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Literature summary extracted from

  • Ranjan, B.; Satyanarayana, T.
    Recombinant HAP phytase of the thermophilic mold Sporotrichum thermophile expression of the codon-optimized phytase gene in Pichia pastoris and applications (2016), Mol. Biotechnol., 58, 137-147 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.8 butanol slightly stimulates the phytase activity Thermothelomyces heterothallicus
3.1.3.8 hexane slightly stimulates the phytase activity Thermothelomyces heterothallicus
3.1.3.8 isoamyl alcohol slightly stimulates the phytase activity Thermothelomyces heterothallicus
3.1.3.8 additional information the chelating agent EDTA has no discernible effect on the activity of rSt-Phy Thermothelomyces heterothallicus

Application

EC Number Application Comment Organism
3.1.3.8 agriculture enzyme rSt-Phy is useful in the dephytinization of broiler feeds efficiently in simulated gut conditions of chick leading to the liberation of soluble inorganic phosphate with concomitant mitigation in anti-nutrient effects of phytates Thermothelomyces heterothallicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.18 gene phyA, DNA and amino acid sequence determination and analysis, recombinant expression of the codon-optimized phytase gene in Pichia pastoris strain X-33, quantitative real-time PCR for gene copy number determination Thermothelomyces thermophilus
3.1.3.8 gene phyA, DNA and amino acid sequence determination and analysis, recombinant expression of the codon-optimized phytase gene in Pichia pastoris strain X-33, quantitative real-time PCR for gene copy number determination Thermothelomyces heterothallicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.11.1.18 additional information the enzyme is resistant to both pepsin and trypsin. The chelating agent EDTA has no discernible effect on the activity of rSt-Phy Thermothelomyces thermophilus
3.1.3.8 2,3-Butanedione
-
 Thermothelomyces heterothallicus
3.1.3.8 Al3+ 23% inhibition at 5 mM Thermothelomyces heterothallicus
3.1.3.8 Co2+ 10% inhibition at 5 mM Thermothelomyces heterothallicus
3.1.3.8 Cu2+ 18% inhibition at 5 mM Thermothelomyces heterothallicus
3.1.3.8 Fe2+ 12% inhibition at 5 mM Thermothelomyces heterothallicus
3.1.3.8 Fe3+ 18% inhibition at 5 mM Thermothelomyces heterothallicus
3.1.3.8 guanidinium hydrochloride
-
 Thermothelomyces heterothallicus
3.1.3.8 Mn2+ 12% inhibition at 5 mM Thermothelomyces heterothallicus
3.1.3.8 additional information the enzyme is resistant to both pepsin and trypsin. The chelating agent EDTA has no discernible effect on the activity of rSt-Phy Thermothelomyces heterothallicus
3.1.3.8 Na+ 8% inhibition at 5 mM Thermothelomyces heterothallicus
3.1.3.8 potassium iodide
-
 Thermothelomyces heterothallicus
3.1.3.8 Urea
-
 Thermothelomyces heterothallicus
3.1.3.8 Woodward's reagent K
-
 Thermothelomyces heterothallicus
3.1.3.8 Zn2+ 61% inhibition at 5 mM Thermothelomyces heterothallicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.8 additional information
-
 additional information kinetics and thermodynamics, overview Thermothelomyces heterothallicus
3.1.3.8 0.147
-
 myo-inositol hexakisphosphate calcium phytate, pH 5.0, 60°C Thermothelomyces heterothallicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.11.1.18 extracellular the enzyme is secreted Thermothelomyces thermophilus
-
-
3.1.3.8 extracellular the enzyme is secreted Thermothelomyces heterothallicus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.8 Ba2+ activates Thermothelomyces heterothallicus
3.1.3.8 Mg2+ activates Thermothelomyces heterothallicus
3.1.3.8 additional information poor effect by Ca2+ at 1-5 mM 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
1.11.1.18 Thermothelomyces thermophilus V5M269
-
-
3.1.3.8 Thermothelomyces heterothallicus V5M269 i.e. Sporotrichum thermophile or Myceliophthora thermophila
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.11.1.18 glycoprotein the enzyme is N-glycosylated, but also contains three potential O-glycosylation sites at positions 181, 185, and 268, it may be possible that the enzyme has one or more O-glycosylation. Deglycosylation using 10.0 U of endoglycosidase Hf (EndoHf) for 3 h at 37°C Thermothelomyces thermophilus
3.1.3.8 glycoprotein the enzyme is N-glycosylated, but also contains three potential O-glycosylation sites at positions 181, 185, and 268, it may be possible that the enzyme has one or more O-glycosylation. Deglycosylation using 10.0 U of endoglycosidase Hf (EndoHf) for 3 h at 37°C Thermothelomyces heterothallicus

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.18 recombinant enzyme from Pichia pastoris strain X-33 by ultrafiltration, anion exchange chromatography, dialysis, and gel filtration Thermothelomyces thermophilus
3.1.3.8 recombinant enzyme from Pichia pastoris strain X-33 by ultrafiltration, anion exchange chromatography, dialysis, and gel filtration Thermothelomyces heterothallicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.11.1.18 additional information the thermophilic mold Sporotrichum thermophile produces very low titers of phytase extracellularly in both solid state and submerged fermentations Thermothelomyces thermophilus
-
3.1.3.8 additional information the thermophilic mold Sporotrichum thermophile produces very low titers of phytase extracellularly in both solid state and submerged fermentations 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 0.0524
-
 purified native enzyme, pH 5.0, 60°C Thermothelomyces heterothallicus
3.1.3.8 46
-
 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.
1.11.1.18 KBr + 2 H2O
-
 Thermothelomyces thermophilus KH + HBr + H2O2
-
 ?
1.11.1.18 additional information besides its phytase activity (EC 3.1.3.8) with myo-inositol hexakisphosphate, the enzyme rSt-Phy also shows haloperoxidase activity. Enzyme rSt-Phy brings out a change in color of phenol red from red-orange to blue-violet in the presence of metavanadate ions, H2O2 and KBr in the reaction mixture, which confirms the bromoperoxidation of phenol red. Only histidine acid phosphatases with the active site sequence RHGXRXP can function as haloperoxidase, when vanadate ion is incorporated into the active site. Vanadate is a phosphate analogue, which is generally considered to bind as a transition state analogue to the phosphoryl transfer enzymes and inhibits their activities Thermothelomyces thermophilus ?
-
 ?
3.1.3.8 additional information enzyme rSt-Phy also shows haloperoxidase activity with KBr, metavanadate, and H2O2, only histidine acid phosphatases with the active site sequence RHGXRXP can function as haloperoxidase, overview Thermothelomyces heterothallicus ?
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
 Thermothelomyces heterothallicus 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O substrate is calcium phytate Thermothelomyces heterothallicus 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
1.11.1.18 ? x * 70000, recombinant enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE Thermothelomyces thermophilus
3.1.3.8 ? x * 70000, recombinant enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE Thermothelomyces heterothallicus

Synonyms

EC Number Synonyms Comment Organism
1.11.1.18 HAP phytase
-
 Thermothelomyces thermophilus
1.11.1.18 More cf. EC 3.1.3.8 Thermothelomyces thermophilus
1.11.1.18 St-Phy
-
 Thermothelomyces thermophilus
1.11.1.18 vanadate haloperoxidase
-
 Thermothelomyces thermophilus
3.1.3.8 HAP phytase
-
 Thermothelomyces heterothallicus
3.1.3.8 More cf. EC 1.11.1.18 Thermothelomyces heterothallicus
3.1.3.8 St-Phy
-
 Thermothelomyces heterothallicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.11.1.18 37
-
 assay at Thermothelomyces thermophilus
3.1.3.8 60
-
 native and recombinant enzyme Thermothelomyces heterothallicus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.3.8 30 75 activity range, profile overview Thermothelomyces heterothallicus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.3.8 60
-
 purified enzyme, pH 5.0, half-life of recombinant enzyme is 6 h and of native enzyme 16 h Thermothelomyces heterothallicus
3.1.3.8 80
-
 purified enzyme, pH 5.0, half-life of recombinant enzyme is 1 h and of native enzyme 1.5 h Thermothelomyces heterothallicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.8 1300
-
 myo-inositol hexakisphosphate calcium phytate, pH 5.0, 60°C Thermothelomyces heterothallicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.18 7
-
 assay at Thermothelomyces thermophilus
3.1.3.8 5
-
 native and recombinant enzyme Thermothelomyces heterothallicus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.3.8 2 7.5 activity range, profile overview Thermothelomyces heterothallicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.18 metavanadate required for activity Thermothelomyces thermophilus

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.3.8 8843.5
-
 myo-inositol hexakisphosphate calcium phytate, pH 5.0, 60°C Thermothelomyces heterothallicus