Literature summary for 3.1.3.8 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 .

Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
E153R	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
E230A	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
E230D	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
E230G	site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia enterocolitica
E230G	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
E230K	site-directed mutagenesis, the mutant shows reduced catalytic activity and thermal stability compared to the wild-type enzyme	Yersinia kristensenii
E230P	site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia enterocolitica
E230P	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
E230R	site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia enterocolitica
E230S	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
E230T	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
L162A	site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia enterocolitica
L162A	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
L162G	site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia enterocolitica
L162G	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
L162V	site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia enterocolitica
L162V	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
L99A	site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia enterocolitica
L99A	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
L99A/L162G	site-directed mutagenesis, the mutant shows highly reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia enterocolitica
L99A/L162G	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
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
L99A/L162G/L230G	site-directed mutagenesis, the mutant shows reduced catalytic activity but increased thermal stability compared to the wild-type enzyme	Yersinia kristensenii
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
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

Inhibitors

Inhibitors	Comment	Organism	Structure
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
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

Natural Substrates/ Products (Substrates)

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

Organism	UniProt	Comment	Textmining
Yersinia enterocolitica	D9D7K9	-	-
Yersinia kristensenii	B6RGT1	-	-

Purification (Commentary)

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

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
additional information	the ferrous sulfate-molybdenum blue method is used for enzyme activity detection	Yersinia enterocolitica	?	-	?
additional information	the ferrous sulfate-molybdenum blue method is used for enzyme activity detection	Yersinia kristensenii	?	-	?
myo-inositol hexakisphosphate + H2O	-	Yersinia enterocolitica	1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate	-	?
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

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

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Yersinia enterocolitica
37	-	assay at	Yersinia kristensenii

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4.5	-	assay at	Yersinia enterocolitica
4.5	-	assay at	Yersinia kristensenii

General Information

General Information	Comment	Organism
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