Any feedback?
Literature summary for 3.1.3.8 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)
| Cloned (Comment) | Organism |
|---|---|
| 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
| Protein Variants | Comment | Organism |
|---|---|---|
| D344A | site-directed mutagenesis | Thermothelomyces heterothallicus |
| H71A | site-directed mutagenesis | Thermothelomyces heterothallicus |
| R70A | site-directed mutagenesis | Thermothelomyces heterothallicus |
| R74A | site-directed mutagenesis | Thermothelomyces heterothallicus |
General Stability
| General Stability | Organism |
|---|---|
| tryptophan residues surrounded by negative charges play a key role in maintaining structural integrity of rStPhy | Thermothelomyces heterothallicus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the enzyme rStPhy shows very low sensitivity to pepsin | Thermothelomyces heterothallicus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme is secreted | Thermothelomyces heterothallicus | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| myo-inositol hexakisphosphate + H2O | Thermothelomyces heterothallicus | - |
1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermothelomyces heterothallicus | V5M269 | i.e. Sporotrichum thermophile or Myceliophthora thermophila | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| 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]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 1190 | - |
purified recombinant enzyme, pH 5.0, 60°C | Thermothelomyces heterothallicus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| myo-inositol hexakisphosphate + H2O | - |
Thermothelomyces heterothallicus | 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| HAP phytase | - |
Thermothelomyces heterothallicus |
| histidine acid phosphatase phytase | - |
Thermothelomyces heterothallicus |
| PhyA | - |
Thermothelomyces heterothallicus |
| StPhy | - |
Thermothelomyces heterothallicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
assay at | Thermothelomyces heterothallicus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 73 | - |
melting temperature | Thermothelomyces heterothallicus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
assay at | Thermothelomyces heterothallicus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 7 | over 50% of maximal activity within this range | Thermothelomyces heterothallicus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | enzyme rStPhy belongs to the histidine acid phosphatase (HAP) phytases family | Thermothelomyces heterothallicus |
| 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 |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
