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Literature summary extracted from
- Enzymatic characterization of a novel Xaa-Pro aminopeptidase XpmA from Aspergillus oryzae expressed in Escherichia coli (2017), J. Biosci. Bioeng., 124, 534-541 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.9 | 4-chloromercuribenzoate | slight activation at 0.1 mM | Aspergillus oryzae |  |
| 3.4.11.9 | bacitracin | slight activation at 0.1 mM | Aspergillus oryzae | |
| 3.4.11.9 | bestatin | slight activation at 0.1 mM | Aspergillus oryzae | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.11.9 | gene ampp, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21 | Aspergillus oryzae |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.9 | 2-mercaptoethanol | - |
Aspergillus oryzae | |
| 3.4.11.9 | Arg-Pro | substrate inhibition at concentrations above 3 mM | Aspergillus oryzae | |
| 3.4.11.9 | Co2+ | strong activation at 0.01-1.0 mM, inhibitory at 10 mM | Aspergillus oryzae | |
| 3.4.11.9 | DTT | - |
Aspergillus oryzae | |
| 3.4.11.9 | EDTA | 10 mM EDTA inhibits enzyme activity to 0.26 times of the control level | Aspergillus oryzae | |
| 3.4.11.9 | Fe2+ | slight activation at 0.05 mM, complete inhibition at 1 mM | Aspergillus oryzae | |
| 3.4.11.9 | Leu-Pro | substrate inhibition at concentrations above 4 mM | Aspergillus oryzae | |
| 3.4.11.9 | additional information | no inhibition by 4-(2-aminoethyl)benzensulfonylfluoride, tosyl lysyl chloromethyl ketone, and tosyl phenylalanyl chloromethyl ketone | Aspergillus oryzae | |
| 3.4.11.9 | Ni2+ | - |
Aspergillus oryzae | |
| 3.4.11.9 | Ser-Pro | substrate inhibition at concentrations above 10 mM | Aspergillus oryzae | |
| 3.4.11.9 | Zn2+ | complete inhibition at 1 mM | Aspergillus oryzae | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.11.9 | Ca2+ | slight activation at 10 mM | Aspergillus oryzae | |
| 3.4.11.9 | Co2+ | strong activation at 0.01-1.0 mM, inhibitory at 10 mM | Aspergillus oryzae | |
| 3.4.11.9 | Fe2+ | slight activation at 0.05 mM, complete inhibition at 1 mM | Aspergillus oryzae | |
| 3.4.11.9 | Mg2+ | activates | Aspergillus oryzae | |
| 3.4.11.9 | Mn2+ | required, best metal ion, the enzyme activity increases 27.6 times of the control level at 1 mM Mn2+, strong activation at 0.01-50 mM | Aspergillus oryzae | |
| 3.4.11.9 | additional information | rXpmA is a metalloprotease | Aspergillus oryzae | |
| 3.4.11.9 | NaCl | increases the enzyme activity in the concentration range 0.5-3.0 M, suggesting that the enzyme is halophilic | Aspergillus oryzae | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.9 | 129000 | - |
recombinant His-tagged enzyme, gel filtration | Aspergillus oryzae |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.11.9 | Aspergillus oryzae | Q2U7S5 | - |
- |
| 3.4.11.9 | Aspergillus oryzae ATCC 42149 | Q2U7S5 | - |
- |
| 3.4.11.9 | Aspergillus oryzae RIB 40 | Q2U7S5 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.4.11.9 | recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography, gel filtration, and dialysis | Aspergillus oryzae |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.9 | 177.69 | - |
pH 8.5, 50°C, purified recombinant enzyme | Aspergillus oryzae |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.11.9 | Ala-Pro + H2O | - |
Aspergillus oryzae | Ala + Pro | - |
? | |
| 3.4.11.9 | Ala-Pro + H2O | - |
Aspergillus oryzae RIB 40 | Ala + Pro | - |
? | |
| 3.4.11.9 | Ala-Pro + H2O | - |
Aspergillus oryzae ATCC 42149 | Ala + Pro | - |
? | |
| 3.4.11.9 | Ala-Pro-Tyr-Ala + H2O | - |
Aspergillus oryzae | Ala + Pro-Tyr-Ala | - |
? | |
| 3.4.11.9 | Ala-Pro-Tyr-Ala + H2O | - |
Aspergillus oryzae RIB 40 | Ala + Pro-Tyr-Ala | - |
? | |
| 3.4.11.9 | Ala-Pro-Tyr-Ala + H2O | - |
Aspergillus oryzae ATCC 42149 | Ala + Pro-Tyr-Ala | - |
? | |
| 3.4.11.9 | additional information | the recombinant enzyme XpmA shows hydrolysis activity toward Xaa-Pro-oligopeptides, especially the two dipeptides Ala-Pro and Phe-Pro. Peptides APRTPGGRR, RPPGFSPFR, LPFFD, and Gly-Pro-Ala show poor activity with the enzyme, while the dipeptide Gly-Pro gives no activity. rXpmA also shows no activity toward three peptides with proline at the N-terminus (Pro-Ala, Pro-Leu-Gly, and Pro-Leu-Ser-Arg-Tyr-Leu-Ser-Val-Ala-Ala-Lys-Lys) | Aspergillus oryzae | ? | - |
? | |
| 3.4.11.9 | additional information | the recombinant enzyme XpmA shows hydrolysis activity toward Xaa-Pro-oligopeptides, especially the two dipeptides Ala-Pro and Phe-Pro. Peptides APRTPGGRR, RPPGFSPFR, LPFFD, and Gly-Pro-Ala show poor activity with the enzyme, while the dipeptide Gly-Pro gives no activity. rXpmA also shows no activity toward three peptides with proline at the N-terminus (Pro-Ala, Pro-Leu-Gly, and Pro-Leu-Ser-Arg-Tyr-Leu-Ser-Val-Ala-Ala-Lys-Lys) | Aspergillus oryzae RIB 40 | ? | - |
? | |
| 3.4.11.9 | additional information | the recombinant enzyme XpmA shows hydrolysis activity toward Xaa-Pro-oligopeptides, especially the two dipeptides Ala-Pro and Phe-Pro. Peptides APRTPGGRR, RPPGFSPFR, LPFFD, and Gly-Pro-Ala show poor activity with the enzyme, while the dipeptide Gly-Pro gives no activity. rXpmA also shows no activity toward three peptides with proline at the N-terminus (Pro-Ala, Pro-Leu-Gly, and Pro-Leu-Ser-Arg-Tyr-Leu-Ser-Val-Ala-Ala-Lys-Lys) | Aspergillus oryzae ATCC 42149 | ? | - |
? | |
| 3.4.11.9 | Phe-Pro + H2O | - |
Aspergillus oryzae | Phe + Pro | - |
? | |
| 3.4.11.9 | Phe-Pro + H2O | - |
Aspergillus oryzae RIB 40 | Phe + Pro | - |
? | |
| 3.4.11.9 | Phe-Pro + H2O | - |
Aspergillus oryzae ATCC 42149 | Phe + Pro | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.11.9 | homodimer | 2 * 69000, recombinant His-tagged enzyme, SDS-PAGE | Aspergillus oryzae |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.11.9 | aminopeptidase P | - |
Aspergillus oryzae |
| 3.4.11.9 | AMPP | - |
Aspergillus oryzae |
| 3.4.11.9 | XpmA | - |
Aspergillus oryzae |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.9 | 50 | - |
- |
Aspergillus oryzae |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.9 | 20 | 50 | purified recombinant enzyme, stable up to, inactivation at 60°C | Aspergillus oryzae |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.9 | 8.5 | 9 | - |
Aspergillus oryzae |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.9 | 7 | 12 | activity range, recombinant enzyme | Aspergillus oryzae |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.4.11.9 | 4 | 11 | purified recombinant enzyme, stable at. The enzyme maintains activity after incubation at pH 3.5 -12.0, pretreatment between pH 4.0 and pH 7.5 or between pH 8.5 and pH 11.0 results in enzyme activity above 100% of control, in particular at pH 4.0-5.5 about 4-5fold | Aspergillus oryzae |
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