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Literature summary for 3.1.3.8 extracted from

  • Li, Z.; Huang, H.; Yang, P.; Yuan, T.; Shi, P.; Zhao, J.; Meng, K.; Yao, B.
    The tandemly repeated domains of a beta-propeller phytase act synergistically to increase catalytic efficiency (2011), FEBS J., 278, 3032-3040.
    View publication on PubMed
Search for more literature for 3.1.3.8

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged enzyme domains PhyH, PhyH-DI, and PhyH-DII in Escherichia coli strain BL21 (DE3) Bacillus sp. (in: Bacteria)

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.191
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate phytase domain Phy-DI fused to beta-propeller phytase 168PhyA, pH 7.0, 55°C Bacillus sp. (in: Bacteria)
0.24
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate beta-propeller phytase 168PhyA, pH 7.0, 55°C Bacillus sp. (in: Bacteria)
0.5
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate dual domain phytase PhyH, pH 7.0, 35°C Bacillus sp. (in: Bacteria)
1.086
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate phytase domain Phy-DI fused to beta-propeller phytase PhyP, pH 7.0, 37°C Bacillus sp. (in: Bacteria)
1.28
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate beta-propeller phytase PhyP, pH 7.0, 37°C Bacillus sp. (in: Bacteria)
1.432
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate phytase domain Phy-DII, pH 7.0, 35°C Bacillus sp. (in: Bacteria)

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ the purified recombinant enzyme domains PhyH and PhyH-DII require Ca2+ for phytase activity, optimal at 1 mM Bacillus sp. (in: Bacteria)

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O Bacillus sp. (in: Bacteria)
-
 ? + phosphate
-
 ?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O Bacillus sp. (in: Bacteria) HJB17
-
 ? + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
 gene phyH
-
Bacillus sp. (in: Bacteria) HJB17
-
 gene phyH
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme domains PhyH, PhyH-DI, and PhyH-DII from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography Bacillus sp. (in: Bacteria)

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.82
-
 functional domain Phyd-DII, myo-inositol-1,2,3,4,5,6-hexakisphosphate as substrate, pH 7.0, 35°C Bacillus sp. (in: Bacteria)
4.43
-
 dual domain PhyH, myo-inositol-1,2,3,4,5,6-hexakisphosphate as substrate, pH 7.0, 35°C Bacillus sp. (in: Bacteria)
13.01
-
 beta-propeller phytase 168PhyA, myo-inositol-1,2,3,4,5,6-hexakisphosphate as substrate, pH 7.0, 55°C Bacillus sp. (in: Bacteria)
14.87
-
 incomplete domain Phyd-DI fused to beta-propeller phytase 168PhyA, myo-inositol-1,2,3,4,5,6-hexakisphosphate as substrate, pH 7.0, 55°C Bacillus sp. (in: Bacteria)
21.61
-
 beta-propeller phytase PhyP, myo-inositol-1,2,3,4,5,6-hexakisphosphate as substrate, pH 7.0, 37°C Bacillus sp. (in: Bacteria)
29.82
-
 incomplete domain Phyd-DI fused to beta-propeller phytase PhyP, myo-inositol-1,2,3,4,5,6-hexakisphosphate as substrate, pH 7.0, 37°C Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate specificity of the incomplete domain and the functional relationship of tandemly repeated domains in beta-propeller phytases. The incomplete domain Phy-DI is not functional with myo-inositol-1,2,3,4,5,6-hexakisphosphate at 35°C and pH 7.0 Bacillus sp. (in: Bacteria) ?
-
 ?
additional information substrate specificity of the incomplete domain and the functional relationship of tandemly repeated domains in beta-propeller phytases. The incomplete domain Phy-DI is not functional with myo-inositol-1,2,3,4,5,6-hexakisphosphate at 35°C and pH 7.0 Bacillus sp. (in: Bacteria) HJB17 ?
-
 ?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
-
 Bacillus sp. (in: Bacteria) ? + phosphate
-
 ?
myo-inositol-1,2,3,4,5,6-hexakisphosphate + H2O
-
 Bacillus sp. (in: Bacteria) HJB17 ? + phosphate
-
 ?

Subunits

Subunits Comment Organism
More the dual-domain beta-propeller phytase PhyH from Bacillus sp. HJB17 contains an incomplete N-terminal beta-propeller phytase domain, PhyH-DI, residues 41-318, and a typical beta-propeller phytase domain, PhyH-DII, residues 319-644, at the C-terminus. Modelling of the three-dimensional structures of domains PhyH-DI and PhyH-DII, PhyH-DI is predicted to have a five-blade propeller structure and PhyH-DII a six-blade beta-propeller containing five four-stranded sheets and one five-stranded sheet Bacillus sp. (in: Bacteria)

Synonyms

Synonyms Comment Organism
168phyA
-
 Bacillus sp. (in: Bacteria)
beta-propeller phytase
-
 Bacillus sp. (in: Bacteria)
BPP
-
 Bacillus sp. (in: Bacteria)
dual-domain BPP
-
 Bacillus sp. (in: Bacteria)
PhyH
-
 Bacillus sp. (in: Bacteria)
PhyP
-
 Bacillus sp. (in: Bacteria)

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 dual domain phytase PhyH and intact domain Phy-DII Bacillus sp. (in: Bacteria)
55
-
 domain Phy-DI fused to beta-propeller phytases PhyP and 168PhyA Bacillus sp. (in: Bacteria)

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
-
 37 purified recombinant enzyme domains PhyH and PhyH-DII Bacillus sp. (in: Bacteria)

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
20 45 purified recombinant enzyme domains PhyH and PhyH-DII, stable up to for 30 min Bacillus sp. (in: Bacteria)
60
-
 purified recombinant enzyme domains PhyH and PhyH-DII, about 80% of maximal activity remaining after 30 min in presence of 10 mM Ca2+, 50% at 1 mM Ca2+, and 20% without Ca2+ Bacillus sp. (in: Bacteria)

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.17
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate phytase domain Phy-DII, pH 7.0, 35°C Bacillus sp. (in: Bacteria)
5.92
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate beta-propeller phytase 168PhyA, pH 7.0, 55°C Bacillus sp. (in: Bacteria)
12.28
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate phytase domain Phy-DI fused to beta-propeller phytase 168PhyA, pH 7.0, 55°C Bacillus sp. (in: Bacteria)
27.72
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate dual domain phytase PhyH, pH 7.0, 35°C Bacillus sp. (in: Bacteria)
44.94
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate beta-propeller phytase PhyP, pH 7.0, 37°C Bacillus sp. (in: Bacteria)
94.4
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate phytase domain Phy-DI fused to beta-propeller phytase PhyP, pH 7.0, 37°C Bacillus sp. (in: Bacteria)

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Bacillus sp. (in: Bacteria)

pH Range

pH Minimum pH Maximum Comment Organism
6 8 purified recombinant enzyme domains PhyH and PhyH-DII Bacillus sp. (in: Bacteria)

General Information

General Information Comment Organism
evolution dual-domain beta-propeller phytases have succeeded evolutionarily because they can increase the amount of available phosphate by interacting together Bacillus sp. (in: Bacteria)
additional information the tandemly repeated domains of a beta-propeller phytase act synergistically to increase catalytic efficiency. The intact domain is responsible for phytate hydrolysis. Enzyme domain PhyH-DI also hydrolyzes the phytate intermediate D-Ins(1,4,5,6)P4, and acts synergistically, causing a 1.2-2.5fold increase in phosphate release, with domain PhyH-DII, other beta-propeller phytases, PhyP and 168PhyA, and a histidine acid phosphatase. Fusion of PhyH-DI with PhyP or 168PhyA significantly enhanced their catalytic efficiencies Bacillus sp. (in: Bacteria)
physiological function importance of enzyme domain PhyH-DI in phytate degradation Bacillus sp. (in: Bacteria)

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
 additional information the tandemly repeated domains of a beta-propeller phytase act synergistically to increase catalytic efficiency, fusion of domain PhyH-DI with PhyP or 168PhyA significantly enhanced their catalytic efficiencies Bacillus sp. (in: Bacteria)
2.9
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate phytase domain Phy-DII, pH 7.0, 35°C Bacillus sp. (in: Bacteria)
35
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate beta-propeller phytase PhyP, pH 7.0, 37°C Bacillus sp. (in: Bacteria)
54
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate dual domain phytase PhyH, pH 7.0, 35°C Bacillus sp. (in: Bacteria)
87
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate phytase domain Phy-DI fused to beta-propeller phytase PhyP, pH 7.0, 37°C Bacillus sp. (in: Bacteria)
250
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate beta-propeller phytase 168PhyA, pH 7.0, 55°C Bacillus sp. (in: Bacteria)
640
-
 myo-inositol-1,2,3,4,5,6-hexakisphosphate phytase domain Phy-DI fused to beta-propeller phytase 168PhyA, pH 7.0, 55°C Bacillus sp. (in: Bacteria)