Literature summary for 1.11.1.B2 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 .

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Cloned(Commentary)

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

Organism

Organism	UniProt	Comment	Textmining
Wickerhamomyces anomalus	D3HIF3	i.e. Pichia anomala or Hansenula anomala	-

Purification (Commentary)

Purification (Comment)	Organism
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)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	?	-	?
RH + Cl- + H2O2 + H+	-	Wickerhamomyces anomalus	RCl + 2 H2O	-	?

Synonyms

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

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Wickerhamomyces anomalus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6	-	assay at	Wickerhamomyces anomalus

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)