Literature summary for 3.5.1.1 extracted from

Zhang, J.F.; Shi, L.Y.; Wei, D.Z.
Chemical modification of L-asparaginase from Escherichia coli with a modified polyethyleneglycol under substrate protection conditions (2004), Biotechnol. Lett., 26, 753-756.

Search for more literature for 3.5.1.1

Application

Application	Comment	Organism
medicine	the enzyme is a potential therapeutic agent in acute lymphocytic leukemia, acute lymphoblastic leukemia, and chromic myelogenyous leukemia, but causes high allergic reactions	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	reduction of the allergenic potential of the enzyme as therapeutic agent by chemical modification of the enzyme with 2,4-bis(O-methoxypolyethyleneglycol)-6-chloro-S-triazine, mPEG2, in presence of L-asparagine, optimally with a mPEG2/-NH2 molar ratio of 10, the modified enzyme retains 33% of initial enzymatic activity with complete abolishment of immunogenicity, in vitro half-life increments from 4.6 h to 33 h is obtained, method overview	Escherichia coli

Natural Substrates/ Products (Substrates)

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

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-asparaginase	-	Escherichia coli

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Escherichia coli

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Release 2023.1 (January 2023)