3.4.14.5: dipeptidyl-peptidase IV
This is an abbreviated version!
For detailed information about dipeptidyl-peptidase IV, go to the full flat file.
Word Map on EC 3.4.14.5
-
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
- 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
Reaction
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
(GLP1)-degrading enzyme, ACT3, ADA binding protein, ADA-binding protein, ADABP, adenosine deaminase binding protein, Adenosine deaminase complexing protein, adenosine deaminase-binding protein, amino acyl-prolyl dipeptidyl aminopeptidase, aminopeptidase, glycylproline, Bile canaliculus domain-specific membrane glycoprotein, CD26, CD26 peptidase, CD26/dipeptidyl peptidase, CD26/DP IV, DAP IV, DapB, dapUm, dipeptidyl aminopeptidase IV, dipeptidyl dipeptidase IV, dipeptidyl peptidase 4, dipeptidyl peptidase 8, dipeptidyl peptidase 9, dipeptidyl peptidase IV, dipeptidyl peptidase-4, dipeptidyl peptidase-IV, dipeptidyl-aminopeptidase IV, dipeptidyl-peptidase 4, dipeptidyl-peptidase IV (CD26), dipeptidyl-peptide hydrolase, dipeptidylpeptidase 4a, dipeptidylpeptidase 4b, dipeptidylpeptidase IV, dipeptidylpeptidase IV/CD26, dipeptidylpeptidase-IV, DP IV, DP-IV, DPIV, DPP, DPP IV, DPP IV/CD26, DPP-4, DPP-IV, DPP4, DPP8, DPP9, DPPIV, DppIVA, DppIVB, glucagon-like peptide 1-degrading enzyme, Gly-Pro-naphthylamidase, glycoprotein GP110, glycylproline aminopeptidase, glycylproline-dipeptidyl-aminopeptidase, glycylprolyl aminopeptidase, glycylprolyl dipeptidylaminopeptidase, GP110 glycoprotein, h-DPPIV, hDPPIV, leukocyte antigen CD26, lymphocyte, antigen CD26, More, omega DPPIV, omega enzyme, omega gene product, Pep X, peptidase, dipeptidyl, IV, PepX, postproline dipeptidyl aminopeptidase IV, prolyl-dipeptidyl-aminopeptidase, sipeptidyl peptidase IV, T cell triggering molecule Tp103, T-cell activation antigen CD26, THAM, Thymocyte-activating molecule, TP103, type IV dipeptidyl aminopeptidase, WC10, X-PDAP, X-prolyl dipeptidyl aminopeptidase, X-prolyl-dipeptidyl aminopeptidase, Xaa-Pro-dipeptidyl-aminopeptidase
ECTree
3.4.14.5 dipeptidyl-peptidase IVAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.14.5 - dipeptidyl-peptidase IV
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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-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala-Ala
-
-
with traces of Ala4 and Ala after 2.5 h incubation
?
Ala-Pro-7-amido-4-trifluoromethyl coumarin + H2O
Ala-Pro + 7-amino-4-trifluoromethyl coumarin
-
-
?
Ala-Pro-7-amido-4-trifluoromethylcoumarin + H2O
Ala-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
amyloid beta40 + H2O
?
-
-
enzyme is able to truncate the commercial amyloid beta40 and amyloid beta42 peptides, to hinder the fibril formation by them and to participate in the disaggregation of preformed fibrils of these peptides
-
?
amyloid beta42 + H2O
?
-
-
enzyme is able to truncate the commercial amyloid beta40 and amyloid beta42 peptides, to hinder the fibril formation by them and to participate in the disaggregation of preformed fibrils of these peptides
-
?
Arg-Pro-7-amido-4-methylcoumarin + H2O
Arg-Pro + 7-amino-4-methylcoumarin
-
high activity
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly
Arg-Pro + Lys-Pro-Gln-Gln-Phe-Phe-Gly
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2 + H2O
Arg-Pro + Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2
-
-
-
-
?
Asn-Pro-7-amido-4-methylcoumarin + H2O
Asn-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Asp-Pro-7-amido-4-methylcoumarin + H2O
Asp-Pro + 7-amino-4-methylcoumarin
-
low activity
-
?
B-type natriuretic peptide (1-32) + H2O
B-type natriuretic peptide (3-32) + L-Ser-L-Pro
-
DPP IV removes the two amino terminal amino acids (Ser-Pro) from B-type natriuretic peptide (1-32) to produce B-type natriuretic peptide (3-32)
-
-
?
B-type natriuretic peptide(1-32) + H2O
B-type natriuretic peptide(3-32) + ?
-
-
-
-
?
B-type natriuretic propeptide (1-108) + H2O
B-type natriuretic propeptide (3-306) + ?
-
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Gly-Gly-Pro-Ala + H2O
Gly-Gly-Pro + Gly-Gly-Pro-Ala + Ala + Gly-Pro + Gly-Pro-Ala + ?
-
-
-
?
beta-casomorphin + H2O
fragments
-
cleavage sites: YP-/-FP-/-GP-/-IGP-/-RP
-
?
EPLGRQLTSGP + H2O
Glu-Pro + LGRQLTSGP
-
the sequence EPLGRQLTSGP, which corresponds to the propeptide fragment of alpha-2 plasmin inhibitor
-
-
?
gastrin releasing peptide-(1-27) + H2O
?
-
i.e. GRP-(1-27), cleaves N-terminal dipeptide VP
-
ir
gastrin releasing peptide-(3-27) + H2O
?
-
i.e. GRP-(3-27), cleaves N-terminal dipeptide LP
-
ir
Gln-Pro-7-amido-4-methylcoumarin + H2O
Gln-Pro + 7-amino-4-methylcoumarin
-
-
-
?
GLP-1 + H2O
?
-
an incretin involved in the glucose-dependent production of insulin
-
?
Glu-Pro-4-methylcoumarin 7-amide + H2O
Glu-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Glu-Pro-7-amido-4-methylcoumarin + H2O
Glu-Pro + 7-amino-4-methylcoumarin
-
low activity
-
?
glucose-dependent insulinotropic polypeptide(1-30) peptide + H2O
?
-
GIP-fragment
-
?
glucose-dependent insulinotropic polypeptide(1-42) peptide + H2O
?
-
GIP-fragment
-
?
glucose-dependent insulinotropic polypeptide(1-6) peptide + H2O
?
-
GIP-fragment, very low activity
-
?
gluteomorphin + H2O
?
-
food-derived opioid from wheat gluten, 45.7% hydrolysis at 2 mM
-
-
?
Gly-Ala-4-methylcoumarin 7-amide + H2O
Gly-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-azetidine-2-carboxyl-3,5-dibromo-4-hydroxyanilide + H2O
Gly-azetidine + 3,5-dibromo-4-hydroxyaniline
-
-
-
-
?
Gly-L-hydroxyproline-3,5-dibromo-4-hydroxyanilide + H2O
Gly-L-hydroxyproline + 3,5-dibromo-4-hydroxyaniline
-
-
-
-
?
Gly-L-Pro-4-methoxy-beta-naphthylamide + H2O
Gly-L-Pro + 4-methoxy-beta-naphthylamine
-
-
-
?
Gly-L-Pro-rhodamine 110-(N-pentyl)maleimide + H2O
Gly-L-Pro + rhodamine 110-(N-pentyl)maleimide
-
-
-
-
?
Gly-Pro-3,5-dibromo-4-hydroxyanilide + H2O
Gly-Pro + 3,5-dibromo-4-hydroxyaniline
-
-
-
-
?
Gly-Pro-4-methoxy-2-naphthylamide
Gly-Pro + 4-methoxy-2-naphthylamine
fluorogenic substrate
-
?
Gly-Pro-4-methoxy-beta-naphthylamide + H2O
Gly-Pro + 4-methoxy-beta-naphthylamine
-
-
-
-
?
Gly-Pro-4-methylcoumarin-7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-trifluoromethyl coumarin + H2O
Gly-Pro + 7-amino-4-trifluoromethyl coumarin
-
-
-
-
?
Gly-Pro-beta-naphthylamide + H2O
Gly-Pro + beta-naphthylamine
-
-
-
-
?
Gly-Pro-glycinamide + H2O
?
-
CD26 plays a direct regulatory and indispensable role in the eventual antiretroviral activity of small synthetic molecules such as the antiretroviral prodrug Gly-Pro-glycinamide
-
-
?
Gly-Pro-glycinamide + H2O
Gly-Pro + glycinamide
-
the anti-HIV drug Gly-Pro-glycinamide is not active as such, but rather behaves as a prodrug that must be obligatorily cleaved by VD26/DPP IV to Gly-Pro and glycinamide to exert its antiretroviral activity
-
-
?
Gly-Pro-Leu-Gly-Pro + H2O
?
-
11% of the activity with Gly-Pro-4-nitroanilide
-
-
?
growth hormone releasing hormone-(1-29) fragment + H2O
?
-
i.e. GHRH-(1-29), cleaves N-terminal dipeptide YA
-
ir
growth hormone releasing hormone-(1-44) fragment + H2O
?
-
i.e. GHRH-(1-44), cleaves N-terminal dipeptide YA
-
ir
His-Pro-7-amido-4-methylcoumarin + H2O
His-Pro + 7-amino-4-methylcoumarin
-
-
-
?
human glucagon-like peptide 1 (7-36) + H2O
?
-
i.e. His-Ala-/-Glu-Gly-Thr-Phe-Thr-Ser-Asp
-
-
?
human glucagon-like peptide 2 + H2O
?
-
i.e. His-Ala-/-Asp-Gly-Ser-Phe-Ser-Asp-Glu
-
-
?
human glucose-dependent insulinotropic polypeptide + H2O
?
-
i.e. Tyr-Ala-/-Glu-Gly-Thr-Phe-Thr-Ser-Asp-
-
-
?
human growth hormone-releasing factor + H2O
?
-
i.e. Tyr-Ala-/-Asp-Ala-Ile-Phe-Thr-Asn-Ser-
-
-
?
human neuropeptide Y + H2O
Tyr-Pro + Ser-Lys-Pro-Asp-Asn-Pro-Gly
-
i.e. Tyr-Pro-/-Ser-Lys-Pro-Asp-Asn-Pro-Gly
-
-
?
human peptide YY + H2O
Tyr-Pro + Ile-Lys-Pro-Glu-Ala-Pro-Gly-
-
i.e. Tyr-Pro-/-Ile-Lys-Pro-Glu-Ala-Pro-Gly-
-
?
IFN-gamma-inducible protein 10 + H2O
?
-
i.e. IP-10 or CXCL10, chemokine
-
?
IFN-inducible T-cell alpha-chemoattractant + H2O
?
-
i.e. I-TAC or CXCL11, chemokine
-
?
Ile-Pro-7-amido-4-methylcoumarin + H2O
Ile-Pro + 7-amino-4-methylcoumarin
-
-
-
?
incretin hormone glucagon-like peptide 1 + H2O
?
-
i.e. GLP-1, degradation, regulation of activity
-
?
L-Ala-L-Pro-7-amido-4-trifluoromethylcoumarin + H2O
L-Ala-L-Pro + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
L-Arg-L-Pro-7-amido-4-methylcoumarin + H2O
L-Arg-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Asp-L-Pro-p-nitroanilide + H2O
L-Asp-L-Pro + p-nitroaniline
-
least preferred substrate
-
-
?
L-Pro-L-Ala-7-amido-4-trifluoromethylcoumarin + H2O
L-Pro-L-Ala + 7-amino-4-trifluoromethylcoumarin
-
-
-
-
?
L-Thr-L-Pro-7-amido-4-methylcoumarin + H2O
L-Thr-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Val-L-Pro-L-Val-L-Pro-beta-D-arabinofuranosyladenosine + H2O
L-Val-L-Pro-L-Val-L-Pro + beta-D-arabinofuranosyladenosine
L-Val-L-Pro-L-Val-L-Pro-beta-D-arabinofuranosylcytosine + H2O
L-Val-L-Pro-L-Val-L-Pro + beta-D-arabinofuranosylcytosine
Leu-Pro-4-methylcoumarin 7-amide + H2O
Leu-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Leu-Pro-7-amido-4-methylcoumarin + H2O
Leu-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Lys-Pro-4-methylcoumarin 7-amide + H2O
Lys-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Met-Pro-7-amido-4-methylcoumarin + H2O
Met-Pro + 7-amino-4-methylcoumarin
-
-
-
?
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
N-terminal B-type natriuretic propeptide (1-76) + H2O
N-terminal B-type natriuretic propeptide (3-76) + ?
-
-
-
-
?
N-tosyl-Gly-L-Pro-7-amido-4-methylcoumarin + H2O
N-tosyl-Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
norleucine-Pro-7-amido-4-methylcoumarin + H2O
norleucine-Pro + 7-amino-4-methylcoumarin
-
-
-
?
NPY + H2O
?
-
important step in the neuropeptide-Y NPY-mediated angiogenesis
-
?
peptide YY + H2O
peptide YY fragment 3-36
-
high affinity substrate of DPP-IV
-
-
?
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
-
-
?
pituitary adenylate cyclase-activating polypeptide-(1-27) + H2O
?
-
i.e. PACAP27, cleaves N-terminal dipeptide HS
-
?
Pro-4-nitroanilide + H2O
Pro + 4-nitroaniline
-
2% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Pro-Pro-7-amido-4-methylcoumarin + H2O
Pro-Pro + 7-amino-4-methylcoumarin
-
-
-
?
QPDAINAP + H2O
Gln-Pro + DAINAP
peptide sequence corresponds to the N-terminus of human MCP1 protein
-
?
RANTES + H2O
?
-
i.e. CCL5 or regulated on activation normal T-cell expressed and secreted, chemokine
-
?
Ser-Pro-7-amido-4-methylcoumarin + H2O
Ser-Pro + 7-amino-4-methylcoumarin
-
-
-
?
soymorphin + H2O
?
-
food-derived opioid from soybean beta-conglycinin beta-subunit, 83.8% hydrolysis at 2 mM
-
-
?
SPYSSDTT + H2O
Ser-Pro + YSSDTT
peptide sequence corresponds to the N-terminus of human RANTES protein
-
?
stromal cell derived factor 1 + H2O
?
-
i.e. SDF-1 or CXCL12, chemokine
-
?
substance P + H2O
peptides SP(3-11) + SP(5-11) + ?
-
i.e. SP, sequential cleavage of full length substance P
both fragments are still active
?
substance P + H2O
substance P peptide fragments
-
cleavage sites: RP-/-KP-/-QQFFGLM
-
?
Tyr-Pro-7-amido-4-methylcoumarin + H2O
Tyr-Pro + 7-amino-4-methylcoumarin
-
-
-
?
VPAC2P-PEG + H2O
?
-
VPAC2P-PEG is a VPAC2 receptor agonist peptide that acts as a glucose-dependent insulin secretagogue. Proteolysis by DPPIV may contribute to the in vivo clearance of VPAC2P-PEG. The N-terminus of VPAC2P-PEG is modified by N-terminal acetylation to impart DPPIV resistance. The acetylated peptide, Ac-VPAC2P-PEG, is a selective and potent VPAC2 agonist, resistant to DPPIV proteolysis
-
-
?
[Gly2]glucose-dependent insulinotropic polypeptide(1-30) peptide + H2O
?
-
GIP-fragment with glycine at position 2 in the sequence
-
?
[Ser2]glucose-dependent insulinotropic polypeptide(1-30) peptide + H2O
?
-
GIP-fragment with serine at position 2 in the sequence
-
?
[Ser2]glucose-dependent insulinotropic polypeptide(1-6) peptide + H2O
?
-
GIP-fragment with serine at position 2 in the sequence
-
?
[Val2]glucose-dependent insulinotropic polypeptide(1-30) peptide + H2O
?
-
GIP-fragment with valine at position 2 in the sequence
-
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
-
1% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Ala-Ala-4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
-
2% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Ala-Ala-4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
-
2% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Ala-Ala-4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
-
-
-
-
?
Ala-Ala-4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
-
-
-
-
?
Ala-Ala-4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
-
20% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Ala-Ala-4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
36% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
-
high activity
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
-
-
-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
-
-
-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
-
-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
-
-
-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
80% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Ala-Pro-7-amido-4-methylcoumarin + H2O
Ala-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Pro-7-amido-4-methylcoumarin + H2O
Ala-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Pro-7-amido-4-methylcoumarin + H2O
Ala-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Pro-7-amido-4-methylcoumarin + H2O
Ala-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Pro-7-amido-4-methylcoumarin + H2O
Ala-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Ala-Pro-Gly + H2O
Ala-Pro + Gly
-
11% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Ala-Pro-Gly + H2O
Ala-Pro + Gly
-
11% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Ala-Pro-Gly + H2O
Ala-Pro + Gly
-
72% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
2% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
-
2% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
130% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
130% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
-
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
-
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
48.6% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
48.6% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
42% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
55% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
-
55% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Asn-Pro-4-nitroanilide + H2O
Asn-Pro + 4-nitroaniline
-
poor substrate
-
?
Asp-Pro-4-nitroanilide + H2O
Asp-Pro + 4-nitroaniline
11% of the activity with Gly-Pro-4-nitroanilide
-
-
?
beta-casein + H2O
?
-
cleavage of the proline-rich sequence
-
-
?
beta-casomorphin + H2O
?
-
food-derived opioid from milk casein, 33.4% hydrolysis at 2 mM
-
-
?
beta-casomorphin + H2O
?
-
beta-casomorphin from human, i.e. Tyr-Pro-Phe-Val-Glu-Pro-Ileu
-
-
?
beta-casomorphin + H2O
?
-
beta-casomorphin from bovine, i.e. Tyr-Pro-Phe-Val-Glu-Pro-Ile
-
-
?
gastrin releasing peptide + H2O
?
-
sequential cleavage of 2 N-terminal peptides
-
?
Glu-Pro-4-nitroanilide + H2O
Glu-Pro + 4-nitroaniline
-
23% of the activity with Gly-Pro-4-nitroanilide
-
-
?
glucagon-like peptide 1 + H2O
?
-
-
679446, 695514, 697297, 697436, 697526, 697551, 697832, 698213, 698335, 699174, 699445, 699745, 700399, 701371, 702611, 703552
-
-
?
glucagon-like peptide 1 + H2O
?
-
i.e. GLP-1, degradation, regulation of activity
-
ir
glucagon-like peptide 1 + H2O
?
-
i.e. GLP-1, incretin, degradation, regulation of activity
-
?
glucagon-like peptide 1 + H2O
?
-
-
-
-
?
glucagon-like peptide 1 + H2O
?
-
i.e. GLP-1, degradation, regulation of activity
-
?
glucagon-like peptide 1 + H2O
?
-
i.e. GLP-1, degradation, regulation of activity, cleaves N-terminal dipeptide HA
-
ir
glucagon-like peptide 2 + H2O
?
-
i.e. GLP-1, degradation, regulation of activity, cleaves N-terminal dipeptide HA
-
ir
glucagon-like peptide-1 + H2O
?
-
-
-
-
?
glucagon-like peptide-1 + H2O
?
-
dipeptidyl peptidase IV inactivates the hormone, thereby cancelling the prandial insulinotropic effect
-
-
?
glucagon-like peptide-1 + H2O
?
-
DPP-IV is the main proteolytic enzyme responsible for the rapid inactivation of glucagon-like peptide-1 into metabolites that are devoid of insulin-releasing activity
-
-
?
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 peptide + H2O
?
-
-
-
-
?
glucose-dependent insulinotropic peptide + H2O
?
-
-
-
-
?
glucose-dependent insulinotropic polypeptide + H2O
?
-
-
-
-
?
glucose-dependent insulinotropic polypeptide + H2O
?
-
i.e. GIP, incretin
-
?
glucose-dependent insulinotropic polypeptide + H2O
?
-
dipeptidyl peptidase IV inactivates the hormone, thereby cancelling the prandial insulinotropic effect
-
-
?
glucose-dependent insulinotropic polypeptide + H2O
?
-
DPP-IV is the main proteolytic enzyme responsible for the rapid inactivation of glucose-dependent insulinotropic polypeptide into metabolites that are devoid of insulin-releasing activity
-
-
?
glucose-dependent insulinotropic polypeptide + H2O
?
-
i.e. GIP, cleaves N-terminal dipeptide YA
-
ir
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-Ala-4-nitroanilide + H2O
Gly-Ala + 4-nitroaniline
-
poor substrate
-
?
Gly-hydroxyproline-4-nitroanilide + H2O
Gly-hydroxyproline + 4-nitroaniline
-
-
-
-
?
Gly-hydroxyproline-4-nitroanilide + H2O
Gly-hydroxyproline + 4-nitroaniline
-
10% of the activity with Gly-Pro-4-nitroanilide
-
?
Gly-L-Pro-4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
-
-
-
-
?
Gly-L-Pro-4-nitroanilide + H2O
Gly-L-Pro + 4-nitroaniline
-
-
-
-
?
Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-L-Pro-7-amido-4-methylcoumarin + H2O
Gly-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Phe-4-nitroanilide + H2O
Gly-Phe + 4-nitroaniline
-
1% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Gly-Pro-2-naphthylamide + H2O
Gly-Pro + 2-naphthylamine
-
L-Gly-Pro-2-naphthylamide
-
-
?
Gly-Pro-2-naphthylamide + H2O
Gly-Pro + 2-naphthylamine
-
-
-
-
?
Gly-Pro-2-naphthylamide + H2O
Gly-Pro + 2-naphthylamine
-
-
-
-
?
Gly-Pro-4-methoxy-2-naphthylamide + H2O
Gly-Pro + 4-methoxy-2-naphthylamine
-
-
-
-
?
Gly-Pro-4-methoxy-2-naphthylamide + H2O
Gly-Pro + 4-methoxy-2-naphthylamine
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-4-methylcoumarin 7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-4-methylcoumaryl-7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-4-methylcoumaryl-7-amide + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
low activity
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro-4-nitroanilide + H2O
Gly-Pro + 4-nitroaniline
-
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-7-amido-4-methylcoumarin + H2O
Gly-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Gly-Pro-Arg-Pro + H2O
?
-
as active as with Gly-Pro-4-nitroanilide
-
-
?
Gly-Pro-Arg-Pro + H2O
?
-
as active as with Gly-Pro-4-nitroanilide
-
-
?
Gly-Pro-p-nitroanilide + H2O
Gly-Pro + p-nitroaniline
-
-
-
-
?
growth hormone-(1-43) fragment + H2O
?
-
cleaves N-terminal dipeptide FP
-
ir
H-Ala-L-Pro-7-amido-4-methylcoumarin + H2O
H-Ala-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
H-Ala-L-Pro-7-amido-4-methylcoumarin + H2O
H-Ala-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
H-Ala-L-Pro-7-amido-4-methylcoumarin + H2O
H-Ala-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
His-Ala-4-nitroanilide + H2O
His-Ala + 4-nitroaniline
-
poor substrate
-
?
His-Pro-4-nitroanilide + H2O
His-Pro + 4-nitroaniline
-
low activity
-
?
Ile-Pro-4-nitroanilide + H2O
Ile-Pro + 4-nitroaniline
-
low activity
-
?
Ile-Pro-Ile + H2O
?
-
34% of the activity with Gly-Pro-4-nitroanilide
-
-
?
L-Ala-L-Ala-L-Ala-L-Ala + H2O
L-Ala-L-Ala
-
-
with traces of Ala3 and Ala after 2.5 h incubation
?
L-Ala-L-Pro-7-amido-4-methylcoumarin + H2O
L-Ala-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-L-Pro-7-amido-4-methylcoumarin + H2O
L-Ala-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-L-Pro-7-amido-4-methylcoumarin + H2O
L-Ala-L-Pro + 7-amino-4-methylcoumarin
-
-
-
?
L-Ala-L-Pro-7-amido-4-methylcoumarin + H2O
L-Ala-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Ala-L-Pro-7-amido-4-methylcoumarin + H2O
L-Ala-L-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
L-Lys-L-Pro-p-nitroanilide + H2O
L-Lys-L-Pro + p-nitroaniline
-
most preferred substrate
-
-
?
L-Val-L-Pro-L-Val-L-Pro-beta-D-arabinofuranosyladenosine + H2O
L-Val-L-Pro-L-Val-L-Pro + beta-D-arabinofuranosyladenosine
-
-
-
-
?
L-Val-L-Pro-L-Val-L-Pro-beta-D-arabinofuranosyladenosine + H2O
L-Val-L-Pro-L-Val-L-Pro + beta-D-arabinofuranosyladenosine
-
-
-
-
?
L-Val-L-Pro-L-Val-L-Pro-beta-D-arabinofuranosylcytosine + H2O
L-Val-L-Pro-L-Val-L-Pro + beta-D-arabinofuranosylcytosine
-
-
-
-
?
L-Val-L-Pro-L-Val-L-Pro-beta-D-arabinofuranosylcytosine + H2O
L-Val-L-Pro-L-Val-L-Pro + beta-D-arabinofuranosylcytosine
-
-
-
-
?
Lys-Ala-4-methylcoumarin 7-amide + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
?
Lys-Ala-4-methylcoumarin 7-amide + H2O
Lys-Ala + 7-amino-4-methylcoumarin
8.7% of the activity with Pro-4-methylcoumarin 7-amide
-
-
?
Lys-Ala-4-methylcoumarin 7-amide + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Ala-4-methylcoumarin 7-amide + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Ala-4-methylcoumarin 7-amide + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Ala-4-nitroanilide + H2O
Lys-Ala + 4-nitroaniline
-
-
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
?
Lys-Ala-7-amido-4-methylcoumarin + H2O
Lys-Ala + 7-amino-4-methylcoumarin
-
-
-
-
?
Lys-Pro-4-methoxy-2-naphthylamide + H2O
Lys-Pro + 4-methoxy-2-naphthylamine
-
-
-
-
?
Lys-Pro-4-methoxy-2-naphthylamide + H2O
Lys-Pro + 4-methoxy-2-naphthylamine
-
-
-
-
?
Lys-Pro-4-methoxy-2-naphthylamide + H2O
Lys-Pro + 4-methoxy-2-naphthylamine
-
-
-
-
?
Lys-Pro-4-nitroanilide + H2O
Lys-Pro + 4-nitroaniline
-
-
-
?
Lys-Pro-4-nitroanilide + H2O
Lys-Pro + 4-nitroaniline
-
65% of the activity with Gly-Pro-4-nitroanilide
-
?
Lys-Pro-4-nitroanilide + H2O
Lys-Pro + 4-nitroaniline
-
48.6% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Lys-Pro-4-nitroanilide + H2O
Lys-Pro + 4-nitroaniline
-
48.6% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Lys-Pro-4-nitroanilide + H2O
Lys-Pro + 4-nitroaniline
51% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Lys-Pro-4-nitroanilide + H2O
Lys-Pro + 4-nitroaniline
-
34% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Lys-Pro-7-amido-4-methylcoumarin + H2O
Lys-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Lys-Pro-7-amido-4-methylcoumarin + H2O
Lys-Pro + 7-amino-4-methylcoumarin
-
best 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
-
?
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
-
-
-
?
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
-
?
Phe-4-nitroanilide + H2O
Phe + 4-nitroaniline
-
7% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Phe-4-nitroanilide + H2O
Phe + 4-nitroaniline
-
7% of the activity with Gly-Pro-4-nitroanilide
-
-
?
Phe-Pro-2-naphthylamide + H2O
Phe-Pro + 2-naphthylamine
-
L-Phe-L-Pro-2-naphthylamide
-
-
?
Phe-Pro-4-methylcoumarin 7-amide + H2O
Phe-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Phe-Pro-4-methylcoumarin 7-amide + H2O
Phe-Pro + 7-amino-4-methylcoumarin
108.6% of the activity with Pro-4-methylcoumarin 7-amide
-
-
?
Phe-Pro-4-methylcoumarin 7-amide + H2O
Phe-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Phe-Pro-4-methylcoumarin 7-amide + H2O
Phe-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
Phe-Pro-4-nitroanilide + H2O
Phe-Pro + 4-nitroaniline
-
low activity
-
?
Phe-Pro-7-amido-4-methylcoumarin + H2O
Phe-Pro + 7-amino-4-methylcoumarin
-
low activity
-
?
Phe-Pro-7-amido-4-methylcoumarin + H2O
Phe-Pro + 7-amino-4-methylcoumarin
-
-
-
-
?
pituitary adenylate cyclase-activating polypeptide-(1-38) + H2O
?
-
i.e. PACAP38, a critical mediator in lipid and carbohydrate metabolism
-
?
pituitary adenylate cyclase-activating polypeptide-(1-38) + H2O
?
-
i.e. PACAP38, enzyme plays a major role in the degradation of circulating PACAP38, cleaves N-terminal dipeptide HS
-
?
Pro-Ala-4-nitroanilide + H2O
Pro-Ala + 4-nitroaniline
-
best substrate
-
?
Pro-Ala-4-nitroanilide + H2O
Pro-Ala + 4-nitroaniline
-
-
-
?
Pro-Pro-4-nitroanilide + H2O
Pro-Pro + 4-nitroaniline
-
high activity
-
?
Pro-Pro-4-nitroanilide + H2O
Pro-Pro + 4-nitroaniline
-
-
-
?
SDF-1/CXCL12 + H2O
?
-
CD26 may play a role in SDF-1/CXCL12 mediated functions such as chemotaxis
-
-
?
SDF-1/CXCL12 + H2O
?
-
CD26 can cleave SDF-1/CXCL12 to a chemotactically-null molecule
-
-
?
SDF-1/CXCL12 + H2O
?
-
CD26 may play a role in SDF-1/CXCL12 mediated functions such as chemotaxis
-
-
?
SDF-1/CXCL12 + H2O
?
-
CD26 can cleave SDF-1/CXCL12 to a chemotactically-null molecule
-
-
?
Ser-Pro-4-nitroanilide + H2O
Ser-Pro + 4-nitroaniline
-
low activity
-
?
substance P + H2O
Arg-Pro + Lys-Pro + ?
-
Arg-Pro-/-Lys-Pro-/-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH2
-
-
?
Tyr-Ala-4-nitroanilide + H2O
Tyr-Ala + 4-nitroaniline
-
poor substrate
-
?
Tyr-Pro-4-nitroanilide + H2O
Tyr-Pro + 4-nitroaniline
-
-
-
?
Val-Pro-4-nitroanilide + H2O
Val-Pro + 4-nitroaniline
-
best substrate
-
?
Val-Pro-Leu + H2O
?
-
83% of the activity with Gly-Pro-4-nitroanilide
-
-
?
additional information
?
-
the enzyme is involved in protein maturation
-
-
?
additional information
?
-
-
the enzyme is involved in protein maturation
-
-
?
additional information
?
-
-
XaaPro dipeptides linked to a free amino group present on an aromatic ring or on a sugar entity are prodrugs that efficiently release the parent drug upon conversion by DPPIV
-
-
?
additional information
?
-
-
the omega gene product is a modifier of larval cuticle protein 5 and its alleles in the third instar of Drosophila melanogaster
-
-
?
additional information
?
-
-
cleaves Gly-Pro from the N-terminal end of the fibrin alpha chain
-
-
?
additional information
?
-
-
broad substrate specificity, structural elements of the substrate protein outside the immediate primary sequence of the cleavage site are crucial
-
?
additional information
?
-
-
enzyme binds adenosine deaminase at the highly glycosylated beta-propeller domain
-
?
additional information
?
-
enzyme binds to adenosine deaminase, EC 3.5.4.4
-
?
additional information
?
-
-
enzyme binds to adenosine deaminase, EC 3.5.4.4
-
?
additional information
?
-
-
substrate specificity, enzyme binds adenosine deaminase
-
?
additional information
?
-
-
substrate specificity, positional scanning combinatorial dipeptide library profile shows that the enzyme is specific for Pro at P1 position and accepts a broad amino acid spectrum at P2 position with isoleucine and norleucine resulting in highest activity, norleucine-norleucine-rhodamine is no substrate, Gly-Ala-7-amido-4-methylcoumarin and Lys-Ala-7-amido-4-methylcoumarin are poor substrates
-
?
additional information
?
-
-
substrate specificty, no activity with glucose-dependent insulinotropic polypeptide(3-42) peptide, [Gly2]glucose-dependent insulinotropic polypeptide(1-6) peptide, and [Val2]glucose-dependent insulinotropic polypeptide(1-6) peptide
-
?
additional information
?
-
the enzyme binds with high affinity to adenosine deaminase, EC 3.5.4.4
-
?
additional information
?
-
-
the enzyme binds with high affinity to adenosine deaminase, EC 3.5.4.4
-
?
additional information
?
-
-
on human T cells the enzyme has been demonstrated to be a functional collagen receptor leading to cell activation. The enzyme may be important in modulation of the biological activity on some of the cytokines, growth factors and neuropeptides. CD/DPP IV plays a role in HIV infection, but the exact mechanism remains to be elucidated
-
-
?
additional information
?
-
-
the enzyme may hinder blood coagulation in intact vessels in vivo, because it is located on the surface of the capillary endothelium
-
-
?
additional information
?
-
-
the enzyme is an important constituent in the process of lymphocyte activation: The inhibition of dipeptidyl peptidase IV results in a supression of DNA synthesis and impairment of B cell differentiation and Ig synthesis of nitrogen-activated human lymphocytes
-
-
?
additional information
?
-
-
the enzyme plays a significant role in the process of activation and proliferation of human thymus-derived lymphocytes
-
-
?
additional information
?
-
-
binding of adenosine deaminase to the T-cell surface protects the T-cell from adenosine-mediated inhibition of proliferation
-
?
additional information
?
-
contributes to the regulation of various physiological processes, including blood sugar homeostasis, by cleaving peptide hormones, chemokines, and neuropeptides
-
?
additional information
?
-
-
contributes to the regulation of various physiological processes, including blood sugar homeostasis, by cleaving peptide hormones, chemokines, and neuropeptides
-
?
additional information
?
-
-
enzyme is implicated in several diseases
-
?
additional information
?
-
-
enzyme is involved in diabetes mellitus, AIDS, and immunoregulatory processes
-
?
additional information
?
-
-
enzyme is involved in glucose metabolism in contributing to the regulation of glucagon family peptides
-
?
additional information
?
-
-
enzyme plays an important role in the activation and proliferation of lymphocytes
-
?
additional information
?
-
-
enzyme plays an important role in the process of activation and proliferation of lymphocytes, inhibition of the enzyme activity results in induction or mediation of diverse cellular processes and effects, such as induction of tyrosine phosphorylations, p38 MAP kinase activation, induction of TGF-beta1 secretion, suppression of DNA synthesis and proliferation, reduced production of various cytokines, and alteration anti-CD3-induced signalling pathways, overview
-
?
additional information
?
-
-
physiological function of enzyme activities with natural substrates, enzyme is involved in immune regulation, altered enzyme activity and expression level, and diverse physiological effects of increased enzyme expression, in cancer cells, overview, disregulation of the enzyme may contribute to cancer development
-
?
additional information
?
-
-
the enzyme is supposed to mediate the immunosuppressive effects of HIV-1 Tat protein, enzyme plays a central role in signal transduction processes
-
?
additional information
?
-
-
dipeptidyl peptidase IV is the major enzyme responsible for degrading the incretins in vivo
-
-
?
additional information
?
-
-
DPP-4 is an important determinant of incretin inactivation
-
-
?
additional information
?
-
homodimeric DPP-IV interacts extracellularly with adenosine deaminase, and this interaction is critical for adenosine signaling and T-cell proliferation
-
-
?
additional information
?
-
-
kinetic characteristics of SADA (the catalytic subunit of adenosine deaminase), are modulated by the interaction with DPPIV-CD26 in favour of neutralization of toxic nucleosides (especially 2´-dAdo) in the extracellular medium
-
-
?
additional information
?
-
-
no endopeptidase or tripeptidase activity is detected for DPP9, tested against Z-Gly-L-Pro-p-nitroanilide, L-Ala-L-Ala-L-Ala-p-nitroanilide, and L-Ala-L-Ala-L-Pro-p-nitroanilide
-
-
?
additional information
?
-
-
DPP-IV typically cleaves Xaa-Pro or Xaa-Ala dipeptides from the N-terminus of peptides
-
-
?
additional information
?
-
-
XaaPro dipeptides linked to a free amino group present on an aromatic ring or on a sugar entity are prodrugs that efficiently release the parent drug upon conversion by DPPIV
-
-
?
additional information
?
-
-
the substrate specificity of DPP IV is not that strict and cleavage after the penultimate Ser, Gly, Thr, Val, and Leu has also been observed
-
-
?
additional information
?
-
-
substrate specificity study, no activity with bradykinin, Pro-7-amido-4-methylcoumarin, benzyloxycarbonyl-Gly-Pro-7-amido-4-methylcoumarin, and benzyloxycarbonyl-Phe-Ala-7-amido-4-methylcoumarin
-
?
additional information
?
-
-
possible role of the enzyme seems to match the high Pro content of beta-casein
-
-
?
additional information
?
-
-
possible role of the enzyme seems to match the high Pro content of beta-casein
-
-
?
additional information
?
-
-
possible role of the enzyme seems to match the high Pro content of beta-casein
-
-
?
additional information
?
-
-
use of fluorogenic rhodamine 110 (R110)-based substrates for the sensitive detection of DP IV on the surface of T cells
-
-
?
additional information
?
-
-
broad substrate specificity, structural elements of the substrate protein outside the immediate primary sequence of the cleavage site are crucial
-
?
additional information
?
-
-
enzyme has several purposes, e.g. as signaling molecule and adenosine deaminase binding protein, enzyme is involved in development of diverse diseases, overview
-
?
additional information
?
-
-
the enzyme may be involved in the initial phase of fibronectin-mediated cell spreading on collagen
-
-
?
additional information
?
-
-
specifically recognized immobilized gelatin and type I collagen
-
-
?
additional information
?
-
-
Ser624, Asp702, and His734 form the catalytic triad
-
-
?
additional information
?
-
-
enzyme binds to CD45 and to adenosine deaminase
-
?
additional information
?
-
-
may play a role in cell attachment to collagen
-
-
?
additional information
?
-
-
enzyme is important for metabolic regulation
-
?
additional information
?
-
-
substrate specificity, cleavage of N-terminal dipeptide, no activity with vasoactive intestinal peptide, glucagon and secretin are poor substrates
-
?
additional information
?
-
-
DPP-IV influences pain perception via modulation of the peripheral concentration of substance P
-
-
?
additional information
?
-
-
CD26/DP IV is a nonredundant inhibitory receptor controlling T cell activation and Th1-mediated autoimmunity
-
-
?
additional information
?
-
-
DPP-4 plays a role in the control of immune function, inflammatory responses, and behavior
-
-
?
additional information
?
-
the enzyme does not bind to adenosine deaminase, EC 3.5.4.4
-
?
additional information
?
-
-
the enzyme does not bind to adenosine deaminase, EC 3.5.4.4
-
?
additional information
?
-
-
peptides with proline penultimate to the amino terminus are more favored substrates while those substrates having Leu at both the penultimate position and amino terminus Leu-Leu
-
-
?
additional information
?
-
-
LVV-hemorphin-7 and LVV-hemorphin-6 are no substrates for the enzyme
-
?
additional information
?
-
-
obligatory role of the enzyme in renal handling of proline- and hydroxyproline-containing peptides
-
-
?
additional information
?
-
-
binding of dipeptidyl peptidase IV to fibronectin may play a role in interaction of hepatocytes with extracellular matrix in vivo and possibly in matrix assembly
-
-
?
additional information
?
-
-
enzyme is important for metabolic regulation
-
?
additional information
?
-
-
hemorphins may represent endogenous regulators of the enzyme activity
-
?
additional information
?
-
-
DPP-4 plays a role in the control of immune function, inflammatory responses, and behavior
-
-
?
additional information
?
-
-
activity in glucose-containing medium remains constant during exponential growth and increases less than twofold when cells reach the stationary phase. Growth of yeast on poor nitrogen source or under nitrogen starvation results in a three- or fourfold increase in the level of the enzyme
-
-
?
additional information
?
-
-
no hydrolysis of Ala-Ala-Pro-4-nitroanilide, Ala-Phe-Pro-4-nitroanilide, Pro-4-nitroanilide, Leu-4-nitroanilide, Arg, 4-nitroanilide, Ala-Ala-Ala-4-nitroanilide
-
-
?
additional information
?
-
-
specifically hydrolyzes N-terminal X-Pro from X-Pro-4-nitroanilides
-
-
?
additional information
?
-
-
specifically hydrolyzes N-terminal X-Pro from X-Pro-4-nitroanilides
-
-
?
additional information
?
-
-
dipeptidyl peptidase IV is a serine protease that cleaves X-Pro/Ala dipeptide from the N-terminus of proteins
-
-
?
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
?
-
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
?
-
-
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
-
?
