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Literature summary for 3.5.1.1 extracted from

  • Offman, M.N.; Krol, M.; Patel, N.; Krishnan, S.; Liu, J.; Saha, V.; Bates, P.A.
    Rational engineering of L-asparaginase reveals importance of dual activity for cancer cell toxicity (2011), Blood, 117, 1614-1621.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
N24A increase in activity compared to wild-type, a unique hydrogen bond network contributes to higher activity Escherichia coli
N24A/R195S activity similar to wild-type Escherichia coli
N24A/Y250L about 75% of wild-type activity. Mutation Y250L is an interface mutation selected to stablize the active tetramer Escherichia coli
N24G mutant has a much higher loop flexibility compared with those of wild-type and the other mutants, and a decreased catalytic activity Escherichia coli
N24H mutant displays low flexibility in the central part of the loop; the C-terminal region of the loop shows high RMSF values that are likely to cause stability problems Escherichia coli
N24S/D281E RMSF profile similar to that of WT, with a slight increase in flexibility for residues 20-24 Escherichia coli
N24T increase in activity compared to wild-type. Mutant has very stable lid-loops, resulting in a tightly locked substrate molecule in the active site, stabilized for the catalytic reaction Escherichia coli
N24T/R195S about 85% of wild-type activity. Mutation R195S is an interface mutation selected to stablize the active tetramer Escherichia coli
N24T/Y250L about 70% of wild-type activity. Mutation Y250L is an interface mutation selected to stablize the active tetramer Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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General Information

General Information Comment Organism
metabolism L-asparaginase is degraded by leukemic lysosomal cysteine proteases Escherichia coli