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Literature summary extracted from

  • Qiao, J.; Qi, L.; Ma, H.; Chen, Y.; Wang, M.; Wang, D.
    Study on amino amides and enzyme kinetics of L-asparaginase by MCE (2010), Electrophoresis, 31, 1565-1571.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.1.1 biotechnology development of a MCE method (micellar electrokinetic electrophoresis) that is sufficiently sensitive and selective for the separation of amino amides and determination of enzyme kinetic constants of L-Asnase Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.1 0.442
-
L-asparagine Vmax: 0.0699 mM/min, 37°C, pH not specified in the publication Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 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-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 37
-
assay at Escherichia coli