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Literature summary for 3.5.1.1 extracted from

  • Feng, Y.; Liu, S.; Jiao, Y.; Wang, Y.; Wang, M.; Du, G.; Chen, J.
    Improvement of L-asparaginase thermal stability by regulating enzyme kinetic and thermodynamic states (2018), Process Biochem., 71, 45-52 .
No PubMed abstract available
Search for more literature for 3.5.1.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
D289T highly stabilized mutant Bacillus subtilis
E260F thermodynamically stabilized mutant Bacillus subtilis
E292S thermodynamically stabilized mutant Bacillus subtilis
S180N highly stabilized mutant Bacillus subtilis
S180N/D289T/E260F/E292S mutant exhibits a 8.1-fold increase in half-life at 65°C and a 5.56 degrees increase in melting temperature and also displays a substantial increase in the transition state energy barrier and a clear decrease in folding free energy relative to the wild-type Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1
-
 L-asparagine mutant S180N/D289T/E260F/E292S, pH not specified in the publication, 37°C Bacillus subtilis
3.2
-
 L-asparagine mutant E292S, pH not specified in the publication, 37°C Bacillus subtilis
3.7
-
 L-asparagine mutant E260F, pH not specified in the publication, 37°C Bacillus subtilis
3.9
-
 L-asparagine mutant D289T, pH not specified in the publication, 37°C Bacillus subtilis
3.9
-
 L-asparagine mutant S180N, pH not specified in the publication, 37°C Bacillus subtilis
5
-
 L-asparagine wild-type, pH not specified in the publication, 37°C Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis 168
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-asparagine + H2O
-
 Bacillus subtilis L-aspartate + NH3
-
 ?
L-asparagine + H2O
-
 Bacillus subtilis 168 L-aspartate + NH3
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
70
-
 melting temperature, wild-type Bacillus subtilis
70.6
-
 melting temperature, mutant E260F Bacillus subtilis
70.9
-
 melting temperature, mutant E292S Bacillus subtilis
71.4
-
 melting temperature, mutant D289T Bacillus subtilis
72.5
-
 melting temperature, mutant S180N Bacillus subtilis
75.5
-
 melting temperature, mutant S180N/D289T/E260F/E292S Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
24.5
-
 L-asparagine mutant S180N/D289T/E260F/E292S, pH not specified in the publication, 37°C Bacillus subtilis
32.2
-
 L-asparagine mutant E260F, pH not specified in the publication, 37°C Bacillus subtilis
34.5
-
 L-asparagine mutant E292S, pH not specified in the publication, 37°C Bacillus subtilis
43.2
-
 L-asparagine mutant D289T, pH not specified in the publication, 37°C Bacillus subtilis
47.9
-
 L-asparagine mutant S180N, pH not specified in the publication, 37°C Bacillus subtilis
48.5
-
 L-asparagine wild-type, pH not specified in the publication, 37°C Bacillus subtilis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
8.6
-
 L-asparagine mutant E260F, pH not specified in the publication, 37°C Bacillus subtilis
9.7
-
 L-asparagine wild-type, pH not specified in the publication, 37°C Bacillus subtilis
10.9
-
 L-asparagine mutant E292S, pH not specified in the publication, 37°C Bacillus subtilis
11.1
-
 L-asparagine mutant D289T, pH not specified in the publication, 37°C Bacillus subtilis
11.9
-
 L-asparagine mutant S180N/D289T/E260F/E292S, pH not specified in the publication, 37°C Bacillus subtilis
12.3
-
 L-asparagine mutant S180N, pH not specified in the publication, 37°C Bacillus subtilis