Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Temperature Stability

Temperature Stability on EC 3.5.1.1 - asparaginase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28
-
half-life 35 h
34
-
melting temperature, 50 mM sodium phosphate buffer, pH 6.0, 375 mM NaCl
37 - 50
the enzyme shows no loss of activity after 30 min at 37°C and 40% loss of activity after 30 min at 50°C
41.5
-
melting temperature, 50 mM Tris-HCl pH 9.0
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
46
enzyme shows higher thermal stability at acidic to neutral pH values, lower stability is observed at alkaline pH. The inactivation profiles at pH 5.5 and 7 are biphasic and shows two clear transitions with inflection points corresponding to Tm values of 46.6°C and 62.5°C at pH 5.5, and 46.4 and 57.2°C at pH 7, respectively
46.4
wild type, half-inactivation temperature, 7.5 min
47
enzyme shows higher thermal stability at acidic to neutral pH values, lower stability is observed at alkaline pH. The inactivation profiles at pH 5.5 and 7 are biphasic and shows two clear transitions with inflection points corresponding to Tm values of 46.6°C and 62.5°C at pH 5.5, and 46.4 and 57.2°C at pH 7, respectively
50 - 60
-
the enzyme exhibits about 14.7 and 9.0% retention of activity following 2 h incubation at 50 or 60°C, respectively
53
the wild type enzyme shows 50% activity after 10 min incubation at 53°C
55.8
mutant D133V, half-inactivation temperature, 7.5 min
57
enzyme shows higher thermal stability at acidic to neutral pH values, lower stability is observed at alkaline pH. The inactivation profiles at pH 5.5 and 7 are biphasic and shows two clear transitions with inflection points corresponding to Tm values of 46.6°C and 62.5°C at pH 5.5, and 46.4 and 57.2°C at pH 7, respectively
59
melting temperature, mutant N24S
63
enzyme shows higher thermal stability at acidic to neutral pH values, lower stability is observed at alkaline pH. The inactivation profiles at pH 5.5 and 7 are biphasic and shows two clear transitions with inflection points corresponding to Tm values of 46.6°C and 62.5°C at pH 5.5, and 46.4 and 57.2°C at pH 7, respectively
70 - 95
the enzyme retains more than 60% of its initial activityafter 30 min at 70–95°C, and retains 66%, 60%, 54%, 53%, and 43% of its initial activity after 2 h of exposure at 70, 80, 85, 90, and 95°C, respectively
70.6
-
melting temperature, mutant E260F
70.9
-
melting temperature, mutant E292S
71.4
-
melting temperature, mutant D289T
72.5
-
melting temperature, mutant S180N
75.5
-
melting temperature, mutant S180N/D289T/E260F/E292S
85
-
5 min, 30% loss of activity
95
-
5 min, 90% loss of activity
additional information
-
D178P mutation enhances the thermostability of the enzyme without changing the activity of the enzyme and thus the therapeutical use of L-asparaginase II might be benefit from these result