Literature summary for 3.5.1.1 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.

Search for more literature for 3.5.1.1

Application

Application	Comment	Organism
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]

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

Organism

Organism	UniProt	Comment	Textmining
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-ASNase	-	Escherichia coli
L-asparaginase	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Escherichia coli

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Release 2023.1 (January 2023)