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Literature summary extracted from

  • Niu, C.; Yang, P.; Luo, H.; Huang, H.; Wang, Y.; Yao, B.
    Engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency (2017), Sci. Rep., 7, 42133 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.8 gene appA, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Yersinia enterocolitica
3.1.3.8 gene appA, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Yersinia kristensenii
3.1.3.26 gene appA, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Yersinia rohdei
3.1.3.26 gene appA, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Yersinia kristensenii

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.8 E153R site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 E230A site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 E230D site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 E230G site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia enterocolitica
3.1.3.8 E230G site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 E230K site-directed mutagenesis, the mutant shows reduced catalytic activity and thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 E230P site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia enterocolitica
3.1.3.8 E230P site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 E230R site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia enterocolitica
3.1.3.8 E230S site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 E230T site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 L162A site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia enterocolitica
3.1.3.8 L162A site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 L162G site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia enterocolitica
3.1.3.8 L162G site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 L162V site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia enterocolitica
3.1.3.8 L162V site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 L99A site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia enterocolitica
3.1.3.8 L99A site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 L99A/L162G site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia enterocolitica
3.1.3.8 L99A/L162G site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 L99A/L162G/L230G site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia enterocolitica
3.1.3.8 L99A/L162G/L230G site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.8 additional information engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview Yersinia enterocolitica
3.1.3.8 additional information engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview Yersinia kristensenii
3.1.3.26 E153R site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 E230A site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 E230D site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 E230G site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 E230K site-directed mutagenesis, the mutant shows reduced catalytic activity and thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 E230P site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 E230S site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 E230T site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 L162A site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 L162G site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 L162V site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 L99A site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 L99A/L162G site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 L99A/L162G/L230G site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme Yersinia kristensenii
3.1.3.26 additional information engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview Yersinia rohdei
3.1.3.26 additional information engineering the residual side chains of HAP phytases to improve their pepsin resistance and catalytic efficiency. Proteolytic resistance of wild-type and mutant phytases, overview Yersinia kristensenii
3.1.3.26 V162L site-directed mutagenesis, the mutant shows increased sensitivity to pepsin in contrast to the less sensitive wild-type enzyme Yersinia rohdei

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.8 additional information when treated with trypsin in 0.25 M Tris-HCl (pH 7.0) for 2 h, the enzyme mutant E230R of YeAPPA retains less activity than the wild-type at ratios ranging from 1/1000 to 1/1 and 1/200 to 1/1, but the activity in the other mutants is similar to the wild-type at the various ratios. Residues at positions 99, 162, and 230 in Yersinia phytases play a major role in pepsin resistance, especially position 230 Yersinia enterocolitica
3.1.3.8 additional information when treated with trypsin in 0.25 M Tris-HCl (pH 7.0) for 2 h, the enzyme mutants E230K and E230R of YkAPPA retain less activity than the wild-type at ratios ranging from 1/1000 to 1/1 and 1/200 to 1/1, but the activity in the other mutants is similar to the wild-type at the various ratios. Residues at positions 99, 162, and 230 in Yersinia phytases play a major role in pepsin resistance, especially position 230 Yersinia kristensenii
3.1.3.26 additional information when treated with trypsin in 0.25 M Tris-HCl (pH 7.0) for 2 h, the enzyme mutants E230K and E230R of YkAPPA retain less activity than the wild-type at ratios ranging from 1/1000 to 1/1 and 1/200 to 1/1, but the activity in the other mutants is similar to the wild-type at the various ratios. Residues at positions 99, 162, and 230 in Yersinia phytases play a major role in pepsin resistance, especially position 230 Yersinia kristensenii
3.1.3.26 additional information the mutant V162L shows increased sensitivity to cleavage by pepsin (loss of 73% activity) compared to the wild-type (loss of 35% activity), while the sensitivity to trypsin is unaltered. Residues at positions 99, 162, and 230 in Yersinia phytases play a major role in pepsin resistance, especially position 230 Yersinia rohdei

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 Yersinia enterocolitica
-
 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O Yersinia kristensenii phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 1D-myo-inositol pentakisphosphate + phosphate
-
 ?
3.1.3.26 myo-inositol hexakisphosphate + H2O Yersinia rohdei
-
 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
-
 ?
3.1.3.26 myo-inositol hexakisphosphate + H2O Yersinia kristensenii phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 1D-myo-inositol pentakisphosphate + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.8 Yersinia enterocolitica D9D7K9
-
-
3.1.3.8 Yersinia kristensenii B6RGT1
-
-
3.1.3.26 Yersinia kristensenii B6RGT1
-
-
3.1.3.26 Yersinia rohdei B4X9S4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.3.8 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography Yersinia enterocolitica
3.1.3.8 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography Yersinia kristensenii
3.1.3.26 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography Yersinia rohdei
3.1.3.26 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography Yersinia kristensenii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.8 additional information the ferrous sulfate-molybdenum blue method is used for enzyme activity detection Yersinia enterocolitica ?
-
 ?
3.1.3.8 additional information the ferrous sulfate-molybdenum blue method is used for enzyme activity detection Yersinia kristensenii ?
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O
-
 Yersinia enterocolitica 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
-
 ?
3.1.3.8 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Yersinia kristensenii 1D-myo-inositol pentakisphosphate + phosphate
-
 ?
3.1.3.26 additional information the ferrous sulfate-molybdenum blue method is used for enzyme activity detection Yersinia rohdei ?
-
 ?
3.1.3.26 additional information the ferrous sulfate-molybdenum blue method is used for enzyme activity detection Yersinia kristensenii ?
-
 ?
3.1.3.26 myo-inositol hexakisphosphate + H2O
-
 Yersinia rohdei 1D-myo-inositol 1,2,3,5,6-pentakisphosphate + phosphate
-
 ?
3.1.3.26 myo-inositol hexakisphosphate + H2O phosphate cleavage position is not determined, cf. EC 3.1.3.8 and 3.1.3.26 Yersinia kristensenii 1D-myo-inositol pentakisphosphate + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.8 AppA
-
 Yersinia enterocolitica
3.1.3.8 AppA
-
 Yersinia kristensenii
3.1.3.8 HAP phytase
-
 Yersinia enterocolitica
3.1.3.8 HAP phytase
-
 Yersinia kristensenii
3.1.3.8 More cf. EC 3.1.3.26 Yersinia kristensenii
3.1.3.8 YeAPPA
-
 Yersinia enterocolitica
3.1.3.8 YkAPPA
-
 Yersinia kristensenii
3.1.3.26 AppA
-
 Yersinia rohdei
3.1.3.26 AppA
-
 Yersinia kristensenii
3.1.3.26 HAP phytase
-
 Yersinia rohdei
3.1.3.26 HAP phytase
-
 Yersinia kristensenii
3.1.3.26 More cf. EC 3.1.3.8 Yersinia kristensenii
3.1.3.26 YkAPPA
-
 Yersinia kristensenii
3.1.3.26 YrAPPA
-
 Yersinia rohdei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.3.8 37
-
 assay at Yersinia enterocolitica
3.1.3.8 37
-
 assay at Yersinia kristensenii
3.1.3.26 37
-
 assay at Yersinia rohdei
3.1.3.26 37
-
 assay at Yersinia kristensenii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.3.8 4.5
-
 assay at Yersinia enterocolitica
3.1.3.8 4.5
-
 assay at Yersinia kristensenii
3.1.3.26 4.5
-
 assay at Yersinia rohdei
3.1.3.26 4.5
-
 assay at Yersinia kristensenii

General Information

EC Number General Information Comment Organism
3.1.3.8 additional information catalytic center structures of wild-type YkAPPA and its mutants E230G and L162G, catalytic sites are catalytic sites R44, R48, D115, R119, H333, and D334, overview Yersinia kristensenii
3.1.3.26 additional information catalytic center structures of wild-type YkAPPA and its mutants E230G and L162G, catalytic sites are R44, R48, D115, R119, H333, and D334, overview Yersinia kristensenii