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Literature summary for 3.1.3.2 extracted from

  • Al-Omair, M.
    Purification and biochemical characterization of acid phosphatase from Vigna aconitifolia (2010), Am. J. Plant Physiol., 5, 361-370.
No PubMed abstract available
Search for more literature for 3.1.3.2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
133
-
 4-nitrophenyl phosphate pH 5.4, 30°C Vigna aconitifolia

Organism

Organism UniProt Comment Textmining
Vigna aconitifolia
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, chromatographic adsorption by DEAE-cellulose and sephadex G200. Protein is purified up to 60fold Vigna aconitifolia

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl phosphate + H2O
-
 Vigna aconitifolia 4-nitrophenol + phosphate
-
 ?
D-fructose 6-phosphate + H2O decreased activity compared to substrate 4-nitrophenyl phosphate Vigna aconitifolia D-fructose + phosphate
-
 ?
sodium phytate + H2O decreased activity compared to substrate 4-nitrophenyl phosphate Vigna aconitifolia ?
-
 ?

Synonyms

Synonyms Comment Organism
acid phosphatase
-
 Vigna aconitifolia

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
 Vigna aconitifolia

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 after 50°C activity decreases continously Vigna aconitifolia

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4
-
-
 Vigna aconitifolia

pH Range

pH Minimum pH Maximum Comment Organism
3.6 5.4 enzyme activity increases gradually Vigna aconitifolia