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Literature summary for 3.1.3.2 extracted from

  • Granjeiro, P.A.; Cavagis, A.D.M.; Leite, L.d.C.; Ferreira, C.V.; Granjeiro, J.M.; Aoyama, H.
    The thermal stability of a castor bean seed acid phosphatase (2004), Mol. Cell. Biochem., 266, 11-15.
    View publication on PubMed
Search for more literature for 3.1.3.2

Organism

Organism UniProt Comment Textmining
Ricinus communis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
2100fold to homogeneity from seeds Ricinus communis

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
 Ricinus communis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
230
-
 purified enzyme Ricinus communis

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
AP
-
 Ricinus communis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
 substrate 4-nitrophenyl phosphate Ricinus communis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
-
-
 Ricinus communis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 thermal inactivation of the enzyme is influenced by pH, at pH 3.0 the inactivation is more rapid than at pH 7.0, overview Ricinus communis
50
-
 30 min, 80% remaining activity Ricinus communis
55
-
 30 min, 50% remaining activity Ricinus communis
60
-
 30 min, inactivation Ricinus communis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 assay at Ricinus communis