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(GLP1)-degrading enzyme
-
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/dipeptidyl peptidase
-
-
dipeptidyl aminopeptidase IV
dipeptidyl dipeptidase IV
-
-
dipeptidyl peptidase 8
-
-
dipeptidyl peptidase 9
-
-
dipeptidyl-aminopeptidase IV
-
-
-
-
dipeptidyl-peptidase IV (CD26)
-
-
-
-
dipeptidyl-peptide hydrolase
-
-
-
-
dipeptidylpeptidase IV/CD26
dipeptidylpeptidase-IV
-
-
DPP8
-
DPP8 is a prolyl dipeptidases, cleaving the peptide bond after the penultimate proline residue
DPP9
-
DPP9 is a prolyl dipeptidases, cleaving the peptide bond after the penultimate proline residue
glucagon-like peptide 1-degrading enzyme
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Gly-Pro-naphthylamidase
-
-
-
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glycoprotein GP110
-
-
-
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glycylproline aminopeptidase
-
-
-
-
glycylproline-dipeptidyl-aminopeptidase
-
-
-
-
glycylprolyl aminopeptidase
-
-
-
-
glycylprolyl dipeptidylaminopeptidase
-
-
-
-
GP110 glycoprotein
-
-
-
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leukocyte antigen CD26
-
-
-
-
lymphocyte, antigen CD26
-
-
-
-
omega gene product
-
one of five putative DPP IV genes
peptidase, dipeptidyl, IV
-
-
-
-
postproline dipeptidyl aminopeptidase IV
-
-
-
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prolyl-dipeptidyl-aminopeptidase
-
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sipeptidyl peptidase IV
-
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T cell triggering molecule Tp103
-
-
-
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T-cell activation antigen CD26
-
-
-
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Thymocyte-activating molecule
-
-
-
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type IV dipeptidyl aminopeptidase
-
X-prolyl dipeptidyl aminopeptidase
X-prolyl-dipeptidyl aminopeptidase
-
-
Xaa-Pro-dipeptidyl-aminopeptidase
-
-
-
-
ADABP
-
-
-
-
adenosine deaminase binding protein
-
-
adenosine deaminase binding protein
-
CD26
-
-
CD26
-
-
649200, 649276, 649284, 649286, 651150, 651533, 653810, 653811, 665212, 667032, 677572, 682869, 697297, 697519, 697526, 699329, 699938, 702623, 702941, 703039, 703263, 703552, 704834, 705071, 705754, 706453
CD26
enzyme is identical with adenosine deaminase binding protein, CD26
CD26
dipeptidyl-peptidase IV is identical with the adenosine deaminase binding protein CD26 on lymphocytes
DAP IV
-
dipeptidyl aminopeptidase IV
-
-
-
-
dipeptidyl aminopeptidase IV
-
-
dipeptidyl aminopeptidase IV
-
-
dipeptidyl aminopeptidase IV
-
dipeptidyl peptidase 4
-
-
dipeptidyl peptidase 4
-
-
dipeptidyl peptidase 4
-
-
dipeptidyl peptidase IV
-
-
dipeptidyl peptidase IV
-
-
dipeptidyl peptidase IV
-
-
dipeptidyl peptidase IV
-
-
dipeptidyl peptidase IV
-
-
dipeptidyl peptidase IV
-
-
649200, 649276, 649278, 649281, 649283, 649284, 649285, 649615, 649748, 650930, 651150, 651533, 653810, 653811, 667032, 677291, 677572, 678597, 678622, 678629, 678634, 678642, 678659, 678686, 678691, 679409, 679410, 679635, 680101, 681068, 681080, 681247, 696621, 696624, 697297, 697489, 697526, 698335, 699329, 699445, 699976, 702583, 702611, 702623, 702941, 703039, 703389, 703552, 703784, 704834, 704968, 705071, 705305, 705754, 706453
dipeptidyl peptidase IV
-
649229, 651079, 653298, 653913, 678611, 678650, 678653, 678662, 678700, 679651, 681303, 681506, 696651, 696670, 696912, 703678, 704844, 705230
dipeptidyl peptidase IV
-
-
dipeptidyl peptidase IV
-
-
dipeptidyl peptidase IV
-
-
dipeptidyl peptidase IV
-
-
dipeptidyl peptidase IV
-
-
dipeptidyl peptidase IV
-
-
650432, 650930, 651514, 678597, 678611, 678634, 678689, 679299, 680337, 681305, 681325, 681575, 681582, 696621, 696668, 696746, 699329, 699445, 700398, 702514, 702578, 702585, 702623, 702985, 703377, 703569, 704840, 706014
dipeptidyl peptidase IV
-
dipeptidyl peptidase IV
-
-
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dipeptidyl peptidase IV
-
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dipeptidyl peptidase IV
-
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dipeptidyl peptidase IV
-
-
dipeptidyl peptidase IV
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dipeptidyl peptidase-4
-
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dipeptidyl peptidase-4
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-
dipeptidyl peptidase-4
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679305, 679395, 679437, 679443, 679444, 679451, 679452, 680074, 681066, 681081, 681082, 681578, 697436, 697550, 697764, 697832, 701371
dipeptidyl peptidase-4
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dipeptidyl peptidase-4
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dipeptidyl peptidase-4
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dipeptidyl peptidase-IV
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dipeptidyl peptidase-IV
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679369, 679397, 679450, 679663, 695514, 696134, 697519, 697522, 697551, 698213, 699174, 699938, 700399
dipeptidyl peptidase-IV
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dipeptidyl peptidase-IV
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dipeptidyl peptidase-IV
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-
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dipeptidyl peptidase-IV
-
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dipeptidyl peptidase-IV
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dipeptidyl-peptidase 4
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dipeptidyl-peptidase 4
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dipeptidylpeptidase IV
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dipeptidylpeptidase IV
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dipeptidylpeptidase IV
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dipeptidylpeptidase IV
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dipeptidylpeptidase IV/CD26
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dipeptidylpeptidase IV/CD26
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DP IV
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DP-IV
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DPIV
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DPP IV
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DPP IV
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DPP IV has the preference for X-Pro over X-Ala, where X is any amino acid other than L-proline
DPP-4
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DPP-4
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677582, 677897, 678652, 678664, 678679, 678691, 679305, 679369, 679370, 679395, 679410, 679437, 679445, 679447, 679478, 679479, 679480, 679635, 679709, 680074, 680224, 680234, 696621, 696624, 697436, 697526, 697764, 697832, 698335, 699174, 699745, 699748, 701371, 702583, 705305
DPP-4
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678666, 678682, 678689, 678702, 679445, 679447, 679454, 681305, 681319, 696621, 697764, 699745, 699748, 702578
DPP-IV
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DPP-IV
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649200, 649286, 649626, 649748, 651533, 664847, 677326, 677580, 678597, 678617, 678622, 678629, 678658, 678659, 678967, 679397, 679409, 679411, 679450, 679650, 681283, 681573, 695514, 696134, 697297, 697519, 697522, 697526, 697551, 698213, 699445, 700399, 702611, 702623, 703552, 703784, 705754
DPP-IV
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653298, 653913, 678195, 678611, 678650, 678694, 681294, 696651, 696912, 705230, 753766
DPP-IV
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663815, 681506, 681575, 696134, 697556, 697561, 699445, 699753, 699944, 699985, 700399, 700400, 700615, 702894
DPP-IV
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-
664847, 678597, 678611, 678617, 678646, 678658, 678694, 681294, 681575, 696134, 696668, 696746, 699445, 700398, 702623, 703377, 703569
DPP4
-
-
DPPIV
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DPPIV
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649615, 653810, 653811, 667032, 677291, 678675, 680101, 681297, 699329, 699976, 701430, 702941, 703039, 704834, 704968, 705071, 706453
h-DPPIV
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X-PDAP
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X-prolyl dipeptidyl aminopeptidase
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X-prolyl dipeptidyl aminopeptidase
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additional information
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enzyme belongs to the group of dipeptidylpeptidase-IV activity and/or structure homologues, i.e. DASH
additional information
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enzyme belongs to the group of dipeptidylpeptidase-IV activity and/or structure homologues, i.e. DASH
additional information
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enzyme belongs to the prolyl oligopeptidase POP family
additional information
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enzyme belongs to the protease clan SC
additional information
the enzyme is not identical with attractin
additional information
enzyme belongs to the SC clan that includes 38 families of peptidases, and is the prototype of the S15 family
additional information
-
enzyme belongs to the protease clan SC
additional information
-
enzyme belongs to the protease clan SC
additional information
-
enzyme belongs to the protease clan SC
additional information
-
enzyme belongs to the protease clan SC
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
-
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
reaction mechanism
-
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
active site structure and accessibility
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
active site structure modeling and reaction mechanism
-
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
active site structure, containing the catalytic triad Ser630, Asp708, and His740, is located in a large cavity at the interface of the 2 domains, substrate binding and catalytic mechanism, serine exopeptidase
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
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
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
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
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
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
conserved residues Ser624, Asp702, and His734 form a catalytic triad and are involved in the catalytic reaction, Ser593 is likely to be the catalytic serine of the serine protease
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 a serine protease, catalytic and substrate binding mechanism, active site structure, catalytic triad Ser630, Asp708, His740
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
enzyme prefers Ala in P1 position, reduced activity is observed with Ser, Gly, or Val at the P1 position, modeling of reaction mechanism and substrate binding at the catalytic site
-
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
exopeptidase that cleaves dipeptides from the N-terminus of oligo- and polypeptides with the penultimate residue being proline or alanine
-
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
prefers Pro or Ala at position P1, substrate recognition involves the negatively charged active site residues E205 and E206, reaction mechanism, active site structure and substrate binding
-
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
-
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
-
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
serine protease
-
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
serine protease
-
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
serine protease, catalytic triad Ser630, Asp708, His740, active site architecture
-
release of an N-terminal dipeptide, Xaa-Yaa-/-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline
specific for hydrolysis of peptide bond on the carboxylic side of proline residues which are penultimate from the amino terminus
-
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(Ala-Pro)2-rhodamine R110 + H2O
Ala-Pro + rhodamine R110
-
-
-
?
4-(glycyl-L-prolyl hydrazido)-N-hexyl-1,8-naphthalimide + H2O
?
-
-
-
-
?
Ala-4-nitroanilide + H2O
Ala + 4-nitroaniline
Ala-Ala-2-naphthylamide + H2O
Ala-Ala + 2-naphthylamine
Ala-Ala-4-nitroanilide + H2O
Ala-Ala + 4-nitroaniline
Ala-Ala-Ala + H2O
Ala-Ala + Ala
Ala-Ala-Ala-Ala-Ala + H2O
Ala-Ala + Ala-Ala-Ala
-
-
with traces of Ala4 and Ala after 2.5 h incubation
?
Ala-Ala-Pro-4-nitroanilide + H2O
?
-
-
-
-
?
Ala-Pro-4-nitroanilide + H2O
Ala-Pro + 4-nitroaniline
Ala-Pro-7-amido-4-methylcoumarin + H2O
Ala-Pro + 7-amino-4-methylcoumarin
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
-
-
-
-
?
Ala-Pro-Gly + H2O
Ala-Pro + Gly
Ala-Pro-p-nitroanilide + H2O
Ala-Pro + p-nitroaniline
-
-
-
-
?
alpha1-microglobulin + H2O
?
-
-
-
-
?
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
-
?
aprotinin + H2O
?
-
-
-
-
?
Arg-4-nitroanilide + H2O
Arg + 4-nitroaniline
Arg-Pro-4-nitroanilide + H2O
Arg-Pro + 4-nitroaniline
Arg-Pro-7-amido-4-methylcoumarin + H2O
Arg-Pro + 7-amino-4-methylcoumarin
-
high activity
-
?
Arg-Pro-Lys-Pro + H2O
?
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe + H2O
?
-
-
-
-
?
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 + H2O
?
-
-
-
-
?
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
-
-
-
-
?
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Met-NH3 + H2O
?
-
-
-
-
?
Arg-Pro-Pro + H2O
?
-
-
-
-
?
Asn-Pro-4-nitroanilide + H2O
Asn-Pro + 4-nitroaniline
Asn-Pro-7-amido-4-methylcoumarin + H2O
Asn-Pro + 7-amino-4-methylcoumarin
-
-
-
?
Asp-Pro-4-nitroanilide + H2O
Asp-Pro + 4-nitroaniline
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 + ?
-
-
-
?
benzyloxycarbonyl-Gly-Pro-Leu-Gly-Pro + H2O
Leu-Gly-Pro + ?
-
-
-
?
beta-casomorphin + H2O
fragments
-
cleavage sites: YP-/-FP-/-GP-/-IGP-/-RP
-
?
beta-endorphin + H2O
?
-
-
-
?
bradykinin + H2O
?
-
-
-
-
?
BRI peptide (1-23) + H2O
?
-
-
-
-
?
casomorphin + H2O
?
-
-
-
-
?
CCL11 + H2O
CCL11(3-74) + ?
chemokines + H2O
?
-
-
-
?
corticotropin-like intermediate lobe peptide + H2O
?
-
-
-
-
?
CXCL 11 + H2O
?
-
chemokine bound to receptor on T cell surface
-
?
des-Pro2-bradykinin + H2O
fragments
-
cleavage sites: RP-/-GFSPFR
-
?
eotaxin + H2O
?
-
i.e. CCL11, chemokine
-
?
EPLGRQLTSGP + H2O
Glu-Pro + LGRQLTSGP
-
the sequence EPLGRQLTSGP, which corresponds to the propeptide fragment of alpha-2 plasmin inhibitor
-
-
?
gastric inhibitory polypeptide + H2O
?
3.4.14.5 dipeptidyl-peptidase IV
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