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Literature summary for 3.5.1.1 extracted from

  • Mahajan, R.V.; Kumar, V.; Rajendran, V.; Saran, S.; Ghosh, P.C.; Saxena, R.K.
    Purification and characterization of a novel and robust L-asparaginase having low-glutaminase activity from Bacillus licheniformis: in vitro evaluation of anti-cancerous properties (2014), PLoS ONE, 9, e99037.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine anticancer drug Bacillus licheniformis

General Stability

General Stability Organism
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 Bacillus licheniformis

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol strongest inhibition Bacillus licheniformis
4-phenylbutanoic acid more than 80% residual activity at 10 mM Bacillus licheniformis
Bromoacetic acid
-
Bacillus licheniformis
Ca2+
-
Bacillus licheniformis
Cd2+
-
Bacillus licheniformis
Co2+
-
Bacillus licheniformis
dithiothreitol
-
Bacillus licheniformis
EDTA 30% residual activity at 10 mM Bacillus licheniformis
EGTA
-
Bacillus licheniformis
Hg2+
-
Bacillus licheniformis
Lactate about 70% inhibition at 10 mM Bacillus licheniformis
Mn2+
-
Bacillus licheniformis
Ni2+
-
Bacillus licheniformis
oxylate about 70% inhibition at 10 mM Bacillus licheniformis
p-chloromercuribenzoic acid
-
Bacillus licheniformis
phenylmethylsulfonyl fluoride more than 80% residual activity at 10 mM Bacillus licheniformis
pyruvate about 70% inhibition at 10 mM Bacillus licheniformis
Urea 30% residual activity at 10 mM Bacillus licheniformis
Zn2+
-
Bacillus licheniformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.014
-
L-asparagine in 50 mM Tris-HCl buffer (pH 8.6), at 37°C Bacillus licheniformis

Metals/Ions

Metals/Ions Comment Organism Structure
K+ activates at 100 mM Bacillus licheniformis
Na+ activates at 100 mM Bacillus licheniformis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
33700
-
4 * 33700, SDS-PAGE Bacillus licheniformis
134800
-
gel filtration Bacillus licheniformis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-asparagine + H2O Bacillus licheniformis less than 10% activity compared to L-asparagine D-aspartate + NH3
-
?
L-asparagine + H2O Bacillus licheniformis highly specific substrate L-aspartate + NH3
-
?
L-glutamine + H2O Bacillus licheniformis less than 1% activity compared to L-asparagine L-glutamate + NH3
-
?
additional information Bacillus licheniformis no activity with D-glutamine, L-aspartic acid, D-aspartic acid, L-glutamic acid, and ornathine ?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
acetone precipitation, DEAE cellulose column chromatography, and Sephadex G-100 gel filtration Bacillus licheniformis

Storage Stability

Storage Stability Organism
-20°C, 50 mM Tris-HCl (pH 8.6), 30 days, almost no loss of activity Bacillus licheniformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-asparagine + H2O less than 10% activity compared to L-asparagine Bacillus licheniformis D-aspartate + NH3
-
?
L-asparagine + H2O highly specific substrate Bacillus licheniformis L-aspartate + NH3
-
?
L-glutamine + H2O less than 1% activity compared to L-asparagine Bacillus licheniformis L-glutamate + NH3
-
?
additional information no activity with D-glutamine, L-aspartic acid, D-aspartic acid, L-glutamic acid, and ornathine Bacillus licheniformis ?
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 33700, SDS-PAGE Bacillus licheniformis

Synonyms

Synonyms Comment Organism
L-ASNase
-
Bacillus licheniformis
L-asparaginase
-
Bacillus licheniformis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
Bacillus licheniformis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 50 the enzyme is active at the temperature range of 30-50°C and shows a steep decent in activity above 60°C Bacillus licheniformis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2680
-
L-asparagine in 50 mM Tris-HCl buffer (pH 8.6), at 37°C Bacillus licheniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
-
Bacillus licheniformis

pH Range

pH Minimum pH Maximum Comment Organism
6 10
-
Bacillus licheniformis

pH Stability

pH Stability pH Stability Maximum Comment Organism
7 9 the enzyme is maximally stable at pH range of 7.0 to 9.0 over a period of 24 h Bacillus licheniformis

pI Value

Organism Comment pI Value Maximum pI Value
Bacillus licheniformis calculated from amino acid sequence
-
5.5

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1503
-
L-asparagine in 50 mM Tris-HCl buffer (pH 8.6), at 37°C Bacillus licheniformis