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Literature summary extracted from

  • Borek, D.; Kozak, M.; Pei, J.; Jaskolski, M.
    Crystal structure of active site mutant of antileukemic L-asparaginase reveals conserved zinc-binding site (2014), FEBS J., 281, 4097-4111.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.5.1.1 medicine the enzyme is an important drug in the treatment of childhood acute lymphoblastic leukemia Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.1.1 mutant enzyme D90E, hanging drop vapor diffusion method, using 25% PEG MME 550, 100 mM MES pH 6.5, 10 mM ZnSO4 or 30% (w/v) PEG MME 550, 100 mM bicine pH 9.0, 100 mM NaCl or 100 mM HEPES pH 7.5, saturated solution of tribasic sodium citrate mixed with buffer, at citrate:buffer ratio of 9:1 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.1 D90E active site mutation Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.1.1 periplasm
-
 Escherichia coli
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.1 Zn2+ contains zinc Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 Escherichia coli P00805
-
-

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-asparaginase type II
-
 Escherichia coli