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Literature summary extracted from
- Bioprocess for the production of recombinant HAP phytase of the thermophilic mold Sporotrichum thermophile and its structural and biochemical characteristics (2017), Int. J. Biol. Macromol., 94, 36-44 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.3.8 | gene phyA, real-time PCR expression analysis, constitutive secretary expression of codon-optimized rStPhy under glyceraldehyde phosphate dehydrogenase (GAP) promoter in Pichia pastoris strain X-33 | Thermothelomyces heterothallicus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | D344A | site-directed mutagenesis | Thermothelomyces heterothallicus |
| 3.1.3.8 | H71A | site-directed mutagenesis | Thermothelomyces heterothallicus |
| 3.1.3.8 | R70A | site-directed mutagenesis | Thermothelomyces heterothallicus |
| 3.1.3.8 | R74A | site-directed mutagenesis | Thermothelomyces heterothallicus |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.1.3.8 | tryptophan residues surrounded by negative charges play a key role in maintaining structural integrity of rStPhy | Thermothelomyces heterothallicus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.8 | additional information | the enzyme rStPhy shows very low sensitivity to pepsin | Thermothelomyces heterothallicus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.1.3.8 | extracellular | the enzyme is secreted | Thermothelomyces heterothallicus | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | Thermothelomyces heterothallicus | - |
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.8 | Thermothelomyces heterothallicus | V5M269 | i.e. Sporotrichum thermophile or Myceliophthora thermophila | - |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | glycoprotein | in silico analysis reveals 4 potential N-glycosylation sites, Asp165,Asp200, Asp275 and Asp346, and 3 potential O-glycosylation sites, Thr185, Thr274, and Thr321, in the enzyme | Thermothelomyces heterothallicus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 1190 | - |
purified recombinant enzyme, pH 5.0, 60°C | Thermothelomyces heterothallicus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.8 | myo-inositol hexakisphosphate + H2O | - |
Thermothelomyces heterothallicus | 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | More | the recombinant enzyme StPhy is composed of 26.65% alpha-helices, 5.26% beta-sheets and 68.09% random coils at pH 5.0 and 60°C. The three-dimensional structure of rStPhy displays characteristic signature sequences, RHGXRXP and HD, of HAP phytases, three-dimensional modeling, overview. Tryptophan residues surrounded by negative charges play a key role in maintaining structural integrity of rStPhy | Thermothelomyces heterothallicus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | HAP phytase | - |
Thermothelomyces heterothallicus |
| 3.1.3.8 | histidine acid phosphatase phytase | - |
Thermothelomyces heterothallicus |
| 3.1.3.8 | PhyA | - |
Thermothelomyces heterothallicus |
| 3.1.3.8 | StPhy | - |
Thermothelomyces heterothallicus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 60 | - |
assay at | Thermothelomyces heterothallicus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 73 | - |
melting temperature | Thermothelomyces heterothallicus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 5 | - |
assay at | Thermothelomyces heterothallicus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.3.8 | 4 | 7 | over 50% of maximal activity within this range | Thermothelomyces heterothallicus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.3.8 | evolution | enzyme rStPhy belongs to the histidine acid phosphatase (HAP) phytases family | Thermothelomyces heterothallicus |
| 3.1.3.8 | additional information | the catalytically important amino acids Arg74, His75, Arg78, His368, and Asp369 are identified by docking and site-directed mutagenesis, molecular surface analysis, and three-dimensional modeling | Thermothelomyces heterothallicus |
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