptidase-IV is an enzyme responsible for the inactivation of the glucoregulatory incretin hormones glucagon-like peptide-1and glucose-dependent insulinotropic polypeptide
-
-
?
glucose-dependent insulinotropic polypeptide + H2O
?
-
dipeptidyl peptidase-IV is an enzyme responsible for the inactivation of the glucoregulatory incretin hormones glucagon-like peptide-1and glucose-dependent insulinotropic polypeptide
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
L-Ala-L-Ala-L-Ala-L-Ala + H2O
L-Ala-L-Ala
-
-
with traces of Ala3 and Ala after 2.5 h incubation
?
N-(Ala-Pro)-N'-6-(3,4-dichloromaleimidyl)-hexanoyl-rhodamine 110 + H2O
Ala-Pro + N-6-(3,4-dichloromaleimidyl)-hexanoyl-rhodamine 110
-
fluorogenic substrate
-
?
N-(Ala-Pro)-N'-6-(3,4-dichloromaleimidyl)-hexanoyl-rhodamine 110 + H2O
Ala-Pro + N-6-(3,4-dichloromaleimidyl)-hexanoyl-rhodamine 110
-
fluorogenic substrate, membrane-anchored on the cell surface in a cell-based assay
-
?
N-(Gly-Pro)-N'-(4-chlorobutanoyl)-rhodamine 110 + H2O
Gly-Pro + N-(4-chlorobutanoyl)-rhodamine 110
-
fluorogenic substrate
-
?
N-(Gly-Pro)-N'-(4-chlorobutanoyl)-rhodamine 110 + H2O
Gly-Pro + N-(4-chlorobutanoyl)-rhodamine 110
-
fluorogenic substrate, membrane-anchored on the cell surface in a cell-based assay
-
?
N-(Gly-Pro)-N'-(4-chloromethyl)benzoyl-rhodamine 110 + H2O
Gly-Pro + N-(4-chloromethyl)benzoyl-rhodamine 110
-
fluorogenic substrate
-
?
N-(Gly-Pro)-N'-(4-chloromethyl)benzoyl-rhodamine 110 + H2O
Gly-Pro + N-(4-chloromethyl)benzoyl-rhodamine 110
-
fluorogenic substrate, membrane-anchored on the cell surface in a cell-based assay
-
?
N-(Gly-Pro)-N'-(5-bromopentanoyl)-rhodamine 110 + H2O
Gly-Pro + N-(5-bromopentanoyl)-rhodamine 110
-
fluorogenic substrate
-
?
N-(Gly-Pro)-N'-(5-bromopentanoyl)-rhodamine 110 + H2O
Gly-Pro + N-(5-bromopentanoyl)-rhodamine 110
-
fluorogenic substrate, membrane-anchored on the cell surface in a cell-based assay
-
?
N-(Gly-Pro)-N'-(5-chloropentanoyl)-rhodamine 110 + H2O
Gly-Pro + N-(5-chloropentanoyl)-rhodamine 110
-
fluorogenic substrate
-
?
N-(Gly-Pro)-N'-(5-chloropentanoyl)-rhodamine 110 + H2O
Gly-Pro + N-(5-chloropentanoyl)-rhodamine 110
-
fluorogenic substrate, membrane-anchored on the cell surface in a cell-based assay
-
?
N-(Gly-Pro)-N'-4-(maleimidyl)butanoyl-rhodamine 110 + H2O
Gly-Pro + N-4-(maleimidyl)butanoyl-rhodamine 110
-
fluorogenic substrate
-
?
N-(Gly-Pro)-N'-4-(maleimidyl)butanoyl-rhodamine 110 + H2O
Gly-Pro + N-4-(maleimidyl)butanoyl-rhodamine 110
-
fluorogenic substrate, membrane-anchored on the cell surface in a cell-based assay
-
?
N-(Gly-Pro)-N'-6-(maleimidyl)hexanoyl-rhodamine 110 + H2O
Gly-Pro + N-6-(maleimidyl)hexanoyl-rhodamine 110
-
fluorogenic substrate
-
?
N-(Gly-Pro)-N'-6-(maleimidyl)hexanoyl-rhodamine 110 + H2O
Gly-Pro + N-6-(maleimidyl)hexanoyl-rhodamine 110
-
fluorogenic substrate, membrane-anchored on the cell surface in a cell-based assay
-
?
N-(Gly-Pro)-N'-acetyl-rhodamine 110 + H2O
Gly-Pro + N-acetyl-rhodamine 110
-
fluorogenic substrate
-
?
N-(Gly-Pro)-N'-acetyl-rhodamine 110 + H2O
Gly-Pro + N-acetyl-rhodamine 110
-
fluorogenic substrate, membrane-anchored on the cell surface in a cell-based assay
-
?
N-(Gly-Pro)-N'-chloroacetyl-rhodamine 110 + H2O
Gly-Pro + N-chloroacetyl-rhodamine 110
-
fluorogenic substrate
-
?
N-(Gly-Pro)-N'-chloroacetyl-rhodamine 110 + H2O
Gly-Pro + N-chloroacetyl-rhodamine 110
-
fluorogenic substrate, membrane-anchored on the cell surface in a cell-based assay
-
?
additional information
?
-
oligomerization state is important for interaction with other compounds, enzyme binds via Leu294 and Val341 to adenosine deaminase at T-cells, which is controlled by formation of a tetramer and glycosylation at Asn279
-
?
additional information
?
-
-
oligomerization state is important for interaction with other compounds, enzyme binds via Leu294 and Val341 to adenosine deaminase at T-cells, which is controlled by formation of a tetramer and glycosylation at Asn279
-
?
additional information
?
-
-
specificity: specific for the S configuration of the amino-acid residue in P1 and P2 position if the penultimate residue is Pro, derivatives of Gly-Pro-4-nitroanilide where the N-terminal amino group is methylated are hydrolyzed
-
-
?
additional information
?
-
-
broad substrate specificity, structural elements of the substrate protein outside the immediate primary sequence of the cleavage site are crucial
-
?
additional information
?
-
-
larger compounds are cleaved with lower efficiency, importance of steric effects
-
?
additional information
?
-
-
the enzyme participates in the catabolism of bradykinin and substance P as well as the post-translational processing of various other peptides
-
-
?
additional information
?
-
-
enzyme plays a key role in the regulation of differentiation and growth of lymphocytes
-
?
NATURAL SUBSTRATE
NATURAL 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
glucagon-like peptide-1 + H2O
?
-
dipeptidyl peptidase-IV is an enzyme responsible for the inactivation of the glucoregulatory incretin hormones glucagon-like peptide-1and glucose-dependent insulinotropic polypeptide
-
-
?
glucose-dependent insulinotropic polypeptide + H2O
?
-
dipeptidyl peptidase-IV is an enzyme responsible for the inactivation of the glucoregulatory incretin hormones glucagon-like peptide-1and glucose-dependent insulinotropic polypeptide
-
-
?
additional information
?
-
-
the enzyme participates in the catabolism of bradykinin and substance P as well as the post-translational processing of various other peptides
-
-
?
additional information
?
-
-
enzyme plays a key role in the regulation of differentiation and growth of lymphocytes
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-{2-[2-(5-cyano-4,5-dihydropyrazol-1-yl)-2-oxoethylamino]ethylamino}nicotinonitrile
-
i.e. KR-62436, IC50: 0.00049 mM, selective competitive inhibitor, good lead compound for further development as a new anti-diabetic agent, almost completely inhibits DPP-IV mediated degradation of glucagon-like peptide-1
7-[(3R)-3-amino-1-oxo-4-(2,5-difluorophenyl)butyl]-5,6,7,8-tetrahydro-3-(trifluoromethyl)-1,2,4-triazolo[4,3-a]pyrazine
-
inhibition of DPP-IV does not alter the circulating levels of insulin-like growth factor 1 (biomarker for the physiological relevance of DPP-IV activity) in the growing pig
diethyldicarbonate
-
modification of 4 His residues per subunit using diethyldicarbonate results in 30% inactivation
diphenyl [1-(N-(15-oxo-19-[(4R)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-4,7,10-trioxa-14-azanonadec-1-yl)-L-glutaminyl)pyrrolidin-2-yl]phosphonate
-
irreversible inhibitor
human HIV-1 Asp2-Tat(1-9) peptide
-
amino acid sequence MDPVDPNIE, moderate inhibitor
human HIV-1 Glu2-Tat(1-9) peptide
-
amino acid sequence MEPVDPNIE, moderate inhibitor
human HIV-1 His2-Tat(1-9) peptide
-
amino acid sequence MHPVDPNIE, strong inhibitor
human HIV-1 Phe2-Tat(1-9) peptide
-
amino acid sequence MFPVDPNIE, strong inhibitor
human HIV-1 Tat(1-9) peptide
-
amino acid sequence MDPVDPNIE, N-terminal peptide of the viral Tat protein, natural inhibitor, inhibits antigen-, anti-CD-3- and mitogen-induced activation of human T-cells
-
human HIV-1 Trp2-Tat(1-9) peptide
-
amino acid sequence MWPVDPNIE, most effective Tat peptide inhibitor derivative
-
human HIV-1 Tyr2-Tat(1-9) peptide
-
amino acid sequence MYPVDPNIE, strong inhibitor
interleukin-2 peptide Met-IL-2(1-9)
-
amino acid sequence MAPTSSSTKK, weak inhibitor
Met-GCSF(1-9) peptide
-
GCSF is the granulocyte colony stimulating factor, weak inhibitor
N-bromosuccinimide
-
almost completely inactivates with the modification of only one Trp residue per subunit, protective action of the substrate and inhibitors such as Ala-Pro-Ala and Pro-Pro
thromboxane A2 receptor peptide TXA2-R(1-9)
-
N-terminal MWP sequence motif MWPNGSSLG, strong inhibitor
-
Nepsilon-nitrobenzyloxycarbonyl-Lys-thiazolidide
-
suppresses mitogen- and alloantigen-induced T-cell proliferation, B-cell differentiation, immunoglobulin secretion and modulates cytokine production
additional information
-
proline substrates, Pro in P1, with R configuration in P2 are inhibitors of the hydrolysis of proline substrates with an S,S configuration in an uncompetitive or mixed inhibition type
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00058
N-(Ala-Pro)-N'-6-(3,4-dichloromaleimidyl)-hexanoyl-rhodamine 110
-
pH 7.2, 30°C
additional information
additional information
-
Km values for X-Pro-4-nitroanilides
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
turnover-numbers for X-Pro-4-nitroanilides
-
0.55
N-(Ala-Pro)-N'-6-(3,4-dichloromaleimidyl)-hexanoyl-rhodamine 110
-
pH 7.2, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000251
1-[2-amino-3-(4-iodophenyl)propanoyl]pyrrolidine--2-carbonitrile
-
0.04316
diphenyl [1-(N-(15-oxo-19-[(4R)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-4,7,10-trioxa-14-azanonadec-1-yl)-L-glutaminyl)pyrrolidin-2-yl]phosphonate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00049
6-{2-[2-(5-cyano-4,5-dihydropyrazol-1-yl)-2-oxoethylamino]ethylamino}nicotinonitrile
Sus scrofa
-
i.e. KR-62436, IC50: 0.00049 mM, selective competitive inhibitor, good lead compound for further development as a new anti-diabetic agent, almost completely inhibits DPP-IV mediated degradation of glucagon-like peptide-1
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8 - 8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). DPP4_PIG
766
1
88242
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
115000
130000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
is likely to enhance the receptor-ligand affinity by bivalent interaction which may be critical for signal transduction into the cell
dimer
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
N-glycosylation at Asn279 is important for adenosine deaminase binding
glycoprotein
side-chain modification
side-chain modification
-
contains 18.3% of carbohydrate consisting of mannose, galactose, fucose, glucosamine and sialic acid
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
20 mg/ml purified enzyme, sitting drop vapour diffusion method, room temperature, several days, from 20-22% PEG 2000, 0.1 ammonium sulfate, 0.1 M Tris-HCl, pH 8.0, covering of the drops with perfluoropolyether oil, humidity control during harvest of crystals, multiple wavelength anomalous dispersion using a mercury derivative and subsequent noncrystallographic symmetry averaging, structure determination and analysis, modeling
DPIV complexes with a t-butyl-Gly-Pro-Ile tripeptide, Pro-boroPro, tert-butyl-Gly-L-Pro-L-Ile, 7-benzyl-1,3-dimethyl-8-piperazin-1-yl-3,7-dihydro-purine-2,6-dione and 4-(2-aminoethyl)-benzene sulfonyl fluoride
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
modification of 4 His residues per subunit using diethyldicarbonate results in 30% inactivation
-
N-bromosuccinimide almost completely inactivates with the modification of only one Trp residue per subunit, protective action of the substrate and inhibitors such as Ala-Pro-Ala and Pro-Pro
-
treatment with trypsin, chymotrypsin A, pronase P and papain decrease the activity of the kidney enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
inhibition of DPP-IV can be an effective approach to treat type 2 diabetes mellitus by potentiating insulin secretion. 6-{2-[2-(5-cyano-4,5-dihydropyrazol-1-yl)-2-oxoethylamino]ethylamino}nicotinonitrile, i.e. KR-62436, could be good lead compound for further development as a new anti-diabetic agent
medicine
-
pituitary adenylate cyclase-activating polypeptide (PACAP) is a neuropeptide with promising therapeutic applications for the treatment of several pathophysiological states related to neurodegenerative diseases. However, its use for therapeutic applications is actually limited by its restricted bioavailability and rapid degradation. N-terminal modifications confer resistance to dipeptidyl peptidase IV, a major proteolytic process involved in PACAP degradation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heins, J.; Welker, P.; Schnlein, C.; Born, I.; Hartrodt, B.; Neubert, K.; Tsuru, D.; Barth, A.
Mechanism of proline-specific proteinases: (I) Substrate specificity of dipeptidyl peptidase IV from pig kidney and proline-specific endopeptidase from Flavobacterium meningosepticum
Biochim. Biophys. Acta
954
161-169
1988
Sus scrofa
Gonschor, H.; Schfer, W.
Dipeptidyl peptidase IV. Purification for use in peptide sequencing
Biol. Chem. Hoppe-Seyler
366
157-165
1985
Sus scrofa
Harada, M.; Hiraoka, B.Y.; Fukasawa, K.M.; Fukasawa, K.
Chemical modification of dipeptidyl peptidase iv: involvement of an essential tryptophan residue at the substrate binding site
Arch. Biochem. Biophys.
234
622-628
1984
Sus scrofa
Heins, J.; Neubert, K.; Barth, A.; Canizaro, P.C.; Behal, F.J.
Kinetic investigation of the hydrolysis of aminoacyl p-nitroanilides by dipeptidyl peptidase IV from human and pig kidney
Biochim. Biophys. Acta
785
30-35
1984
Homo sapiens, Rattus norvegicus, Sus scrofa
Fukasawa, K.M.; Fukasawa, K.; Hiraoka, B.Y.; Harada, M.
Characterization of a soluble form of dipeptidyl peptidase IV from pig liver
Experientia
39
1005-1007
1983
Sus scrofa
Ichinose, M.; Maeda, R.; Fukuda, T.; Watanabe, B.; Ishimaru, T.; Izumi, M.; Miyake, S.; Takamori, M.
Partial purification and characterization of glycylprolyl dipeptidyl aminopeptidase in porcine pancreas
Biochim. Biophys. Acta
719
527-531
1982
Sus scrofa
Yoshimoto, T.; Kita, T.; Ichinose, M.; Tsuru, D.
Dipeptidyl aminopeptidase IV from porcine pancreas
J. Biochem.
92
275-282
1982
Sus scrofa
Fukasawa, K.M.; Fukasawa, K.; Hiraoka, B.Y.; Harada, M.
Comparison of dipeptidyl peptidase IV prepared from pig liver and kidney
Biochim. Biophys. Acta
657
179-189
1981
Sus scrofa
Macnair, R.D.C.; Kenny, A.J.
Proteins of the kidney microvillar membrane. The amphipathic form of dipeptidyl peptidase IV
Biochem. J.
179
379-395
1979
Sus scrofa
Svensson, B.; Danielsen, M.; Staun, M.; Jeppesen, L.; Noren, O.; Sjstrm, H.
An amphiphilic form of dipeptidyl peptidase IV from pig small-intestinal brush-border membrane. Purification by immunoadsorbent chromatography and some properties
Eur. J. Biochem.
90
489-498
1978
Sus scrofa
Fukasawa, K.M.; Fukasawa, K.; Harada, M.
Dipeptidyl aminopeptidase IV, a glycoprotein from pig kidney
Biochim. Biophys. Acta
535
161-166
1978
Sus scrofa
Kenny, A.J.; Booth, A.G.; George, S.G.; Ingram, J.; Kershaw, D.; Wood, E.J.; Young, A.R.
Dipeptidyl peptidase IV, a kidney brush-border serine peptidase
Biochem. J.
155
169-182
1976
Sus scrofa
Ohkubo, I.; Huang, K.; Ochiai, Y.; Takagaki, M.; Kani, K.
Dipeptidyl peptidase IV from porcine seminal plasma: purification, characterization, and N-terminal amino acid sequence
J. Biochem.
116
1182-1186
1994
Sus scrofa
Lorey, S.; Faust, J.; Buhling, F.; Ansorge, S.; Neubert, K.
A new type of fluorogenic substrates for determination of cellular dipeptidyl peptidase IV (DP IV/CD26) activity
Adv. Exp. Med. Biol.
477
111-115
2000
Sus scrofa
Stockel-Maschek, A.; Stiebitz, B.; Born, I.; Faust, J.; Mogelin, W.; Neubert, K.
Potent inhibitors of dipeptidyl peptidase IV and their mechanisms of inhibition
Adv. Exp. Med. Biol.
477
117-123
2000
Sus scrofa
Faust, J.; Fuchs, P.; Wrenger, S.; Reinhold, D.; Stoeckel-Maschek, A.; Kaehne, T.; Ansorge, S.; Neubert, K.
Dipeptidyl peptidase IV inhibitors with the N-terminal MXP sequence: structure-activity-relationships
Adv. Exp. Med. Biol.
524
175-179
2003
Sus scrofa
Stoeckel-Maschek, A.; Stiebitz, B.; Faust, J.; Born, I.; Kaehne, T.; Gorrell, M.D.; Neubert, K.
Different inhibition mechanisms of dipeptidyl peptidase IV by tryptophan containing peptides and amides
Adv. Exp. Med. Biol.
524
69-72
2003
Homo sapiens, Sus scrofa
Rosenblum, J.S.; Kozarich, J.W.
Prolyl peptidases: a serine protease subfamily with high potential for drug discovery
Curr. Opin. Chem. Biol.
7
496-504
2003
Homo sapiens, Mammalia, Mus musculus, Rattus norvegicus, Sus scrofa
Lorey, S.; Faust, J.; Mrestani-Klaus, C.; Kaehne, T.; Ansorge, S.; Neubert, K.; Buehling, F.
Transcellular proteolysis demonstrated by novel cell surface-associated substrates of dipeptidyl peptidase IV (CD26)
J. Biol. Chem.
277
33170-33177
2002
Sus scrofa
Engel, M.; Hoffmann, T.; Wagner, L.; Wermann, M.; Heiser, U.; Kiefersauer, R.; Huber, R.; Bode, W.; Demuth, H.U.; Brandstetter, H.
The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism
Proc. Natl. Acad. Sci. USA
100
5063-5068
2003
Sus scrofa (P22411), Sus scrofa
Gilmore, B.F.; Carson, L.; McShane, L.L.; Quinn, D.; Coulter, W.A.; Walker, B.
Synthesis, kinetic evaluation, and utilization of a biotinylated dipeptide proline diphenyl phosphonate for the disclosure of dipeptidyl peptidase IV-like serine proteases
Biochem. Biophys. Res. Commun.
347
373-379
2006
Sus scrofa
Kim, K.R.; Rhee, S.D.; Kim, H.Y.; Jung, W.H.; Yang, S.D.; Kim, S.S.; Ahn, J.H.; Cheon, H.G.
KR-62436, 6-{2-[2-(5-cyano-4,5-dihydropyrazol-1-yl)-2-oxoethylamino]ethylamino}nicotinonitrile, is a novel dipeptidyl peptidase-IV (DPP-IV) inhibitor with anti-hyperglycemic activity
Eur. J. Pharmacol.
518
63-70
2005
Homo sapiens, Rattus norvegicus, Sus scrofa
Engel, M.; Hoffmann, T.; Manhart, S.; Heiser, U.; Chambre, S.; Huber, R.; Demuth, H.U.; Bode, W.
Rigidity and flexibility of dipeptidyl peptidase IV: crystal structures of and docking experiments with DPIV
J. Mol. Biol.
355
768-783
2006
Sus scrofa (P22411), Sus scrofa
Taldone, T.; Zito, S.W.; Talele, T.T.
Inhibition of dipeptidyl peptidase-IV (DPP-IV) by atorvastatin
Bioorg. Med. Chem. Lett.
18
479-484
2008
Sus scrofa
Drucker, D.J.
Dipeptidyl peptidase-4 inhibition and the treatment of type 2 diabetes: preclinical biology and mechanisms of action
Diabetes Care
30
1335-1343
2007
Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Faidley, T.D.; Leiting, B.; Pryor, K.D.; Lyons, K.; Hickey, G.J.; Thompson, D.R.
Inhibition of dipeptidyl-peptidase IV does not increase circulating IGF-1 concentrations in growing pigs
Exp. Biol. Med.
231
1373-1378
2006
Sus scrofa
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Transporter Classification Database (TCDB): 8.A.51.1.5
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