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Literature summary extracted from
- Biochemical characterization of the triticale TsPAP1, a new type of plant prolyl aminopeptidase, and its impact on proline content and flowering time in transgenic Arabidopsis plants (2017), Plant Physiol. Biochem., 116, 18-26 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.5 | 2-mercaptoethanol | 3.9fold activation at 1.0 mM | Secale cereale x Triticum turgidum subsp. durum |  |
| 3.4.11.5 | DTT | 5.7fold activation at 0.1 mM | Secale cereale x Triticum turgidum subsp. durum | |
| 3.4.11.5 | EDTA | 6.13fold activation at 1.0 mM | Secale cereale x Triticum turgidum subsp. durum | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.11.5 | gene pap1, recombinant expression of His-tagged enzyme in Escherichia coli, recombinant expression in transgenic Arabidopsis thaliana plants in rosette leaves | Secale cereale x Triticum turgidum subsp. durum |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.11.5 | additional information | impact of TsPAP1 overexpression on flowering time and the number of siliques due to the enhanced accumulation of proline in transgenic Arabidopsis thaliana plants. The recombinant TsPAP1 protein is expressed without the signal peptide, which could have a negative impact on its activity | Secale cereale x Triticum turgidum subsp. durum |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.5 | Cd2+ | 94% inhibition at 0.0005 mM | Secale cereale x Triticum turgidum subsp. durum | |
| 3.4.11.5 | Co2+ | 95% inhibition at 0.05 mM | Secale cereale x Triticum turgidum subsp. durum | |
| 3.4.11.5 | Cu2+ | 96% inhibition at 0.005 mM | Secale cereale x Triticum turgidum subsp. durum | |
| 3.4.11.5 | diisopropyl fluorophosphate | 87% inhibition at 0.1 mM, 94% at 1.0 mM | Secale cereale x Triticum turgidum subsp. durum | |
| 3.4.11.5 | Fe2+ | 29% inhibition at 0.5 mM | Secale cereale x Triticum turgidum subsp. durum | |
| 3.4.11.5 | iodoacetamide | slight inhibition at 1 mM, 90% inhibition at 10 mM | Secale cereale x Triticum turgidum subsp. durum | |
| 3.4.11.5 | additional information | no inhibition by E64, i.e. trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane, and pepstatin A at 10 mM | Secale cereale x Triticum turgidum subsp. durum | |
| 3.4.11.5 | PMSF | 72% inhibition at 0.1 mM, 92% at 1.0 mM | Secale cereale x Triticum turgidum subsp. durum | |
| 3.4.11.5 | Zn2+ | 97% inhibition at 0.0005 mM | Secale cereale x Triticum turgidum subsp. durum | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.4.11.5 | 0.0775 | - |
Pro-beta-naphthylamide | pH 7.5, 25°C, recombinant enzyme | Secale cereale x Triticum turgidum subsp. durum | |
| 3.4.11.5 | 0.28 | - |
Ala-beta-naphthylamide | pH 7.5, 25°C, recombinant enzyme | Secale cereale x Triticum turgidum subsp. durum | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.11.5 | chloroplast | - |
Secale cereale x Triticum turgidum subsp. durum | 9507 | - |
| 3.4.11.5 | cytoplasm | - |
Secale cereale x Triticum turgidum subsp. durum | 5737 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.5 | Fe2+ | activates slightly at 0.5 mM | Secale cereale x Triticum turgidum subsp. durum | |
| 3.4.11.5 | additional information | no effect by Mg2+, Na+, Ba2+, Mn2+ at 0.5 mM | Secale cereale x Triticum turgidum subsp. durum |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.5 | Secale cereale x Triticum turgidum subsp. durum | G9J616 | triticosecale | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.11.5 | recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography | Secale cereale x Triticum turgidum subsp. durum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.5 | Ala-beta-naphthylamide + H2O | - |
Secale cereale x Triticum turgidum subsp. durum | Ala + beta-naphthylamine | - |
? | |
| 3.4.11.5 | Hyp-beta-naphthylamide + H2O | - |
Secale cereale x Triticum turgidum subsp. durum | Hyp + beta-naphthylamine | - |
? | |
| 3.4.11.5 | additional information | the recombinant enzyme shows preference for substrates with a proline at the N-terminus. The enzyme also hydrolyzes beta-naphthylamides of hydroxyproline and alanine, although the observed activity is almost 2fold lower than against Pro-beta-naphthylamide. The activity against the other amino acid-beta-naphthylamides tested (with Phe-, Glu-, Arg-, Tyr-, Leu-, Asp-, Met-, Trp-, and Val-beta-naphthylamide) is not detectable or does not exceed 7% of the maximal activity. Among the peptides with proline at the N-terminus, TsPAP1 shows a much higher preference for dipeptides than tri- and tetrapeptides. Not only the length of the peptide is important, as also the amino acid in the Y position influences the rate of proline liberation. Among dipeptides, the most preferred is Pro-Gly and Pro-Pro while Pro-Ala is hydrolyzed at only 10% the rate of Pro-Gly. The activity against tripeptide Pro-Gly-Gly is 27% of the maximal activity while the rate of hydrolysis of the tetrapeptides is very low and does not exceed 10% of that against Pro-Gly | Secale cereale x Triticum turgidum subsp. durum | ? | - |
? | |
| 3.4.11.5 | Pro-Ala + H2O | low activity | Secale cereale x Triticum turgidum subsp. durum | Pro + Ala | - |
? | |
| 3.4.11.5 | Pro-beta-naphthylamide + H2O | preferred substrate | Secale cereale x Triticum turgidum subsp. durum | Pro + beta-naphthylamine | - |
? | |
| 3.4.11.5 | Pro-Gly + H2O | - |
Secale cereale x Triticum turgidum subsp. durum | Pro + Gly | - |
? | |
| 3.4.11.5 | Pro-Gly-Gly + H2O | low activity | Secale cereale x Triticum turgidum subsp. durum | Pro + Gly-Gly | - |
? | |
| 3.4.11.5 | Pro-Gly-Gly-Gly + H2O | low activity | Secale cereale x Triticum turgidum subsp. durum | Pro + Gly-Gly-Gly | - |
? | |
| 3.4.11.5 | Pro-Leu + H2O | low activity | Secale cereale x Triticum turgidum subsp. durum | Pro + Leu | - |
? | |
| 3.4.11.5 | Pro-Leu-Gly + H2O | low activity | Secale cereale x Triticum turgidum subsp. durum | Pro + Leu-Gly | - |
? | |
| 3.4.11.5 | Pro-Pro + H2O | - |
Secale cereale x Triticum turgidum subsp. durum | Pro + Pro | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.11.5 | monomer | - |
Secale cereale x Triticum turgidum subsp. durum |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.11.5 | Prolyl aminopeptidase | - |
Secale cereale x Triticum turgidum subsp. durum |
| 3.4.11.5 | TsPAP1 | - |
Secale cereale x Triticum turgidum subsp. durum |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | 25 | - |
recombinant enzyme, without EDTA | Secale cereale x Triticum turgidum subsp. durum |
| 3.4.11.5 | 37 | - |
recombinant enzyme, with EDTA | Secale cereale x Triticum turgidum subsp. durum |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | - |
60 | activity range, profile overview | Secale cereale x Triticum turgidum subsp. durum |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | 7.5 | - |
recombinant enzyme | Secale cereale x Triticum turgidum subsp. durum |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.5 | 6 | 9.2 | activity range, profile overview | Secale cereale x Triticum turgidum subsp. durum |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.11.5 | evolution | enzyme TsPAP1 belongs to the S33.001 subfamily of aminopeptidases with presence of additional tens of amino acids at the N-terminus of the most plant sequences but not of microorganisms. These additional amino acids constitute a potential signal peptide sequence most likely directing the proteins to chloroplasts. The plant PAP sequences display a high percent of amino acid identity from only the second methionine from the N-terminus (M86 in TsPAP1) while not within the sequence of the signal peptide | Secale cereale x Triticum turgidum subsp. durum |
| 3.4.11.5 | malfunction | impact of TsPAP1 overexpression on flowering time and the number of siliques due to the enhanced accumulation of proline in transgenic Arabidopsis thaliana plants, phenotype, overview | Secale cereale x Triticum turgidum subsp. durum |
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