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Literature summary for 3.1.3.2 extracted from

  • Jonsson, I.
    Acid phosphatase from needles of Pinus silvestris L. Purification of two interconvertible enzyme forms and characterization of a low-molecular weight factor associated with the enzyme (1981), Biochim. Biophys. Acta, 660, 204-213.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6
-
p-nitrophenyl phosphate
-
Pinus sylvestris

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
68000
-
gel filtration Pinus sylvestris

Organism

Organism UniProt Comment Textmining
Pinus sylvestris
-
-
-

Purification (Commentary)

Purification (Comment) Organism
2 interconvertible enzyme forms, the acid enzyme form is probably a complex between and basic form and an oligoribonucleotide factor Pinus sylvestris

Source Tissue

Source Tissue Comment Organism Textmining
needle
-
Pinus sylvestris
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Pinus sylvestris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
p-nitrophenyl phosphate + H2O
-
Pinus sylvestris p-nitrophenol + phosphate
-
?

Subunits

Subunits Comment Organism
monomer 1 * 68000, SDS-PAGE Pinus sylvestris
More 2 interconvertible enzyme forms, the acid enzyme form is probably a complex between and basic form and an oligoribonucleotide factor Pinus sylvestris