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Literature summary for 3.5.1.1 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
Search for more literature for 3.5.1.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
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]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Storage Stability

Storage Stability Organism
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)

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

Synonyms

Synonyms Comment Organism
L-asparaginase II
-
 Escherichia coli

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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
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
45
-
 60 min, 97% of activity of mutant enzyme D178P remains, 79% of wild-type activity remains Escherichia coli
50
-
 60 min, 90% of activity of mutant enzyme D178P remains, 71% of wild-type activity remains Escherichia coli
55
-
 60 min, 72% of activity of mutant enzyme D178P remains, 56% of wild-type activity remains Escherichia coli
60
-
 60 min, 52% of activity of mutant enzyme D178P remains, 43% of wild-type activity remains Escherichia coli

Turnover Number [1/s]

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