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Literature summary for 3.1.3.2 extracted from

  • Hamilton, A.; Harrington, D.; Sutcliffe, I.C.
    Characterization of acid phosphatase activities in the equine pathogen Streptococcus equi (2000), Syst. Appl. Microbiol., 23, 325-329.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
EDTA two acid phosphatases: one has a pH-optimum at pH 5.0 and is resistant to EDTA, the other has a pH-optimum at pH 6.0-6.5 and is sensitive to EDTA Streptococcus equi
additional information both acid phosphatases are resistant to tartrate and Triton X-100 Streptococcus equi

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
x * 32000, SDS-PAGE Streptococcus equi

Organism

Organism UniProt Comment Textmining
Streptococcus equi Q9L2M4 subsp. equi and subsp. zooepidemicus
-

Posttranslational Modification

Posttranslational Modification Comment Organism
lipoprotein surface accessible lipoprotein Streptococcus equi

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
Streptococcus equi 4-nitrophenol + phosphate
-
?

Subunits

Subunits Comment Organism
? x * 32000, SDS-PAGE Streptococcus equi

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
two acid phosphatases: one has a pH-optimum at pH 5.0 and is resistant to EDTA, the other has a pH-optimum at pH 6.0-6.5 and is sensitive to EDTA Streptococcus equi
6 6.5 two acid phosphatases: one has a pH-optimum at pH 5.0 and is resistant to EDTA, the other has a pH-optimum at pH 6.0-6.5 and is sensitive to EDTA Streptococcus equi