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Literature summary for 3.1.3.48 extracted from

  • Tsuruta, H.; Aizono, Y.
    Catalytic efficiency and some structural properties of cold-active protein-tyrosine-phosphatase (2003), J. Biochem., 133, 225-230.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.28
-
4-nitrophenyl phosphate pH 7.8, 18°C Shewanella sp.
0.6
-
4-nitrophenyl phosphate pH 7.8, 25°C Shewanella sp.
1.18
-
4-nitrophenyl phosphate pH 7.8, 2°C Shewanella sp.

Organism

Organism UniProt Comment Textmining
Shewanella sp.
-
psychrophilic microorganism, recombinant enzyme
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Shewanella sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
thermodynamic parameters of enzyme Shewanella sp.
73.3
-
pH 7.8, 25°C Shewanella sp.

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
Shewanella sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
-
15 10.8-33.2% of the activity at the optimal temperature Shewanella sp.