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Literature summary extracted from

  • Kotzia, G.A.; Lappa, K.; Labrou, N.E.
    Tailoring structure-function properties of L-asparaginase: engineering resistance to trypsin cleavage (2007), Biochem. J., 404, 337-343.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.1 R206H Arg206 to histidine followed by covalent coupling of mPEG-SNHS [methoxypoly(ethyene glycol) succinate N-hydroxysuccinimide ester] to the mutant enzyme results in an improved modified form of EcaL-ASNase that retains 82% of the original catalytic activity, exhibits enhanced resistance to trypsin degradation, and has higher thermal stability compared with the wild-type enzyme Pectobacterium carotovorum

General Stability

EC Number General Stability Organism
3.5.1.1 limited proteolysis of EcaL-ASNase with trypsin is associated with a first cleavage of the peptide bond between Lys53 and Gly54, and then a second cleavage at Arg206-Ser207 of the C-terminal fragment, peptide 54-327. Site-directed mutagenesis of Arg206 to histidine followed by covalent coupling of mPEG-SNHS [methoxypoly(ethylene glycol) succinate N-hydroxysuccinimide ester] to the mutant enzyme results in an improved modified form of EcaL-ASNase that retains 82% of the original catalytic activity, exhibits enhanced resistance to trypsin degradation, and has higher thermal stability compared with the wild-type enzyme Pectobacterium carotovorum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.1 0.36
-
 L-asparagine 37°C, mutant enzyme R206H covalently coupled to methoxypoly(ethyene glycol) succinate N-hydroxysuccinimide ester Pectobacterium carotovorum
3.5.1.1 0.55
-
 L-asparagine 37°C, mutant enzyme R206H Pectobacterium carotovorum

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 Pectobacterium carotovorum
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.1 L-asparagine + H2O
-
 Pectobacterium carotovorum L-aspartate + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.1 EcaL-ASNase
-
 Pectobacterium carotovorum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.5.1.1 39
-
 Tm-value of wild-type enzyme is 38.9°C, Tm-value of mutant enzyme is 38.8°C Pectobacterium carotovorum
3.5.1.1 43
-
 Tm-value of wild-type enzyme covalently coupled to methoxypoly(ethyene glycol) succinate N-hydroxysuccinimide ester is 42.9°C, Tm-value of mutant enzyme R206H covalently coupled to methoxypoly(ethyene glycol) succinate N-hydroxysuccinimide ester is 43.1°C Pectobacterium carotovorum