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Literature summary for 3.1.3.8 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
Search for more literature for 3.1.3.8

Activating Compound

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

Application

Application Comment Organism
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
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)

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

Inhibitors

Inhibitors Comment Organism Structure
1-butanol 20% inhibition at 10% Wickerhamomyces anomalus
2,3-Butanedione strong inhibition at 1-5 mM, complete inhibition at 10 mM Wickerhamomyces anomalus
2-mercaptoethanol low inhibition at 1-10 mM Wickerhamomyces anomalus
Ag2+ complete inhibition at 5 mM Wickerhamomyces anomalus
Al3+ complete inhibition at 5 mM Wickerhamomyces anomalus
amyl alcohol complete inhibition at 10% Wickerhamomyces anomalus
Ba2+
-
 Wickerhamomyces anomalus
chloroform 53% inhibition at 5%, 92% at 10% Wickerhamomyces anomalus
CTAB complete inhibition at 1-10 mM Wickerhamomyces anomalus
Cu2+ low inhibition at 1-10 mM Wickerhamomyces anomalus
diethyldicarbonate complete inhibition at 1-10 mM Wickerhamomyces anomalus
ethanol 65% inhibition at 10% Wickerhamomyces anomalus
Fe2+
-
 Wickerhamomyces anomalus
guanidinium hydrochloride 50% inhibition at 5 mM Wickerhamomyces anomalus
Hg2+
-
 Wickerhamomyces anomalus
iodoacetate strong inhibition at 5-10 mM Wickerhamomyces anomalus
Isopropanol 65-95% inhibition at 5-10%, respetively Wickerhamomyces anomalus
L-Tartrate inhibition mechanism, overview Wickerhamomyces anomalus
additional information no or poor inhibition by PMSF Wickerhamomyces anomalus
N-bromosuccinimide strong inhibition at 1-5 mM, complete inhibition at 10 mM Wickerhamomyces anomalus
N-ethylmaleimide low inhibition at 1-10 mM Wickerhamomyces anomalus
Pb2+ complete inhibition at 1 mM Wickerhamomyces anomalus
SDS complete inhibition at 1-10 mM Wickerhamomyces anomalus
Sn2+ complete inhibition at 1 mM Wickerhamomyces anomalus
Sodium molybdate strong inhibition at 5-10 mM Wickerhamomyces anomalus
Urea complete inhibition at 1-10 mM Wickerhamomyces anomalus
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
Zn2+
-
 Wickerhamomyces anomalus

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
myo-inositol hexakisphosphate + H2O Wickerhamomyces anomalus
-
 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?

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 vanadate exhibits competitive inhibition of phytase, making it bifunctional to act as haloperoxidase Wickerhamomyces anomalus ?
-
 ?
myo-inositol hexakisphosphate + H2O
-
 Wickerhamomyces anomalus 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?
myo-inositol hexakisphosphate + H2O i.e. phytate Wickerhamomyces anomalus 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
PPHY
-
 Wickerhamomyces anomalus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
 assay at Wickerhamomyces anomalus

Temperature Range [°C]

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Wickerhamomyces anomalus

General Information

General Information Comment Organism
evolution the phytase of the yeast Pichia anomala is a histidine acid phosphatase based on signature sequences and catalytic amino acids Wickerhamomyces anomalus
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
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