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Literature summary for 3.1.3.8 extracted from
- Heterologous expression and functional characterization of a plant alkaline phytase in Pichia pastoris (2010), Protein Expr. Purif., 74, 196-203.
Application
| Application | Comment | Organism |
|---|---|---|
| nutrition | isozymes LlALP1 and LlALP2 have the potential to be useful as feed and food supplements | Lilium longiflorum |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene LlAlp2, functional heterologous expression of isozyme LlALP2-Ala, with the c-myc and (His)6 tags at the C-terminus, from lily pollen in Pichia pastoris strains X-33 and KM71H, optimization of expression by varying the cDNA coding for LlALP2, host strain and growth conditions, overview | Lilium longiflorum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | - |
Lilium longiflorum |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates the recombinant isozyme LlALP2 4fold at 1 mM | Lilium longiflorum | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 53800 | - |
2 * 53800, about, isozyme LlALP1, sequence calculation | Lilium longiflorum |
| 56200 | - |
2 * 56200, about, isozyme LlALP2, sequence calculation | Lilium longiflorum |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| phytate + H2O | Lilium longiflorum | - |
? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Lilium longiflorum | Q0GYS1 | LIALP1 | - |
| Lilium longiflorum | Q0GYS2 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant isozyme LlALP2-Ala, with the c-myc and (His)6 tags at the C-terminus, from Pichia pastoris strains X-33 and KM71H by cobalt, not nickel, affinity chromatography | Lilium longiflorum |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| pollen | - |
Lilium longiflorum | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 4-nitrophenyl phosphate + H2O | - |
Lilium longiflorum | 4-nitrophenol + phosphate | - |
? | |
| additional information | the substrate specificity of LlALP from lily pollen is unique among phytases, it differs from that of acid phytases, which show broad substrate specificity, and from other alkaline phytases, which exhibit narrow substrate specificity including lack of activity against 4-nitrophenyl phosphate. LlALP from lily pollen hydrolyzes phytate and pNPP | Lilium longiflorum | ? | - |
? | |
| additional information | the substrate specificity of LlALP from lily pollen is unique among phytases, it differs from that of acid phytases, which show broad substrate specificity, and from other alkaline phytases, which exhibit narrow substrate specificity including lack of activity against 4-nitrophenyl phosphate. LlALP from lily pollen hydrolyzes phytate and pNPP. The recombinant LlALP2 expressed in Pichia pastoris hydrolyzes phytate and 4-nitrophenyl phosphate and exhibits no activity towards ATP. Activity against 4-nitrophenyl phosphate is nearly 2.5fold higher than against phytate, similar to what is observed with the native enzyme | Lilium longiflorum | ? | - |
? | |
| phytate + H2O | - |
Lilium longiflorum | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 53800, about, isozyme LlALP1, sequence calculation | Lilium longiflorum |
| homodimer | 2 * 56200, about, isozyme LlALP2, sequence calculation | Lilium longiflorum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alkaline phytase | - |
Lilium longiflorum |
| LlALP1 | - |
Lilium longiflorum |
| LlALP2 | - |
Lilium longiflorum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
recombinant isozyme LlALP2 | Lilium longiflorum |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 70 | activity range of recombinant isozyme LlALP2, sharp decrease in activity at temperatures above 55°C, consistent with the observations with the native LlALP | Lilium longiflorum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
recombinant isozyme LlALP2 | Lilium longiflorum |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 9 | activity range of recombinant isozyme LlALP2. Maximum activity at pH 8.0, 10% of maximal activity at pH 6.0, 60% of maximal activity at pH 9. The pH activity profile is similar to that of wild-type alkaline phytase isolated from lily pollen | Lilium longiflorum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the enzyme is a histidine phosphatase, it contains the signature heptapeptide of histidine phosphatases, -RHGXRXP- , near the N-terminus. Isozymes LlALP1 and LlALP2 possess unique catalytic properties. Substrate specificity and temperature dependence of catalysis of the recombinant isoyzme LlALP2 as well as the effect of pH, inhibitors, calcium ions, and EDTA are very similar to that of the wild-type enzyme from lily pollen | Lilium longiflorum |
| additional information | the enzyme is a histidine phosphatase, it contains the signature heptapeptide of histidine phosphatases, -RHGXRXP-, near the N-terminus. Isozymes LlALP1 and LlALP2 possess unique catalytic properties. Substrate specificity and temperature dependence of catalysis of the recombinant isoyzme LlALP2 as well as the effect of pH, inhibitors, calcium ions, and EDTA are very similar to that of the wild-type enzyme from lily pollen | Lilium longiflorum |
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