Application | Comment | Organism |
---|---|---|
synthesis | the enzyme is interesting for an industrial application, because of the high specificity for N-terminal Asp and Glu | Lactobacillus delbrueckii subsp. lactis |
Cloned (Comment) | Organism |
---|---|
gene pepA, recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Lactobacillus delbrueckii subsp. lactis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
acetic acid | inactivates at 50% w/v | Lactobacillus delbrueckii subsp. lactis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics | Lactobacillus delbrueckii subsp. lactis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Co2+ | activates | Lactobacillus delbrueckii subsp. lactis | |
Cu2+ | activates | Lactobacillus delbrueckii subsp. lactis | |
Mn2+ | activates | Lactobacillus delbrueckii subsp. lactis | |
additional information | PepA ia a metallopeptidase. The metal center can be described as [M1M2-enzyme], where M1 and M2 indicate the type of metal ion in site 1 and site 2. The activity and reaction kinetics, as well as the pH and temperature profile differ depending on the metal ion used in the reaction or reactivation. Quantification of activity of reactivated recombinant apo-PepA with different metal ions, overview | Lactobacillus delbrueckii subsp. lactis | |
Ni2+ | activates | Lactobacillus delbrueckii subsp. lactis | |
Zn2+ | activates | Lactobacillus delbrueckii subsp. lactis |
Organic Solvent | Comment | Organism |
---|---|---|
acetic acid | inactivates at 50% w/v | Lactobacillus delbrueckii subsp. lactis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Lactobacillus delbrueckii subsp. lactis | F0HXE4 | - |
- |
Lactobacillus delbrueckii subsp. lactis DSM 20072 | F0HXE4 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by dialysis, nickel affinity chromatography, and desalting gel filtration | Lactobacillus delbrueckii subsp. lactis |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.85 | - |
recombinant reactivated CuCu-PepA, pH 7.0, 55°C, substrate L-aspartate-beta-naphthylamide | Lactobacillus delbrueckii subsp. lactis |
1.3 | - |
recombinant reactivated NiNi-PepA, pH 6.0, 60°C, substrate L-aspartate-beta-naphthylamide | Lactobacillus delbrueckii subsp. lactis |
27.2 | - |
recombinant reactivated ZnZn-PepA, pH 6.0, 60°C, substrate L-aspartate-beta-naphthylamide | Lactobacillus delbrueckii subsp. lactis |
53.3 | - |
recombinant reactivated CoCo-PepA, pH 6.0, 65°C, substrate L-aspartate-beta-naphthylamide | Lactobacillus delbrueckii subsp. lactis |
78.6 | - |
recombinant reactivated MnMn-PepA, pH 6.0, 60°C, substrate L-aspartate-beta-naphthylamide | Lactobacillus delbrueckii subsp. lactis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Asp-Ala + H2O | - |
Lactobacillus delbrueckii subsp. lactis | Asp + Ala | - |
? | |
Asp-Ala + H2O | - |
Lactobacillus delbrueckii subsp. lactis DSM 20072 | Asp + Ala | - |
? | |
Glu-Ala + H2O | - |
Lactobacillus delbrueckii subsp. lactis | Glu + Ala | - |
? | |
Glu-Ala + H2O | - |
Lactobacillus delbrueckii subsp. lactis DSM 20072 | Glu + Ala | - |
? | |
Glu-Gly + H2O | - |
Lactobacillus delbrueckii subsp. lactis | Glu + Gly | - |
? | |
Glu-Gly + H2O | - |
Lactobacillus delbrueckii subsp. lactis DSM 20072 | Glu + Gly | - |
? | |
L-aspartate-beta-naphthylamide + H2O | - |
Lactobacillus delbrueckii subsp. lactis | L-aspartate + beta-naphthylamine | - |
? | |
L-glutamyl-beta-naphthylamide + H2O | - |
Lactobacillus delbrueckii subsp. lactis | L-glutamine + beta-naphthylamine | - |
? | |
additional information | the wild-type enzyme has a high specificity for N-terminal Asp and Glu. Enzyme specificities of the enzyme-metal variants with different substrates, overview | Lactobacillus delbrueckii subsp. lactis | ? | - |
? | |
additional information | the wild-type enzyme has a high specificity for N-terminal Asp and Glu. Enzyme specificities of the enzyme-metal variants with different substrates, overview | Lactobacillus delbrueckii subsp. lactis DSM 20072 | ? | - |
? | |
Ser-Ala + H2O | - |
Lactobacillus delbrueckii subsp. lactis | Ser + Ala | - |
? | |
Ser-Ala + H2O | - |
Lactobacillus delbrueckii subsp. lactis DSM 20072 | Ser + Ala | - |
? |
Synonyms | Comment | Organism |
---|---|---|
aminopeptidase A | - |
Lactobacillus delbrueckii subsp. lactis |
Lb-PepA | - |
Lactobacillus delbrueckii subsp. lactis |
PepA | - |
Lactobacillus delbrueckii subsp. lactis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
at 60°C, relative activity of 78% is detected for CoCo (PepA). CuCu(PepA) shows a relative activity of 29% at this temperature | Lactobacillus delbrueckii subsp. lactis |
55 | - |
CuCu-PepA | Lactobacillus delbrueckii subsp. lactis |
60 | - |
MnMn-PepA, NiNi-PepA, and ZnZn-PepA | Lactobacillus delbrueckii subsp. lactis |
65 | - |
CoCo-PepA | Lactobacillus delbrueckii subsp. lactis |
Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | 80 | activity range, profile overview | Lactobacillus delbrueckii subsp. lactis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
MnMn-PepA, NiNi-PepA, CoCo-PepA, and ZnZn-PepA | Lactobacillus delbrueckii subsp. lactis |
7 | - |
CuCu-PepA | Lactobacillus delbrueckii subsp. lactis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
4 | 8 | activity range of CuCu-PepA, profile overview | Lactobacillus delbrueckii subsp. lactis |
4.5 | 8 | activity range of CoCo-PepA, NiNi-PepA, and ZnZn-PepA, profiles overview | Lactobacillus delbrueckii subsp. lactis |
5 | 8 | activity range of MnMn-PepA, profile overview | Lactobacillus delbrueckii subsp. lactis |
General Information | Comment | Organism |
---|---|---|
physiological function | aminopeptidase A (PepA) belongs to the group of metallopeptidases with two bound metal ions per subunit, M1M2-PepA, it is specific for the cleavage of N-terminal glutamic (Glu) and aspartic acid (Asp) and, in low amounts, serine (Ser) residues | Lactobacillus delbrueckii subsp. lactis |