Any feedback?
Literature summary for 3.4.14.5 extracted from
- Prolyl peptidases: a serine protease subfamily with high potential for drug discovery (2003), Curr. Opin. Chem. Biol., 7, 496-504.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | specific inhibition of the enzyme shows efficacy in the treatment of type 2 diabetes | Mus musculus |
| medicine | specific inhibition of the enzyme shows efficacy in the treatment of type 2 diabetes | Homo sapiens |
| medicine | specific inhibition of the enzyme shows efficacy in the treatment of type 2 diabetes | Rattus norvegicus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
- |
Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| enzyme forms tetramers in crystals, which may depend on native glycosylation | Sus scrofa |
| recombinant enzyme forms dimers in crystals | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| 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 |
| additional information | mutant strain harboring a mutation which leads to rapid degradation of the enzyme | Rattus norvegicus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| isoleucine thiazolidide | in vivo study | Rattus norvegicus |  |
| Lys-pyrrolidide | - |
Homo sapiens | |
| Lys-pyrrolidide | - |
Mammalia | |
| Lys-pyrrolidide | - |
Sus scrofa | |
| NVP DPP728 | in vivo study | Mus musculus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | kinetics are highly variable with protein substrates | Mammalia |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Mammalia | 5829 | - |
| extracellular | on cell surface | Mus musculus | - |
- |
| extracellular | on the cell surface | Mammalia | - |
- |
| membrane | - |
Mammalia | 16020 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| chemokines + H2O | Mammalia | - |
? | - |
? | |
| 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 | ? | - |
? | |
| additional information | Mus musculus | enzyme is important for metabolic regulation | ? | - |
? | |
| additional information | Rattus norvegicus | enzyme is important for metabolic regulation | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
| Mammalia | - |
- |
- |
| Mus musculus | - |
- |
- |
| Rattus norvegicus | - |
- |
- |
| Sus scrofa | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | glycosylation is a prerquisite for tetramer formation | Sus scrofa |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| 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 | |
| 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 | |
| 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 | |
| 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 | |
| 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
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| plasma | - |
Mammalia | - |
| T-cell | - |
Mammalia | - |
| T-cell | cell surface | Mus musculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| chemokines + H2O | - |
Mammalia | ? | - |
? | |
| CXCL 11 + H2O | chemokine bound to receptor on T cell surface | Mammalia | ? | - |
? | |
| GLP-1 + H2O | an incretin involved in the glucose-dependent production of insulin | Mus musculus | ? | - |
? | |
| Gly-Pro-4-nitroanilide + H2O | - |
Mus musculus | Gly-Pro + 4-nitroaniline | - |
? | |
| incretins + H2O | - |
Mammalia | ? | - |
? | |
| additional information | broad substrate specificity, structural elements of the substrate protein outside the immediate primary sequence of the cleavage site are crucial | Mammalia | ? | - |
? | |
| additional information | broad substrate specificity, structural elements of the substrate protein outside the immediate primary sequence of the cleavage site are crucial | Homo sapiens | ? | - |
? | |
| additional information | broad substrate specificity, structural elements of the substrate protein outside the immediate primary sequence of the cleavage site are crucial | Sus scrofa | ? | - |
? | |
| additional information | enzyme binds to CD45 and to adenosine deaminase | Mus musculus | ? | - |
? | |
| 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 | ? | - |
? | |
| additional information | enzyme is important for metabolic regulation | Mus musculus | ? | - |
? | |
| additional information | enzyme is important for metabolic regulation | Rattus norvegicus | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| tetramer | may be important for adhesion of the enzyme to cells | Sus scrofa |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dipeptidyl peptidase IV | - |
Mammalia |
| dipeptidyl peptidase IV | - |
Mus musculus |
| dipeptidyl peptidase IV | - |
Homo sapiens |
| dipeptidyl peptidase IV | - |
Rattus norvegicus |
| dipeptidyl peptidase IV | - |
Sus scrofa |
| DPP IV | - |
Mammalia |
| DPP IV | - |
Mus musculus |
| DPP IV | - |
Homo sapiens |
| DPP IV | - |
Rattus norvegicus |
| DPP IV | - |
Sus scrofa |
| More | enzyme belongs to the protease clan SC | Mammalia |
| More | enzyme belongs to the protease clan SC | Mus musculus |
| More | enzyme belongs to the protease clan SC | Homo sapiens |
| More | enzyme belongs to the protease clan SC | Rattus norvegicus |
| More | enzyme belongs to the protease clan SC | Sus scrofa |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
