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Literature summary extracted from
- The catalytic properties of alkaline phosphatases under various conditions (2008), Russ. J. Phys. Chem. A, 82, 1947-1951.
No PubMed abstract available
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.1.3.1 | 0.00000001 | - |
4-nitrophenyl phosphate | Vmax (mmol/min mg of protein): 1.8 (dimer), 0.42 (tetramer) | Escherichia coli |  |
| 3.1.3.1 | 0.00000035 | - |
4-nitrophenyl phosphate | - |
Bos taurus | |
| 3.1.3.1 | 0.00000035 | - |
4-nitrophenyl phosphate | pH: 8.5 | Gallus gallus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.1 | Bos taurus | - |
- |
- |
| 3.1.3.1 | Escherichia coli | - |
- |
- |
| 3.1.3.1 | Gallus gallus | Q92058 | - |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.1.3.1 | intestine | - |
Bos taurus | - |
| 3.1.3.1 | intestine | - |
Gallus gallus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.1 | 4-nitrophenyl phosphate + H2O | - |
Escherichia coli | 4-nitrophenol + phosphate | - |
? | |
| 3.1.3.1 | 4-nitrophenyl phosphate + H2O | - |
Bos taurus | 4-nitrophenol + phosphate | - |
? | |
| 3.1.3.1 | 4-nitrophenyl phosphate + H2O | - |
Gallus gallus | 4-nitrophenol + phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.3.1 | dimer | activity of the dimer is three or four times higher than that of the tetramer | Escherichia coli |
| 3.1.3.1 | dimer | activity of the dimer is three or four times higher than that of the tetramer | Bos taurus |
| 3.1.3.1 | dimer | activity of the dimer is three or four times higher than that of the tetramer | Gallus gallus |
| 3.1.3.1 | tetramer | - |
Escherichia coli |
| 3.1.3.1 | tetramer | - |
Bos taurus |
| 3.1.3.1 | tetramer | - |
Gallus gallus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.3.1 | alkaline phosphatase | - |
Escherichia coli |
| 3.1.3.1 | alkaline phosphatase | - |
Bos taurus |
| 3.1.3.1 | alkaline phosphatase | - |
Gallus gallus |
| 3.1.3.1 | ALP | - |
Escherichia coli |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.1 | 8.5 | - |
assay at | Escherichia coli |
| 3.1.3.1 | 8.5 | - |
assay at | Gallus gallus |
| 3.1.3.1 | 8.5 | - |
five buffer systems are investigated at pH 8.5: tris, carbonate, hepes, borate, and glycine buffers, and the lowest catalytic activity of alkaline phosphatases at equal pH is observed in the borate buffer. The highest specific activity, is observed in the buffer solution of tris-(oxymethyl)-aminomethane-HCl | Bos taurus |
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Release 2023.1 (January 2023)
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