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Literature summary extracted from

  • Newsted, W.J.; Ramjeesingh, M.; Zywulko, M.; Rothstein, S.J.; Shami, E.Y.
    Engineering resistance to trypsin inactivation into L-asparaginase through the production of a chimeric protein between the enzyme and a protective single-chain antibody (1995), Enzyme Microb. Technol., 17, 575-764.
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.1 S58A crystallization of the mutant L-asparaginase II Escherichia coli

General Stability

EC Number General Stability Organism
3.5.1.1 the trypsin sensitive enzyme can be rendered trypsin resistant by genetically fusing its gene with that of a single-chain antibody derived from a preselected monoclonal antibody capable of providing protection against trypsin. The chimeric L-asparaginase retains 75% of its original activity upon exposure to trypsin, the native unprotected enzyme is totally inactivated Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.5.1.1 periplasm
-
 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-Asn + H2O
-
 Escherichia coli L-Asp + NH3
-
 ?