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Literature summary for 3.1.3.72 extracted from

  • Puhl, A.A.; Greiner, R.; Selinger, L.B.
    A protein tyrosine phosphatase-like inositol polyphosphatase from Selenomonas ruminantium subsp. lactilytica has specificity for the 5-phosphate of myo-inositol hexakisphosphate (2008), Int. J. Biochem. Cell Biol., 40, 2053-2064 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene phyAsrl, DNA and amino acid sequence determination and analysis, phyAsrl is constitutively expressed Selenomonas ruminantium subsp. lactilytica

Organism

Organism UniProt Comment Textmining
Selenomonas ruminantium subsp. lactilytica Q0ZQJ3
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the tyrosine phosphatase (PTP)-like inositol polyphosphatase from Selenomonas ruminantium subsp. lactilytica dephosphorylates myo-inositol hexakisphosphate (Ins P(6)) in vitro preferentially cleaving the 5-phosphate position. Enzyme PhyAsrl has a general specificity for polyphosphorylated myo-inositol substrates, but can also dephosphorylate molecules containing high energy diphosphate bonds in vitro. It can produce Ins(2)P via a highly unique and ordered pathway of sequential dephosphorylation: Ins P(6), Ins(1,2,3,4,6)P(5), D-Ins(1,2,3,6)P(4), Ins(1,2,3)P(3), and D/L-Ins(1,2)P(2) Selenomonas ruminantium subsp. lactilytica ?
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Synonyms

Synonyms Comment Organism
alkaline phytase
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Selenomonas ruminantium subsp. lactilytica
PhyA gene name, UniProt Selenomonas ruminantium subsp. lactilytica
PhyAsrl
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Selenomonas ruminantium subsp. lactilytica
PTP-like phytase UniProt Selenomonas ruminantium subsp. lactilytica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
55
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Selenomonas ruminantium subsp. lactilytica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4.5
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Selenomonas ruminantium subsp. lactilytica