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Literature summary extracted from

  • Zhang, Y.Q.; Tao, M.L.; Shen, W.D.; Zhou, Y.Z.; Ding, Y.; Ma, Y.; Zhou, W.L.
    Immobilization of L-asparaginase on the microparticles of the natural silk sericin protein and its characters (2004), Biomaterials, 25, 3751-3759.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.1.1 medicine L-asparaginase is an anti-leukemic enzyme Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.1 additional information covalent immobilization of L-asparaginase on poorly soluble microparticles of the natural silk sericin protein, MW 50-200 kDa, from Bomby mori, best at 0.15% glutaraldehyde in 50 mM citrate buffer, pH 8.6, method optimization and biochemical properties of the enzyme-conjugate, overview Escherichia coli

General Stability

EC Number General Stability Organism
3.5.1.1 half-life of immobilized enzyme at 37°C, pH 8.6 is 8 days Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.1 Glutaraldehyde inhibits the enzyme during immobilization at concentrations above 0.2% Escherichia coli
3.5.1.1 Trypsin the free enzyme is completely inactivated by trypsin within 10 min, while the immobilized enzyme is stable for 240 min with loss of 30% activity Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.1 additional information
-
additional information the Km of the immobilized enzyme is 8fold lower compared to the free enzyme Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.1 138000 141000
-
Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.1 L-asparagine + H2O Escherichia coli
-
L-aspartate + NH3
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 Escherichia coli
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.1 commercial preparation
-
Escherichia coli
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.1 L-asparagine + H2O
-
Escherichia coli L-aspartate + NH3
-
?

Subunits

EC Number Subunits Comment Organism
3.5.1.1 tetramer homotetramer with one active center Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
3.5.1.1 L-ASNase
-
Escherichia coli
3.5.1.1 L-asparaginase
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.1 50
-
free enzyme Escherichia coli
3.5.1.1 60
-
immobilized enzyme Escherichia coli

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.5.1.1 30 80 immobilized enzyme, 60% of maximal activity at 70°C Escherichia coli
3.5.1.1 30 60 free enzyme, inactivation at 70°C Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.1 50
-
30 min, about 20% reduced activity, immobilized enzyme and free enzyme Escherichia coli
3.5.1.1 60
-
30 min, about 70% reduced activity, immobilized enzyme and free enzyme Escherichia coli
3.5.1.1 70
-
30 min, about 80% reduced activity, immobilized enzyme and free enzyme Escherichia coli
3.5.1.1 80
-
30 min, inactivation of immobilized enzyme and free enzyme Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.1 8.6
-
assay at, immobilized and free enzyme Escherichia coli