Literature summary for 1.11.1.18 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 .

Search for more literature for 1.11.1.18

Cloned(Commentary)

Cloned (Comment)	Organism
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

Inhibitors

Inhibitors	Comment	Organism	Structure
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

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	the enzyme is secreted	Thermothelomyces thermophilus	-	-

Organism

Organism	UniProt	Comment	Textmining
Thermothelomyces thermophilus	V5M269	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
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

Purification (Commentary)

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

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	the thermophilic mold Sporotrichum thermophile produces very low titers of phytase extracellularly in both solid state and submerged fermentations	Thermothelomyces thermophilus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
KBr + 2 H2O	-	Thermothelomyces thermophilus	KH + HBr + H2O2	-	?
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	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 70000, recombinant enzyme, SDS-PAGE, x * 90000, native enzyme, SDS-PAGE	Thermothelomyces thermophilus

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Thermothelomyces thermophilus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Thermothelomyces thermophilus

Cofactor

Cofactor	Comment	Organism	Structure
metavanadate	required for activity	Thermothelomyces thermophilus

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Release 2023.1 (January 2023)