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Literature summary extracted from

  • Li, L.; Xie, T.; Li, H.; Qing, C.; Zhang, G.; Sun, M.
    Enhancing the thermostability of Escherichia coli L-asparaginase II by substitution with Pro in predicted hydrogen-bonded turn structures (2007), Enzyme Microb. Technol., 41, 523-527.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.1
-
 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.1 D178P mutation enhances the thermostability of the enzyme without changing the activity of the enzyme and thus the therapeutical use of L-asparaginase II might be benefit from these result Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.1 5.1
-
 L-asparagine 37°C, pH 8.0, mutant enzyme D178P Escherichia coli
3.5.1.1 5.3
-
 L-asparagine 37°C, pH 8.0, wild-type enzyme Escherichia coli

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.1
-
 Escherichia coli

Storage Stability

EC Number Storage Stability Organism
3.5.1.1 4°C, after 3 weeks, the residual activity of wild-type enzyme decreases more rapidly compared to the D178P. After 5 weeks, wild-type enzyme loses 80% of its activity, the mutant enzyme D178P loses 58% of its activity 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
-
 ?

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.1 60
-
 wild-type enzyme Escherichia coli
3.5.1.1 65
-
 mutant enzyme D178P Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.1 additional information
-
 D178P mutation enhances the thermostability of the enzyme without changing the activity of the enzyme and thus the therapeutical use of L-asparaginase II might be benefit from these result Escherichia coli
3.5.1.1 37
-
 activities of wild-type and mutant enzyme D178P are stable for 0-4 h. Thereafter, the residual activity of wild type decreases rapidly. After 6 h incubation, wild type enzyme loses 35% activity. The mutant D178P loses 19% activity Escherichia coli
3.5.1.1 45
-
 60 min, 97% of activity of mutant enzyme D178P remains, 79% of wild-type activity remains Escherichia coli
3.5.1.1 50
-
 60 min, 90% of activity of mutant enzyme D178P remains, 71% of wild-type activity remains Escherichia coli
3.5.1.1 55
-
 60 min, 72% of activity of mutant enzyme D178P remains, 56% of wild-type activity remains Escherichia coli
3.5.1.1 60
-
 60 min, 52% of activity of mutant enzyme D178P remains, 43% of wild-type activity remains Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.1 0.0027
-
 L-asparagine 37°C, pH 8.0, wild-type enzyme and mutant enzyme D178P Escherichia coli