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Literature summary extracted from

  • Lee, S.; Cho, J.; Bok, J.; Kang, S.; Choi, Y.; Lee, P.
    Characterization, gene cloning, and sequencing of a fungal phytase, PhyA, from Penicillium oxalicum PJ3 (2015), Prep. Biochem. Biotechnol., 45, 336-347 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.8 EDTA slight activation Penicillium oxalicum
3.1.3.26 EDTA slight activation Penicillium oxalicum

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.8 gene phyA, DNA and amino acid sequence determination and analysis Penicillium oxalicum
3.1.3.26 gene phyA, DNA and amino acid sequence determination and analysis Penicillium oxalicum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.8 Ca2+ strong inhibition at 5 mM Penicillium oxalicum
3.1.3.8 Cu2+ strong inhibition at 5 mM Penicillium oxalicum
3.1.3.8 PMSF strong inhibition at 5 mM Penicillium oxalicum
3.1.3.8 Zn2+ strong inhibition at 5 mM Penicillium oxalicum
3.1.3.26 Ca2+ strong inhibition at 5 mM Penicillium oxalicum
3.1.3.26 Cu2+ strong inhibition at 5 mM Penicillium oxalicum
3.1.3.26 PMSF strong inhibition at 5 mM Penicillium oxalicum
3.1.3.26 Zn2+ strong inhibition at 5 mM Penicillium oxalicum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.8 additional information
-
additional information Line-Weaver Burk plot Penicillium oxalicum
3.1.3.8 0.545
-
myo-inositol hexakisphosphate pH 4.5, 55°C Penicillium oxalicum
3.1.3.26 additional information
-
additional information Line-Weaver Burk plot Penicillium oxalicum
3.1.3.26 0.545
-
myo-inositol hexakisphosphate pH 4.5, 55°C Penicillium oxalicum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.8 extracellular
-
Penicillium oxalicum
-
-
3.1.3.26 extracellular
-
Penicillium oxalicum
-
-

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 Penicillium oxalicum phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O Penicillium oxalicum PJ3 phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O Penicillium oxalicum phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O Penicillium oxalicum PJ3 phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 1D-myo-inositol pentakisphosphate + phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Penicillium oxalicum Q6YNE9
-
-
3.1.3.8 Penicillium oxalicum PJ3 Q6YNE9
-
-
3.1.3.26 Penicillium oxalicum Q6YNE9
-
-
3.1.3.26 Penicillium oxalicum PJ3 Q6YNE9
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.3.8 glycoprotein glycosylation of six potential N-glycosylation sites Penicillium oxalicum
3.1.3.26 glycoprotein glycosylation of six potential N-glycosylation sites Penicillium oxalicum

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.8 native enzyme PhyA 427fold from strain PJ3 by ammonium sulfate fractionation, dialysis, gel filtration, and cation exchange chromatography, and again dialysis, to homogeneity Penicillium oxalicum
3.1.3.26 native enzyme PhyA 427fold from strain PJ3 by ammonium sulfate fractionation, dialysis, gel filtration, and cation exchange chromatography, and again dialysis, to homogeneity Penicillium oxalicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.8 additional information among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate Penicillium oxalicum ?
-
?
3.1.3.8 additional information among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate Penicillium oxalicum PJ3 ?
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Penicillium oxalicum 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate Penicillium oxalicum 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.8 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Penicillium oxalicum PJ3 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.26 additional information among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate Penicillium oxalicum ?
-
?
3.1.3.26 additional information among the many phosphate conjugate substrates PhyA shows fairly high specificity for phytate Penicillium oxalicum PJ3 ?
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Penicillium oxalicum 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate Penicillium oxalicum 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Penicillium oxalicum PJ3 1D-myo-inositol pentakisphosphate + phosphate
-
?
3.1.3.26 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26, substrate is sodium phytate Penicillium oxalicum PJ3 1D-myo-inositol pentakisphosphate + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.1.3.8 ? x * 65000, SDS-PAGE, x * 50481, sequence calculation Penicillium oxalicum
3.1.3.26 ? x * 65000, SDS-PAGE, x * 50481, sequence calculation Penicillium oxalicum

Synonyms

EC Number Synonyms Comment Organism
3.1.3.8 More cf. EC 3.1.3.26 Penicillium oxalicum
3.1.3.8 myo-inositol-hexakisphosphate phosphohydrolase
-
Penicillium oxalicum
3.1.3.8 PhyA
-
Penicillium oxalicum
3.1.3.8 phytase
-
Penicillium oxalicum
3.1.3.8 PJ3 phytase
-
Penicillium oxalicum
3.1.3.26 More cf. EC 3.1.3.8 Penicillium oxalicum
3.1.3.26 myo-inositol-hexakisphosphate phosphohydrolase
-
Penicillium oxalicum
3.1.3.26 PhyA
-
Penicillium oxalicum
3.1.3.26 phytase
-
Penicillium oxalicum
3.1.3.26 PJ3 phytase
-
Penicillium oxalicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.8 55
-
-
Penicillium oxalicum
3.1.3.26 55
-
-
Penicillium oxalicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.8 4.5
-
-
Penicillium oxalicum
3.1.3.26 4.5
-
-
Penicillium oxalicum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.3.8 3.2 5.4 over 70% of the maximum activity within this pH range Penicillium oxalicum
3.1.3.26 3.2 5.4 over 70% of the maximum activity within this pH range Penicillium oxalicum

General Information

EC Number General Information Comment Organism
3.1.3.8 evolution the enzyme belongs to the histidine acid phosphatase family, it contains the active-site motif RHGXRXP Penicillium oxalicum
3.1.3.8 additional information the enzyme has an active-site motif RHGXRXP and a remote C-teminal His-Asp (HD motif) which takes part in the catalysis Penicillium oxalicum
3.1.3.8 physiological function phytase hydrolyzes phytic acid (myo-inositol-hexakisphosphate), which is the major storage form of phosphorus in cereals, legumes, and oilseed crops Penicillium oxalicum
3.1.3.26 evolution the enzyme belongs to the histidine acid phosphatase family, it contains the active-site motif RHGXRXP Penicillium oxalicum
3.1.3.26 additional information the enzyme has an active-site motif RHGXRXP and a remote C-teminal His-Asp (HD motif) which takes part in the catalysis Penicillium oxalicum
3.1.3.26 physiological function phytase hydrolyzes phytic acid (myo-inositol-hexakisphosphate), which is the major storage form of phosphorus in cereals, legumes, and oilseed crops Penicillium oxalicum