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3.5.1.1: asparaginase

This is an abbreviated version!
For detailed information about asparaginase, go to the full flat file.

Word Map on EC 3.5.1.1

Reaction

L-asparagine
+
H2O
=
L-aspartate
 +
NH3

Synonyms

14270 ASNase, alpha-asparaginase, AnsA, ansA3, AnsB, ansZ, Asn, ASNase, ASNase1, ASNase3, ASP1, ASP3, asparaginase, asparaginase II, asparagine amidohydrolase, asparginase II, ASPG, ASPG II, ASPGA1, ASPGB1, ASRGL1, At3g16150, colaspase, crasnitin, DiAsp, EcAII, EcAIII, EcaL-ASNase, ECAR-LANS, elspar, ErA, Erwinase, glutaminase-free L-asparaginase, glutamine-(asparagin-)ase, HPA, L-ASNase, L-asparaginase, L-asparaginase 2, L-asparaginase I, L-asparaginase II, L-asparaginase III, L-asparaginase type II, L-asparaginase type III, L-asparaginase-I, L-asparaginase-II, L-asparagine amidohydrolase, L-asparagine amino hydrolase, L-asparagine aminohydrolase, leunase, PfA, PhA, potassium-dependent asparaginase, potassium-independent asparaginase, potassium-independent L-asparaginase, SAMN05216263_10744, SGR ASNase, type I L-asparaginase, type II L-asparaginase, Ypa

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.1 asparaginase

General Stability

General Stability on EC 3.5.1.1 - asparaginase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
1 h at 23°C in 2 M urea leads to a 100% decrease of activity, presence of L-Asp increased the stability
3 min at 35°C leads to a 60% irreversible decrease of activity, presence of L-Asp increases the stability
after incubation with various concentration of urea for 6 h, the purified enzyme samples almost do not exhibit any change in enzyme activity even by incubation with 8 M of urea
enzyme is stable when incubated with rat serum and ascites fluid
-
freezing at -20°C, complete and irreversible loss of activity
-
half-life of immobilized enzyme at 37°C, pH 8.6 is 8 days
-
in the presence of guanidine hydrochloride (GdnCl) the curves follow a sigmoidal pattern with unfolding beginning at 3.25 M guanidine hydrochloride and complete unfolding achieved at 4.75 M guanidine hydrochloride. The enzymatic activity of urea-containing protein samples remains unchanged. In contrast, the guanidine hydrochloride-incubated samples show a significantly lower activity even with 1 M guanidine hydrochloride.
-
in-vitro half-life of purified L-asparaginase in mammalian blood serum is 93.69 h
-
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
-
reversibly dissociated by urea
-
stable during lyophilization and concentration with aquacide, inactivation after dialysis
-
stable to dialysis in the cold, but labile under conditions which promote surface denaturation
-
stable to freezing and thawing
-
stable to repeated freezing and thawing
the enzyme can be efficiently immobilized on epoxy-activated Sepharose CL-6B. The immobilized enzyme retains most of its activity (60%) and shows high stability at 4°C
the enzyme is stable in the presence of more than 3 M guanidine hydrochloride. The enzyme activity decreases by approximately 40%, when the purified L-asparaginase is incubated with human serum and its components respectively under in vitro conditions for 48 h
-
the enzyme retains more than 60% of its activity under 2 M NaCl condition
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
-