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Literature summary for 5.3.1.4 extracted from
- Enzymatic conversion of D-galactose to D-tagatose: cloning, overexpression and characterization of L-arabinose isomerase from Pediococcus pentosaceus PC-5 (2014), Microbiol. Res., 169, 171-178.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Pediococcus pentosaceus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ba2+ | 33.08% residual activity at 1 mM | Pediococcus pentosaceus |  |
| Ca2+ | 33.61% residual activity at 1 mM | Pediococcus pentosaceus | |
| Cu2+ | 3.31% residual activity at 1 mM | Pediococcus pentosaceus | |
| EDTA | complete inhibition at 1 mM | Pediococcus pentosaceus | |
| Fe3+ | 27.52% residual activity at 1 mM | Pediococcus pentosaceus | |
| Mg2+ | 45.12% residual activity at 1 mM | Pediococcus pentosaceus | |
| Mn2+ | 31.14% residual activity at 1 mM; 60.81% residual activity at 1 mM | Pediococcus pentosaceus | |
| Ni2+ | 39.71% residual activity at 1 mM | Pediococcus pentosaceus | |
| Zn2+ | 12.89% residual activity at 1 mM | Pediococcus pentosaceus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 66 | - |
D-galactose | at 50°C and pH 6.0 | Pediococcus pentosaceus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | this enzyme exhibits a weak requirement for metal ions for its maximal activity evaluated at 0.6 mM Mn2+ and 0.8 mM Co2+ (115.38% activity in the presence of Mn2+ and Co2+) | Pediococcus pentosaceus | |
| Mn2+ | this enzyme exhibits a weak requirement for metall ions for its maximal activity evaluated at 0.6 mM Mn2+ and 0.8 mM Co2+ (115.38% activity in the presence of Mn2+ and Co2+) | Pediococcus pentosaceus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pediococcus pentosaceus | G1JRK8 | - |
- |
| Pediococcus pentosaceus PC-5 | G1JRK8 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni-NTA affinity column chromatography | Pediococcus pentosaceus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| D-Allose | about 10% activity compared to D-galactose | Pediococcus pentosaceus | ? | - |
? | |
| D-Allose | about 10% activity compared to D-galactose | Pediococcus pentosaceus PC-5 | ? | - |
? | |
| D-galactose | 100% activity | Pediococcus pentosaceus | D-tagatose | conversion of 52% after 24 h at 50°C | ? | |
| D-galactose | 100% activity | Pediococcus pentosaceus PC-5 | D-tagatose | conversion of 52% after 24 h at 50°C | ? | |
| D-glucose | less than 40% activity compared to D-galactose | Pediococcus pentosaceus | ? | - |
? | |
| D-glucose | less than 40% activity compared to D-galactose | Pediococcus pentosaceus PC-5 | ? | - |
? | |
| D-Xylose | about 70% activity compared to D-galactose | Pediococcus pentosaceus | ? | - |
? | |
| D-Xylose | about 70% activity compared to D-galactose | Pediococcus pentosaceus PC-5 | ? | - |
? | |
| additional information | no activity with L-arabinose | Pediococcus pentosaceus | ? | - |
? | |
| additional information | no activity with L-arabinose | Pediococcus pentosaceus PC-5 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AraA | - |
Pediococcus pentosaceus |
| L-AI | - |
Pediococcus pentosaceus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Pediococcus pentosaceus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 45 | at 30°C, 40°C and 45°C, the enzyme retains 40%, 80%, 95% of its relative activity, but at higher temperatures (above 60°C) the relative activity decreases rapidly | Pediococcus pentosaceus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 60 | at 55 and 60°C the enzyme stability decreases with half-lives of 2 h and 0.8 h, respectively. The enzyme is perfectly stable showing above 80% of its maximal activity after a 3 h incubation at 50°C in the presence of 0.6 mM Mn2+ or 0.6 mM Mn2+ plus 0.8 mM Co2+ | Pediococcus pentosaceus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
- |
Pediococcus pentosaceus |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.048 | - |
D-galactose | at 50°C and pH 6.0 | Pediococcus pentosaceus | |
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