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Literature summary extracted from

  • Joshi, S.; Satyanarayana, T.
    Characteristics and applicability of phytase of the yeast Pichia anomala in synthesizing haloperoxidase (2015), Appl. Biochem. Biotechnol., 176, 1351-1369 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.8 acetone 30% activation at 5% Wickerhamomyces anomalus
3.1.3.8 Benzene 20% activation at 10% Wickerhamomyces anomalus
3.1.3.8 glycerol 20% activation at 5% Wickerhamomyces anomalus
3.1.3.8 hexane 38% activation at 5% Wickerhamomyces anomalus
3.1.3.8 NaN3 30% activation at 10 mM Wickerhamomyces anomalus
3.1.3.8 Thiourea 8% activation at 10 mM Wickerhamomyces anomalus
3.1.3.8 Toluene 39% activation at 5%, 19% at 10% Wickerhamomyces anomalus

Application

EC Number Application Comment Organism
3.1.3.8 agriculture phytase is used as a feed additive for degradation of anti-nutritional phytate, the phytase from Wickerhamomyces anomalus has adequate thermostability for its applicability as a food and feed additive Wickerhamomyces anomalus
3.1.3.8 food industry the phytase from Wickerhamomyces anomalus has adequate thermostability for its applicability as a food and feed additive, applicability of recombinant PPHY in dephytinization of wheat bread, overview Wickerhamomyces anomalus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.B2 gene pphy, sequence comparisons, subcloning in Escherichia coli XL10-Gold cells, expression in Pichia pastoris strain X33, the recombinant enzyme is secreted Wickerhamomyces anomalus
3.1.3.8 gene pphy, sequence comparisons, subcloning in Escherichia coli XL10-Gold cells, expression in Pichia pastoris strain X33, the recombinant enzyme is secreted Wickerhamomyces anomalus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.8 1-butanol 20% inhibition at 10% Wickerhamomyces anomalus
3.1.3.8 2,3-Butanedione strong inhibition at 1-5 mM, complete inhibition at 10 mM Wickerhamomyces anomalus
3.1.3.8 2-mercaptoethanol low inhibition at 1-10 mM Wickerhamomyces anomalus
3.1.3.8 Ag2+ complete inhibition at 5 mM Wickerhamomyces anomalus
3.1.3.8 Al3+ complete inhibition at 5 mM Wickerhamomyces anomalus
3.1.3.8 amyl alcohol complete inhibition at 10% Wickerhamomyces anomalus
3.1.3.8 Ba2+
-
 Wickerhamomyces anomalus
3.1.3.8 chloroform 53% inhibition at 5%, 92% at 10% Wickerhamomyces anomalus
3.1.3.8 CTAB complete inhibition at 1-10 mM Wickerhamomyces anomalus
3.1.3.8 Cu2+ low inhibition at 1-10 mM Wickerhamomyces anomalus
3.1.3.8 diethyldicarbonate complete inhibition at 1-10 mM Wickerhamomyces anomalus
3.1.3.8 ethanol 65% inhibition at 10% Wickerhamomyces anomalus
3.1.3.8 Fe2+
-
 Wickerhamomyces anomalus
3.1.3.8 guanidinium hydrochloride 50% inhibition at 5 mM Wickerhamomyces anomalus
3.1.3.8 Hg2+
-
 Wickerhamomyces anomalus
3.1.3.8 iodoacetate strong inhibition at 5-10 mM Wickerhamomyces anomalus
3.1.3.8 Isopropanol 65-95% inhibition at 5-10%, respetively Wickerhamomyces anomalus
3.1.3.8 L-Tartrate inhibition mechanism, overview Wickerhamomyces anomalus
3.1.3.8 additional information no or poor inhibition by PMSF Wickerhamomyces anomalus
3.1.3.8 N-bromosuccinimide strong inhibition at 1-5 mM, complete inhibition at 10 mM Wickerhamomyces anomalus
3.1.3.8 N-ethylmaleimide low inhibition at 1-10 mM Wickerhamomyces anomalus
3.1.3.8 Pb2+ complete inhibition at 1 mM Wickerhamomyces anomalus
3.1.3.8 SDS complete inhibition at 1-10 mM Wickerhamomyces anomalus
3.1.3.8 Sn2+ complete inhibition at 1 mM Wickerhamomyces anomalus
3.1.3.8 Sodium molybdate strong inhibition at 5-10 mM Wickerhamomyces anomalus
3.1.3.8 Urea complete inhibition at 1-10 mM Wickerhamomyces anomalus
3.1.3.8 vanadate meta-vanadate and ortho-vanadate, exhibits competitive inhibition of phytase, making it bifunctional to act as haloperoxidase. Molecular docking supports vanadate to share its binding site with substrate phytate, molecular docking study and inhibition mechanism, overview. The active site of haloperoxidase shows close similarity with histidine acid phytases. Inhibition of phytase by vanadate can make the enzyme behave as a vanadate-dependent haloperoxidase provided phosphoesterase activity of the enzyme is shut down by the vanadate. The vanadate exists as an anion at pH 3.0 and possibly binds to the active site cleft of phytase, which has a cluster of positively charged amino acids arginine, lysine, and histidine below the isoelectric point (pI) of the enzyme. Upon molecular docking of metavanadate with the rPPHY, it was observed to interact with the same amino acid residues of the catalytic site, with which substrate interacts. Both inhibitor and substrate might sit into the catalytic cleft of the enzyme which is placed between conserved alpha/beta-domain and a variable alpha-domain of rPPHY. When bonding of the substrate/inhibitor was analyzed, it is found to form bonds with arginine (R70), arginine (R74), and aspartate (D344). Inhibition kinetics of phytase by metavanadate Wickerhamomyces anomalus
3.1.3.8 Zn2+
-
 Wickerhamomyces anomalus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.3.8 additional information
-
 additional information Michaelis-Menten kinetics Wickerhamomyces anomalus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.8 Ca2+ activates slightly Wickerhamomyces anomalus
3.1.3.8 additional information no effect by KI, Mn2+, and Na+ at 1-10 mM, poor effect by Co2+ at 1-10 mM Wickerhamomyces anomalus
3.1.3.8 Ni2+ activates slightly Wickerhamomyces anomalus

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 Wickerhamomyces anomalus
-
 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.B2 Wickerhamomyces anomalus D3HIF3 i.e. Pichia anomala or Hansenula anomala
-
3.1.3.8 Wickerhamomyces anomalus D3HIF3 i.e. Pichia anomala or Hansenula anomala
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.B2 recombinant extracellular enzyme from Pichia pastoris strain X33 cell culture medium by lyophilization, anion exchange chromatography, and gel filtration, to homogeneity Wickerhamomyces anomalus
3.1.3.8 recombinant extracellular enzyme from Pichia pastoris strain X33 cell culture medium by lyophilization, anion exchange chromatography, and gel filtration, to homogeneity Wickerhamomyces anomalus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.B2 additional information meta-vanadate and ortho-vanadate, exhibits competitive inhibition of phytase, making it bifunctional to act as haloperoxidase. Molecular docking supports vanadate to share its binding site with substrate phytate, molecular docking study and inhibition mechanism, overview. The active site of haloperoxidase shows close similarity with histidine acid phytases. Inhibition of phytase by vanadate can make the enzyme behave as a vanadate-dependent haloperoxidase provided phosphoesterase activity of the enzyme is shut down by the vanadate. The vanadate exists as an anion at pH 3.0 and possibly binds to the active site cleft of phytase, which has a cluster of positively charged amino acids arginine, lysine, and histidine below the isoelectric point (pI) of the enzyme. Upon molecular docking of metavanadate with the rPPHY, it was observed to interact with the same amino acid residues of the catalytic site, with which substrate interacts. Both inhibitor and substrate might sit into the catalytic cleft of the enzyme which is placed between conserved alpha/beta-domain and a variable alpha-domain of rPPHY. When bonding of the substrate/inhibitor was analyzed, it is found to form bonds with arginine (R70), arginine (R74), and aspartate (D344). Inhibition kinetics of phytase by metavanadate. Inhibition of phytase by metavanadate suggests the applicability of rPPHY as haloperoxidase. The reaction is carried out with KBr, metavanadate, H2O2, and phenol red, while observed intermittently for change in color from red-orange to blue-violet Wickerhamomyces anomalus ?
-
 ?
1.11.1.B2 RH + Cl- + H2O2 + H+
-
 Wickerhamomyces anomalus RCl + 2 H2O
-
 ?
3.1.3.8 additional information vanadate exhibits competitive inhibition of phytase, making it bifunctional to act as haloperoxidase Wickerhamomyces anomalus ?
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
 Wickerhamomyces anomalus 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O i.e. phytate Wickerhamomyces anomalus 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.B2 More cf. EC 3.1.3.8 Wickerhamomyces anomalus
1.11.1.B2 PPHY
-
 Wickerhamomyces anomalus
3.1.3.8 PPHY
-
 Wickerhamomyces anomalus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.11.1.B2 37
-
 assay at Wickerhamomyces anomalus
3.1.3.8 65
-
 assay at Wickerhamomyces anomalus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.3.8 additional information
-
 activation of phytase up to 60°C followed by inactivation at higher temperatures, kinetics overview Wickerhamomyces anomalus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.3.8 70 73 melting temperature of the native phytase is 73°C, while that of the recombinant phytase is 70°C Wickerhamomyces anomalus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.11.1.B2 6
-
 assay at Wickerhamomyces anomalus
3.1.3.8 7
-
 assay at Wickerhamomyces anomalus

General Information

EC Number General Information Comment Organism
1.11.1.B2 additional information three-dimensional model of recombinant PPHY by homology modeling using the crystal structure of phytase chain A from Debaryomyces castellii (PDB ID 2gfiA) as template, inhibitor docking of sodium phytate, vanadate, and tartrate Wickerhamomyces anomalus
3.1.3.8 evolution the phytase of the yeast Pichia anomala is a histidine acid phosphatase based on signature sequences and catalytic amino acids Wickerhamomyces anomalus
3.1.3.8 additional information three-dimensional model of recombinant PPHY by homology modeling using the crystal structure of phytase chain A from Debaryomyces castellii (PDB ID 2gfiA) as template, inhibitor docking of sodium phytate, vanadate, and tartrate Wickerhamomyces anomalus
3.1.3.8 physiological function phytate present in cereals lowers bioavailability of minerals. The reduction of phytic acid content can lead to improvement in mineral availability, and thus mitigate antinutrient effects of phytic acid Wickerhamomyces anomalus