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Literature summary extracted from
- Prolyl peptidases: a serine protease subfamily with high potential for drug discovery (2003), Curr. Opin. Chem. Biol., 7, 496-504.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.4.14.5 | medicine | specific inhibition of the enzyme shows efficacy in the treatment of type 2 diabetes | Mus musculus |
| 3.4.14.5 | medicine | specific inhibition of the enzyme shows efficacy in the treatment of type 2 diabetes | Homo sapiens |
| 3.4.14.5 | medicine | specific inhibition of the enzyme shows efficacy in the treatment of type 2 diabetes | Rattus norvegicus |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.14.5 | - |
Homo sapiens |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.14.5 | enzyme forms tetramers in crystals, which may depend on native glycosylation | Sus scrofa |
| 3.4.14.5 | recombinant enzyme forms dimers in crystals | Homo sapiens |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.14.5 | additional information | knock-out mutant shows residual activity with Gly-Pro-4-nitroanilide in plasma, but not with GLP-1, mutant mice are healthy | Mus musculus |
| 3.4.14.5 | additional information | mutant strain harboring a mutation which leads to rapid degradation of the enzyme | Rattus norvegicus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.14.5 | isoleucine thiazolidide | in vivo study | Rattus norvegicus |  |
| 3.4.14.5 | Lys-pyrrolidide | - |
Homo sapiens | |
| 3.4.14.5 | Lys-pyrrolidide | - |
Mammalia | |
| 3.4.14.5 | Lys-pyrrolidide | - |
Sus scrofa | |
| 3.4.14.5 | NVP DPP728 | in vivo study | Mus musculus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.14.5 | additional information | - |
additional information | kinetics are highly variable with protein substrates | Mammalia |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.14.5 | cytosol | - |
Mammalia | 5829 | - |
| 3.4.14.5 | extracellular | on cell surface | Mus musculus | - |
- |
| 3.4.14.5 | extracellular | on the cell surface | Mammalia | - |
- |
| 3.4.14.5 | membrane | - |
Mammalia | 16020 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.14.5 | chemokines + H2O | Mammalia | - |
? | - |
? | |
| 3.4.14.5 | additional information | Mammalia | enzyme has several purposes, e.g. as signaling molecule and adenosine deaminase binding protein, enzyme is involved in development of diverse diseases, overview | ? | - |
? | |
| 3.4.14.5 | additional information | Mus musculus | enzyme is important for metabolic regulation | ? | - |
? | |
| 3.4.14.5 | additional information | Rattus norvegicus | enzyme is important for metabolic regulation | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.14.5 | Homo sapiens | - |
- |
- |
| 3.4.14.5 | Mammalia | - |
- |
- |
| 3.4.14.5 | Mus musculus | - |
- |
- |
| 3.4.14.5 | Rattus norvegicus | - |
- |
- |
| 3.4.14.5 | Sus scrofa | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.14.5 | glycoprotein | glycosylation is a prerquisite for tetramer formation | Sus scrofa |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.4.14.5 | 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 | Mammalia | |
| 3.4.14.5 | 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 | Mus musculus | |
| 3.4.14.5 | 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 | Homo sapiens | |
| 3.4.14.5 | 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 | Rattus norvegicus | |
| 3.4.14.5 | 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 | Sus scrofa |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.14.5 | plasma | - |
Mammalia | - |
| 3.4.14.5 | T-cell | - |
Mammalia | - |
| 3.4.14.5 | T-cell | cell surface | Mus musculus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.14.5 | chemokines + H2O | - |
Mammalia | ? | - |
? | |
| 3.4.14.5 | CXCL 11 + H2O | chemokine bound to receptor on T cell surface | Mammalia | ? | - |
? | |
| 3.4.14.5 | GLP-1 + H2O | an incretin involved in the glucose-dependent production of insulin | Mus musculus | ? | - |
? | |
| 3.4.14.5 | Gly-Pro-4-nitroanilide + H2O | - |
Mus musculus | Gly-Pro + 4-nitroaniline | - |
? | |
| 3.4.14.5 | incretins + H2O | - |
Mammalia | ? | - |
? | |
| 3.4.14.5 | additional information | broad substrate specificity, structural elements of the substrate protein outside the immediate primary sequence of the cleavage site are crucial | Mammalia | ? | - |
? | |
| 3.4.14.5 | additional information | broad substrate specificity, structural elements of the substrate protein outside the immediate primary sequence of the cleavage site are crucial | Homo sapiens | ? | - |
? | |
| 3.4.14.5 | additional information | broad substrate specificity, structural elements of the substrate protein outside the immediate primary sequence of the cleavage site are crucial | Sus scrofa | ? | - |
? | |
| 3.4.14.5 | additional information | enzyme binds to CD45 and to adenosine deaminase | Mus musculus | ? | - |
? | |
| 3.4.14.5 | 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 | Mammalia | ? | - |
? | |
| 3.4.14.5 | additional information | enzyme is important for metabolic regulation | Mus musculus | ? | - |
? | |
| 3.4.14.5 | additional information | enzyme is important for metabolic regulation | Rattus norvegicus | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.14.5 | tetramer | may be important for adhesion of the enzyme to cells | Sus scrofa |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.14.5 | dipeptidyl peptidase IV | - |
Mammalia |
| 3.4.14.5 | dipeptidyl peptidase IV | - |
Mus musculus |
| 3.4.14.5 | dipeptidyl peptidase IV | - |
Homo sapiens |
| 3.4.14.5 | dipeptidyl peptidase IV | - |
Rattus norvegicus |
| 3.4.14.5 | dipeptidyl peptidase IV | - |
Sus scrofa |
| 3.4.14.5 | DPP IV | - |
Mammalia |
| 3.4.14.5 | DPP IV | - |
Mus musculus |
| 3.4.14.5 | DPP IV | - |
Homo sapiens |
| 3.4.14.5 | DPP IV | - |
Rattus norvegicus |
| 3.4.14.5 | DPP IV | - |
Sus scrofa |
| 3.4.14.5 | More | enzyme belongs to the protease clan SC | Mammalia |
| 3.4.14.5 | More | enzyme belongs to the protease clan SC | Mus musculus |
| 3.4.14.5 | More | enzyme belongs to the protease clan SC | Homo sapiens |
| 3.4.14.5 | More | enzyme belongs to the protease clan SC | Rattus norvegicus |
| 3.4.14.5 | More | enzyme belongs to the protease clan SC | Sus scrofa |
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Release 2023.1 (January 2023)
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