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Literature summary extracted from

  • Tan, H.; Wu, X.; Xie, L.; Huang, Z.; Peng, W.; Gan, B.
    Identification and characterization of a mesophilic phytase highly resilient to high-temperatures from a fungus-garden associated metagenome (2016), Appl. Microbiol. Biotechnol., 100, 2225-2241 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.8 CTAB 20% activation at 1% w/v Dendroctonus frontalis
3.1.3.8 glycerol activates by 38% at 10% v/v Dendroctonus frontalis
3.1.3.8 additional information no effect by EDTA at 0.1-20 mM Dendroctonus frontalis
3.1.3.8 Tween 20 about 22% and 30% activation at 0.5% and 1% v/v, respectively Dendroctonus frontalis
3.1.3.8 Tween 80 about 27% and 35% activation at 0.5% and 1% v/v, respectively Dendroctonus frontalis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.8 gene phyTX52, phylogenetic analysis, recombinant overexpression of wild-type enzyme in Escherichia coli strain BL21(DE3) Dendroctonus frontalis

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.8 E378A/D128A/D71A/E443A site-directed mutagenesis, mutant rPhyXT52:DELTASB1,3,6,7 with loss of four salt bridges Dendroctonus frontalis
3.1.3.8 E378A/D178A site-directed mutagenesis, mutant rPhyXT52:DELTASB1,5 with loss of two salt bridges Dendroctonus frontalis
3.1.3.8 E378A/R56A/D128A/D267A/D178A/D71A/E443A site-directed mutagenesis, mutant rPhyXT52:DELTASB1-7 with loss of seven salt bridges Dendroctonus frontalis
3.1.3.8 E378A/R56A/D267A/E443A site-directed mutagenesis, mutant rPhyXT52:DELTASB1,2,4,7 with loss of four salt bridges Dendroctonus frontalis
3.1.3.8 additional information construction of mutants that lose salt bridges through the mutations, the combinations of the disabled salt bridges are randomly selected. The mutants show reduced melting temperatures and reduced optimum reaction temperature compared to wild-type rPhyXT52, overview Dendroctonus frontalis
3.1.3.8 R56A/D128A site-directed mutagenesis, mutant rPhyXT52:DELTASB2,3 with loss of two salt bridges Dendroctonus frontalis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.8 2-mercaptoethanol 20% inhibition at 1 mM, 66% at 5 mM Dendroctonus frontalis
3.1.3.8 Ag+ about 40% inhibition at 1 mM, 82% at 5 mM Dendroctonus frontalis
3.1.3.8 Al3+ 67% inhibition at 1 mM, 88% at 5 mM Dendroctonus frontalis
3.1.3.8 Ba2+ about 60% inhibition at 1 mM, 83% at 5 mM Dendroctonus frontalis
3.1.3.8 Ca2+ slightly elevates the phytase activity at 20 mM but inhibits the activity at a higher concentration of 50 mM Dendroctonus frontalis
3.1.3.8 Cd2+ 92.5% inhibition at 1 mM Dendroctonus frontalis
3.1.3.8 citrate slight inhibition at 20-100 mM Dendroctonus frontalis
3.1.3.8 Co2+ about 69% inhibition at 1 mM, 83% at 5 mM Dendroctonus frontalis
3.1.3.8 Cr3+ 87% inhibition at 1 mM Dendroctonus frontalis
3.1.3.8 Cu2+ 72% inhibition at 5 mM Dendroctonus frontalis
3.1.3.8 DTT 23% inhibition at 1 mM, 88% at 5 mM Dendroctonus frontalis
3.1.3.8 Fe2+ 9% inhibition at 5 mM Dendroctonus frontalis
3.1.3.8 glycerol inhibits by 14% at 20% v/v Dendroctonus frontalis
3.1.3.8 Mg2+ has no significant influence at low concentrations of 1 and 5 mM and inhibits the phytase activity at high concentrations of 20 and 50 mM Dendroctonus frontalis
3.1.3.8 Mn2+ 67% inhibition at 5 mM Dendroctonus frontalis
3.1.3.8 additional information no effect by EDTA at 0.1-20 mM Dendroctonus frontalis
3.1.3.8 Ni2+ about 55% inhibition at 1 mM, 78% at 5 mM Dendroctonus frontalis
3.1.3.8 Pb2+ 94% inhibition at 1 mM, almost complete inhibition at 5 mM Dendroctonus frontalis
3.1.3.8 PMSF 44% inhibition at 2 mM Dendroctonus frontalis
3.1.3.8 SDS 73% inhibition at 0.1% w/v, 85% at 0.5% w/v, and 94% at 2% w/v Dendroctonus frontalis
3.1.3.8 Triton-X-100 12% inhibition at 0.5% v/v, 37% at 1% v/v Dendroctonus frontalis
3.1.3.8 Urea 30% inhibition at 2 M, 44% at 4 M Dendroctonus frontalis
3.1.3.8 Zn2+ 53% inhibition at 5 mM Dendroctonus frontalis

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 Dendroctonus frontalis
3.1.3.8 0.262
-
 myo-inositol hexakisphosphate recombinant enzyme, pH 3.9, 52.5°C Dendroctonus frontalis
3.1.3.8 0.326
-
 myo-inositol hexakisphosphate recombinant enzyme, pH 3.9, 37°C Dendroctonus frontalis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.8 Ca2+ slightly elevates the phytase activity at 20 mM but inhibits the activity at a higher concentration of 50 mM Dendroctonus frontalis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.8 51700
-
 recombinant enzyme, gel filtration Dendroctonus frontalis

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 Dendroctonus frontalis highly preferred substrate 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Dendroctonus frontalis KM873028
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.8 recombinant enzyme from Escherichia coli strain BL21(DE3) Dendroctonus frontalis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.3.8 4175
-
 purified recombinant enzyme, pH 3.9, 52.5°C Dendroctonus frontalis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.8 additional information enzyme rPhysXT52 shows nonspecific phosphohydrolytic activity with 4-nitrophenyl phosphate, 1-naphthyl phosphate, 2-naphthyl phosphate, phenyl phosphate, 2-glycerophosphate, glucose-6-phosphate, fructose-6-phosphate, fructose-1,6-diphosphate, AMP, ADP, ATP, and NADP+, overview Dendroctonus frontalis ?
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
 Dendroctonus frontalis 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O highly preferred substrate Dendroctonus frontalis 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.8 monomer 1 * 52000, recombinant enzyme, SDS-PAGE Dendroctonus frontalis

Synonyms

EC Number Synonyms Comment Organism
3.1.3.8 PhyTX52
-
 Dendroctonus frontalis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.8 52.5
-
-
 Dendroctonus frontalis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.3.8 60 100 purified recombinant enzyme, half-life at 60, 80, and 100°C is approximate 5.6 h, 2.1 h, and 27 min, respectively. At 80°C, recombinant PhyXT52 retains about 90% residual activity after 20 min, and at 100°C more than 93% residual activity are retained after 15 min and over 83% after 20 min. Melting temperatures of wild-type rPhyXT52 and mutant enzymes rPhyXT52:DELTASB1,5, rPhyXT52:DELTASB2,3, rPhyXT52:DELTASB1,2,4,7, rPhyXT52:DELTASB1,3,6,7, rPhyXT52:DELTASB1-7 are 60.5°C, 58.2°C; 59.7°C; 54.6°C, 55.2°C, and 52.8°C. Half-lifes of mutants are determined at 60-100°C, overview Dendroctonus frontalis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.1.3.8 284600
-
 myo-inositol hexakisphosphate recombinant enzyme, pH 3.9, 37°C Dendroctonus frontalis
3.1.3.8 375200
-
 myo-inositol hexakisphosphate recombinant enzyme, pH 3.9, 52.5°C Dendroctonus frontalis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.8 3.9
-
 recombinant enzyme Dendroctonus frontalis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.3.8 3 6 activity range, mesophilic phytase, profile overview Dendroctonus frontalis

General Information

EC Number General Information Comment Organism
3.1.3.8 evolution the enzyme belongs to the histidine acid phosphatase (HAP) family phytases present in insect-cultivated fungus gardens Dendroctonus frontalis
3.1.3.8 additional information structural model of rPhyXT52 is deduced by homology modeling using the Yersinia kristensenii phytase (PDB ID 4ARV) structure as template, overview Dendroctonus frontalis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.1.3.8 873006
-
 myo-inositol hexakisphosphate recombinant enzyme, pH 3.9, 37°C Dendroctonus frontalis
3.1.3.8 1432060
-
 myo-inositol hexakisphosphate recombinant enzyme, pH 3.9, 52.5°C Dendroctonus frontalis