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Literature summary extracted from
- Prolyl endopeptidases (2007), Cell. Mol. Life Sci., 64, 345-355.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.4.21.26 | drug development | the enzyme is a pharmacological target for neurological diseases due to its high brain concentration and ability to cleave neuropeptides in vitro | Homo sapiens |
| 3.4.21.26 | pharmacology | microbial PEPs are studied as potential therapeutics for celiac sprue, an inflammatory disease of the small intestine triggered by proline-rich gluten | Pyrococcus furiosus |
| 3.4.21.26 | pharmacology | microbial PEPs are studied as potential therapeutics for celiac sprue, an inflammatory disease of the small intestine triggered by proline-rich gluten | Myxococcus xanthus |
| 3.4.21.26 | pharmacology | microbial PEPs are studied as potential therapeutics for celiac sprue, an inflammatory disease of the small intestine triggered by proline-rich gluten | Elizabethkingia meningoseptica |
| 3.4.21.26 | pharmacology | microbial PEPs are studied as potential therapeutics for celiac sprue, an inflammatory disease of the small intestine triggered by proline-rich gluten | Novosphingobium capsulatum |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.21.26 | individual expression of isolated peptidase domain and catalytic domain | Sus scrofa |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.21.26 | additional information | by using directed evolution techniques, the thermostability of the enzyme from Flavobacterium meningosepticum is improved by 1200fold, measured at 60°C, the thermostable enzyme contains 12 individual mutations, many of which are located near the N and C termini of the enzyme | Elizabethkingia meningoseptica |
| 3.4.21.26 | additional information | kinetic analysis of selected enzyme mutants | Myxococcus xanthus |
| 3.4.21.26 | additional information | knockout mutation reverses the effect of the drugs, the mutants show elevated levels of multiple inositol polyphosphate phosphatase, MIPP, activity | Dictyostelium discoideum |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.4.21.26 | the enzyme is quite stable to the pancreatic enzymes, trypsin, chymotrypsin, elastase, and carboxypeptidase A at pH 6.5 and 37°C for 60 min retaining more than 60% of its activity | Elizabethkingia meningoseptica |
| 3.4.21.26 | the enzyme is quite stable to the pancreatic enzymes, trypsin, chymotrypsin, elastase, and carboxypeptidase A, at upt to 3 mg/ml, at pH 6.5 and 37°C for 60 min retaining more than 60% of its activity | Myxococcus xanthus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.26 | lithium | reverses the effect of the drugs | Dictyostelium discoideum |  |
| 3.4.21.26 | S 17092 | selective enzyme inhibitor, pharmacodynamics and pharmacokinetics, overview | Homo sapiens | |
| 3.4.21.26 | S 17092 | selective enzyme inhibitor, pharmacodynamics and pharmacokinetics, overview | Mus musculus | |
| 3.4.21.26 | S 17092 | selective enzyme inhibitor, pharmacodynamics and pharmacokinetics, overview | Rattus norvegicus | |
| 3.4.21.26 | Valproic acid | reverses the effect of the drugs | Dictyostelium discoideum | |
| 3.4.21.26 | Z-Pro-prolinal | a transition state analog inhibitor, binding structure | Myxococcus xanthus | |
| 3.4.21.26 | Z-Pro-prolinal | a transition state analog inhibitor, binding structure | Novosphingobium capsulatum | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.21.26 | cytosol | - |
Homo sapiens | 5829 | - |
| 3.4.21.26 | cytosol | - |
Rattus norvegicus | 5829 | - |
| 3.4.21.26 | additional information | the highest levels in particulate fractions in the synaptosomal and the myelin fractions | Rattus norvegicus | - |
- |
| 3.4.21.26 | additional information | the highest levels in particulate fractions in the synaptosomal and the myelin fractions with a a fibrillary, cytoskeleton-like distribution, the enzyme is co-localized with tubulin and is a binding partner of tubulin, overview | Homo sapiens | - |
- |
| 3.4.21.26 | perinuclear space | - |
Homo sapiens | - |
- |
| 3.4.21.26 | synaptosome | - |
Homo sapiens | - |
- |
| 3.4.21.26 | synaptosome | - |
Rattus norvegicus | - |
- |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.26 | 71000 | - |
x * 71000 | Pyrococcus furiosus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.26 | alpha-melanocyte-stimulating hormone + H2O | Rattus norvegicus | - |
? | - |
? | |
| 3.4.21.26 | arginine-vasopressin + H2O | Mus musculus | - |
? | - |
? | |
| 3.4.21.26 | arginine-vasopressin + H2O | Homo sapiens | - |
? | - |
? | |
| 3.4.21.26 | arginine-vasopressin + H2O | Rattus norvegicus | - |
? | - |
? | |
| 3.4.21.26 | arginine-vasopressin + H2O | Sus scrofa | - |
? | - |
? | |
| 3.4.21.26 | additional information | Rattus norvegicus | the enzyme is involved with the inactivation of regulatory neuropeptides | ? | - |
? | |
| 3.4.21.26 | additional information | Homo sapiens | the enzyme is involved with the inactivation of regulatory neuropeptides, enzyme activity is correlated to an increase in protein secretion, suggesting that the enzyme may be involved in regulating secretory processes | ? | - |
? | |
| 3.4.21.26 | Substance P + H2O | Mus musculus | - |
? | - |
? | |
| 3.4.21.26 | Substance P + H2O | Homo sapiens | - |
? | - |
? | |
| 3.4.21.26 | Substance P + H2O | Rattus norvegicus | - |
? | - |
? | |
| 3.4.21.26 | Substance P + H2O | Sus scrofa | - |
? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.26 | Dictyostelium discoideum | - |
- |
- |
| 3.4.21.26 | Elizabethkingia meningoseptica | - |
- |
- |
| 3.4.21.26 | Homo sapiens | - |
- |
- |
| 3.4.21.26 | Mus musculus | - |
- |
- |
| 3.4.21.26 | Myxococcus xanthus | - |
- |
- |
| 3.4.21.26 | Novosphingobium capsulatum | - |
- |
- |
| 3.4.21.26 | Pyrococcus furiosus | - |
- |
- |
| 3.4.21.26 | Rattus norvegicus | - |
- |
- |
| 3.4.21.26 | Sus scrofa | - |
- |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.4.21.26 | proteolytic modification | limited proteolysis of the porcine enzyme with trypsin reveals a cleavage site at the Lys196-Ser197 bond in the flexible loop region of the propeller domain that interacts with the catalytic domain | Sus scrofa |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance | Mus musculus | |
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance | Homo sapiens | |
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance | Rattus norvegicus | |
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance | Sus scrofa | |
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance | Pyrococcus furiosus | |
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance | Dictyostelium discoideum | |
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance | Myxococcus xanthus | |
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance | Elizabethkingia meningoseptica | |
| 3.4.21.26 | Hydrolysis of --Pro-/- and to a lesser extent --Ala-/- in oligopeptides | the catalytic triad Ser, Asp, His is located in a large cavity at the interface of the two domains, the serine residue is located on what is called a nucleophile elbow, at the tip of a very sharp turn, it is surrounded by several small residues that provide relatively little steric hindrance | Novosphingobium capsulatum |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.21.26 | brain | - |
Mus musculus | - |
| 3.4.21.26 | brain | - |
Rattus norvegicus | - |
| 3.4.21.26 | brain | - |
Sus scrofa | - |
| 3.4.21.26 | brain | highest enzyme activity in the brain cortex, and lowest in the cerebellum | Homo sapiens | - |
| 3.4.21.26 | brain cortex | - |
Homo sapiens | - |
| 3.4.21.26 | central nervous system | - |
Rattus norvegicus | - |
| 3.4.21.26 | cerebellum | - |
Homo sapiens | - |
| 3.4.21.26 | cerebral cortex | - |
Rattus norvegicus | - |
| 3.4.21.26 | glioma cell | - |
Homo sapiens | - |
| 3.4.21.26 | HEK-293 cell | - |
Homo sapiens | - |
| 3.4.21.26 | hippocampus | - |
Rattus norvegicus | - |
| 3.4.21.26 | kidney | - |
Mus musculus | - |
| 3.4.21.26 | kidney | - |
Homo sapiens | - |
| 3.4.21.26 | kidney | - |
Rattus norvegicus | - |
| 3.4.21.26 | kidney | - |
Sus scrofa | - |
| 3.4.21.26 | liver | - |
Mus musculus | - |
| 3.4.21.26 | liver | - |
Homo sapiens | - |
| 3.4.21.26 | liver | - |
Rattus norvegicus | - |
| 3.4.21.26 | liver | - |
Sus scrofa | - |
| 3.4.21.26 | lung | - |
Mus musculus | - |
| 3.4.21.26 | lung | - |
Homo sapiens | - |
| 3.4.21.26 | lung | - |
Rattus norvegicus | - |
| 3.4.21.26 | lung | - |
Sus scrofa | - |
| 3.4.21.26 | medulla oblongata | - |
Rattus norvegicus | - |
| 3.4.21.26 | additional information | tissue distribution analysis | Mus musculus | - |
| 3.4.21.26 | additional information | tissue distribution analysis | Rattus norvegicus | - |
| 3.4.21.26 | additional information | tissue distribution analysis, no activity in the urine | Homo sapiens | - |
| 3.4.21.26 | muscle | - |
Mus musculus | - |
| 3.4.21.26 | muscle | - |
Homo sapiens | - |
| 3.4.21.26 | muscle | - |
Rattus norvegicus | - |
| 3.4.21.26 | muscle | - |
Sus scrofa | - |
| 3.4.21.26 | neuroblastoma cell | - |
Homo sapiens | - |
| 3.4.21.26 | pituitary gland | - |
Rattus norvegicus | - |
| 3.4.21.26 | saliva | - |
Homo sapiens | - |
| 3.4.21.26 | semen | - |
Homo sapiens | - |
| 3.4.21.26 | serum | - |
Homo sapiens | - |
| 3.4.21.26 | skeletal muscle | - |
Mus musculus | - |
| 3.4.21.26 | skeletal muscle | - |
Homo sapiens | - |
| 3.4.21.26 | skeletal muscle | - |
Rattus norvegicus | - |
| 3.4.21.26 | skeletal muscle | - |
Sus scrofa | - |
| 3.4.21.26 | submandibular gland | - |
Mus musculus | - |
| 3.4.21.26 | submandibular gland | - |
Homo sapiens | - |
| 3.4.21.26 | submandibular gland | - |
Rattus norvegicus | - |
| 3.4.21.26 | submandibular gland | - |
Sus scrofa | - |
| 3.4.21.26 | testis | - |
Mus musculus | - |
| 3.4.21.26 | testis | - |
Homo sapiens | - |
| 3.4.21.26 | testis | - |
Rattus norvegicus | - |
| 3.4.21.26 | testis | - |
Sus scrofa | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.26 | alpha-melanocyte-stimulating hormone + H2O | - |
Rattus norvegicus | ? | - |
? | |
| 3.4.21.26 | arginine-vasopressin + H2O | - |
Mus musculus | ? | - |
? | |
| 3.4.21.26 | arginine-vasopressin + H2O | - |
Homo sapiens | ? | - |
? | |
| 3.4.21.26 | arginine-vasopressin + H2O | - |
Rattus norvegicus | ? | - |
? | |
| 3.4.21.26 | arginine-vasopressin + H2O | - |
Sus scrofa | ? | - |
? | |
| 3.4.21.26 | gluten + H2O | - |
Myxococcus xanthus | ? | - |
? | |
| 3.4.21.26 | gluten + H2O | - |
Elizabethkingia meningoseptica | ? | - |
? | |
| 3.4.21.26 | gluten + H2O | - |
Novosphingobium capsulatum | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme is involved with the inactivation of regulatory neuropeptides | Rattus norvegicus | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme is involved with the inactivation of regulatory neuropeptides, enzyme activity is correlated to an increase in protein secretion, suggesting that the enzyme may be involved in regulating secretory processes | Homo sapiens | ? | - |
? | |
| 3.4.21.26 | additional information | substrate specificity, overview, the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, the S2' subsite had the highest specificity of the S1'-S3' subsites, this subsite prefers Pro residues, followed by Leu, Met, Phe, and Ala residues, the S1' subsite has lower specificity than the S2', with the strongest preference for hydrophobic, e.g. Leu, and aromatic, e.g. Phe, residues, and the greatest discrimination against Pro residues | Elizabethkingia meningoseptica | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview | Mus musculus | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview | Homo sapiens | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview | Rattus norvegicus | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview | Sus scrofa | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview | Pyrococcus furiosus | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview | Dictyostelium discoideum | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview | Myxococcus xanthus | ? | - |
? | |
| 3.4.21.26 | additional information | the enzyme hydrolyzes the peptide bond on the carboxyl side of internal proline residues of oligopeptide substrates with up to 30 amino acids, substrate specificity, overview | Novosphingobium capsulatum | ? | - |
? | |
| 3.4.21.26 | N-carbobenzyloxy-Ala-Pro-2-naphthylamide + H2O | - |
Mus musculus | N-carbobenzyloxy-Ala-Pro + 2-naphthylamine | - |
? | |
| 3.4.21.26 | N-carbobenzyloxy-Ala-Pro-2-naphthylamide + H2O | - |
Homo sapiens | N-carbobenzyloxy-Ala-Pro + 2-naphthylamine | - |
? | |
| 3.4.21.26 | N-carbobenzyloxy-Ala-Pro-2-naphthylamide + H2O | - |
Rattus norvegicus | N-carbobenzyloxy-Ala-Pro + 2-naphthylamine | - |
? | |
| 3.4.21.26 | N-succinyl-glycyl-proline-4-methylcoumarin-7-amide + H2O | - |
Mus musculus | N-succinyl-glycyl-proline + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.21.26 | N-succinyl-glycyl-proline-4-methylcoumarin-7-amide + H2O | - |
Homo sapiens | N-succinyl-glycyl-proline + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.21.26 | N-succinyl-glycyl-proline-4-methylcoumarin-7-amide + H2O | - |
Rattus norvegicus | N-succinyl-glycyl-proline + 7-amino-4-methylcoumarin | - |
? | |
| 3.4.21.26 | Substance P + H2O | - |
Mus musculus | ? | - |
? | |
| 3.4.21.26 | Substance P + H2O | - |
Homo sapiens | ? | - |
? | |
| 3.4.21.26 | Substance P + H2O | - |
Rattus norvegicus | ? | - |
? | |
| 3.4.21.26 | Substance P + H2O | - |
Sus scrofa | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.26 | ? | x * 71000 | Pyrococcus furiosus |
| 3.4.21.26 | More | tertiary structure, overview, the enzyme has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain, mechanism for peptide entry between the two domains, overview | Myxococcus xanthus |
| 3.4.21.26 | More | tertiary structure, overview, the enzyme has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain, mechanism for peptide entry between the two domains, overview | Novosphingobium capsulatum |
| 3.4.21.26 | More | the enzyme has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain, mechanism for peptide entry between the two domains, overview | Mus musculus |
| 3.4.21.26 | More | the enzyme has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain, mechanism for peptide entry between the two domains, overview | Homo sapiens |
| 3.4.21.26 | More | the enzyme has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain, mechanism for peptide entry between the two domains, overview | Rattus norvegicus |
| 3.4.21.26 | More | the enzyme has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain, mechanism for peptide entry between the two domains, overview | Pyrococcus furiosus |
| 3.4.21.26 | More | the enzyme has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain, mechanism for peptide entry between the two domains, overview | Dictyostelium discoideum |
| 3.4.21.26 | More | the enzyme has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain, mechanism for peptide entry between the two domains, overview | Elizabethkingia meningoseptica |
| 3.4.21.26 | More | the enzyme has a two-domain structure whose unique seven-blade beta-propeller domain works with the catalytic domain, mechanism for peptide entry between the two domains, the flexible loop region of the propeller domain, residues 192-205, that interacts with the catalytic domain, has the highest flexibility within the enzyme, molecular dynamics analysis, overview | Sus scrofa |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.26 | POP | - |
Mus musculus |
| 3.4.21.26 | POP | - |
Homo sapiens |
| 3.4.21.26 | POP | - |
Rattus norvegicus |
| 3.4.21.26 | POP | - |
Sus scrofa |
| 3.4.21.26 | POP | - |
Pyrococcus furiosus |
| 3.4.21.26 | POP | - |
Dictyostelium discoideum |
| 3.4.21.26 | POP | - |
Myxococcus xanthus |
| 3.4.21.26 | POP | - |
Elizabethkingia meningoseptica |
| 3.4.21.26 | POP | - |
Novosphingobium capsulatum |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.26 | 85 | 90 | - |
Pyrococcus furiosus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.26 | 4 | - |
24 h, stable | Pyrococcus furiosus |
| 3.4.21.26 | 37 | - |
24 h, stable | Pyrococcus furiosus |
| 3.4.21.26 | 85 | - |
overnight, remaining activity | Pyrococcus furiosus |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.21.26 | 0.000001 | - |
S 17092 | extracellular enzyme | Homo sapiens | |
| 3.4.21.26 | 0.00003 | - |
S 17092 | intracellular enzyme | Homo sapiens | |
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