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Literature summary extracted from
- Structure-function properties of prolyl oligopeptidase family enzymes (2006), Cell Biochem. Biophys., 44, 349-365.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.21.26 | enzyme in open conformation | Novosphingobium capsulatum |
| 3.4.21.26 | enzyme with bound inhibitor | Myxococcus xanthus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.26 | benzyloxycarbonyl-proline-prolinal | specific inhibition | Homo sapiens |  |
| 3.4.21.26 | benzyloxycarbonyl-proline-prolinal | specific inhibition | Myxococcus xanthus | |
| 3.4.21.26 | benzyloxycarbonyl-proline-prolinal | specific inhibition | Novosphingobium capsulatum | |
| 3.4.21.26 | benzyloxycarbonyl-proline-prolinal | specific inhibition | Pyrococcus furiosus | |
| 3.4.21.26 | benzyloxycarbonyl-proline-prolinal | specific inhibition | Trypanosoma cruzi | |
| 3.4.21.26 | fluoxetine | an antidepressant | Homo sapiens | |
| 3.4.21.26 | additional information | inhibitor binding structure | Myxococcus xanthus | |
| 3.4.21.26 | Valproic acid | an antimanic drug | Homo sapiens | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.21.26 | extracellular | secreted enzyme | Trypanosoma cruzi | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.26 | Collagen + H2O | Trypanosoma cruzi | the pathogen POP degrades host collagen and fibronectin, facilitating cell invasion, selective inhibitors for trypanosome POP block parasite entry into cells | ? | - |
? | |
| 3.4.21.26 | Fibronectin + H2O | Trypanosoma cruzi | the pathogen POP degrades host collagen and fibronectin, facilitating cell invasion, selective inhibitors for trypanosome POP block parasite entry into cells | ? | - |
? | |
| 3.4.21.26 | additional information | Homo sapiens | POP activity levels are lowered in different stages of depression, whereas activity is increased in patients with mania and schizophrenia, the antidepressant fluoxetine and the antimanic drug valproic acid both restore POP activity to normal levels | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.26 | Homo sapiens | - |
- |
- |
| 3.4.21.26 | Myxococcus xanthus | - |
- |
- |
| 3.4.21.26 | Novosphingobium capsulatum | Q9ZNM8 | - |
- |
| 3.4.21.26 | Pyrococcus furiosus | - |
- |
- |
| 3.4.21.26 | Trypanosoma cruzi | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview | Homo sapiens | |
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview | Pyrococcus furiosus | |
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview | Trypanosoma cruzi | |
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview | Myxococcus xanthus | |
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | catalytic mechanism, structure-function relationship, the enzyme contains a Ser-Asp-His catalytic triad, substrate specificity and binding structure,overview | Novosphingobium capsulatum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.26 | Collagen + H2O | the pathogen POP degrades host collagen and fibronectin, facilitating cell invasion, selective inhibitors for trypanosome POP block parasite entry into cells | Trypanosoma cruzi | ? | - |
? | |
| 3.4.21.26 | Collagen + H2O | host-derived substrate | Trypanosoma cruzi | ? | - |
? | |
| 3.4.21.26 | Fibronectin + H2O | the pathogen POP degrades host collagen and fibronectin, facilitating cell invasion, selective inhibitors for trypanosome POP block parasite entry into cells | Trypanosoma cruzi | ? | - |
? | |
| 3.4.21.26 | Fibronectin + H2O | host-derived substrate | Trypanosoma cruzi | ? | - |
? | |
| 3.4.21.26 | additional information | POP activity levels are lowered in different stages of depression, whereas activity is increased in patients with mania and schizophrenia, the antidepressant fluoxetine and the antimanic drug valproic acid both restore POP activity to normal levels | Homo sapiens | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, and hydrolyse several peptide hormones and neuropeptides in vitro | Homo sapiens | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, substrate entry into the active site cavity, substrate-binding structure and mechanism, general acid/base catalysis is the rate-limiting step, overview | Pyrococcus furiosus | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, substrate entry into the active site cavity, substrate-binding structure and mechanism, overview | Trypanosoma cruzi | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, substrate entry into the active site cavity, substrate-binding structure and mechanism, overview | Myxococcus xanthus | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme cleaves the peptide bond on the C-terminal side of proline in peptides up to approx 30 residues, substrate entry into the active site cavity, substrate-binding structure and mechanism, the loops connecting the peptidase and propeller domains act like a hinge, holding the structure together as the domains move apart, creating a large opening, overview | Novosphingobium capsulatum | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.26 | More | the enzyme is a member of the prolyl oligopeptidase family, subfamily S9a | Homo sapiens |
| 3.4.21.26 | More | the enzyme is a member of the prolyl oligopeptidase family, subfamily S9a | Pyrococcus furiosus |
| 3.4.21.26 | More | the enzyme is a member of the prolyl oligopeptidase family, subfamily S9a | Trypanosoma cruzi |
| 3.4.21.26 | More | the enzyme is a member of the prolyl oligopeptidase family, subfamily S9a | Myxococcus xanthus |
| 3.4.21.26 | More | the enzyme is a member of the prolyl oligopeptidase family, subfamily S9a | Novosphingobium capsulatum |
| 3.4.21.26 | POP | - |
Homo sapiens |
| 3.4.21.26 | POP | - |
Pyrococcus furiosus |
| 3.4.21.26 | POP | - |
Trypanosoma cruzi |
| 3.4.21.26 | POP | - |
Myxococcus xanthus |
| 3.4.21.26 | POP | - |
Novosphingobium capsulatum |
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