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Literature summary for 3.1.3.8 extracted from

  • Singh, B.; Sharma, K.; Kumari, A.; Kumar, A.; Gakhar, S.
    Molecular modeling and docking of recombinant HAP-phytase of a thermophilic mould Sporotrichum thermophile reveals insights into molecular catalysis and biochemical properties (2018), Int. J. Biol. Macromol., 115, 501-508 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant overexpression in Pichia pastoris strain X-33 using inducible promoter AOX1, the enzyme is secreted Thermothelomyces heterothallicus

Inhibitors

Inhibitors Comment Organism Structure
2,3-Butanedione strong inhibition, interacts with arginine residues Thermothelomyces heterothallicus
meta-vanadate
-
Thermothelomyces heterothallicus
additional information inhibitor docking study, overview. The enzyme is protease resistant Thermothelomyces heterothallicus
myo-inositol hexasulfate a potent competitive inhibitor for phytase Thermothelomyces heterothallicus
Phenylglyoxal interacts with arginine residues. Phenylglyoxal does not show any inhibition under acidic pH 5.0 Thermothelomyces heterothallicus
phosphate
-
Thermothelomyces heterothallicus
tartaric acid
-
Thermothelomyces heterothallicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.159
-
myo-inositol hexakisphosphate substrate sodium phytate, pH 5.0, 60°C, recombinant enzyme Thermothelomyces heterothallicus
0.208
-
myo-inositol hexakisphosphate substrate potassium phytate, pH 5.0, 60°C, recombinant enzyme Thermothelomyces heterothallicus
0.667
-
myo-inositol hexakisphosphate substrate calcium phytate, pH 5.0, 60°C, recombinant enzyme Thermothelomyces heterothallicus

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the enzyme shows no requirement for metal ions 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
-
i.e. Myceliophthora thermophila or Sporotrichum thermophile strain BJTLR50
-

Purification (Commentary)

Purification (Comment) Organism
recombinant extracellular phytase from Pichia pastoris strain X-33 culture medium by lyophilization, dialysis, and anion exchange chromatography Thermothelomyces heterothallicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the recombinant enzyme displayed broad substrate specificity. Molecular modeling and docking of phytase with various substrates show differential binding patterns, overview. Strong binding affinity with ATP and phytic acid, while the lowest with AMP and phosphoenol pyruvate. The enzyme is also active with ATP and 4-nitrophenyl phosphate Thermothelomyces heterothallicus ?
-
?
myo-inositol hexakisphosphate + H2O
-
Thermothelomyces heterothallicus 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
?
myo-inositol hexakisphosphate + H2O substrates are sodium phytate, potassium phytate, and calcium phytate. Highest activity with calcium phytate Thermothelomyces heterothallicus 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
?

Subunits

Subunits Comment Organism
? x * 70000, recombinant enzyme, SDS-PAGE Thermothelomyces heterothallicus

Synonyms

Synonyms Comment Organism
HAP-phytase
-
Thermothelomyces heterothallicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Thermothelomyces heterothallicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
Thermothelomyces heterothallicus

General Information

General Information Comment Organism
additional information structure of the active site pocket of phytase protein, homology modeling of HAP-phytase, overview Thermothelomyces heterothallicus