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

BRENDA support

Literature summary 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

EC Number Application Comment Organism
3.5.1.1 medicine anticancer drug Bacillus licheniformis

General Stability

EC Number General Stability Organism
3.5.1.1 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

EC Number Inhibitors Comment Organism Structure
3.5.1.1 2-mercaptoethanol strongest inhibition Bacillus licheniformis
3.5.1.1 4-phenylbutanoic acid more than 80% residual activity at 10 mM Bacillus licheniformis
3.5.1.1 Bromoacetic acid
-
 Bacillus licheniformis
3.5.1.1 Ca2+
-
 Bacillus licheniformis
3.5.1.1 Cd2+
-
 Bacillus licheniformis
3.5.1.1 Co2+
-
 Bacillus licheniformis
3.5.1.1 dithiothreitol
-
 Bacillus licheniformis
3.5.1.1 EDTA 30% residual activity at 10 mM Bacillus licheniformis
3.5.1.1 EGTA
-
 Bacillus licheniformis
3.5.1.1 Hg2+
-
 Bacillus licheniformis
3.5.1.1 Lactate about 70% inhibition at 10 mM Bacillus licheniformis
3.5.1.1 Mn2+
-
 Bacillus licheniformis
3.5.1.1 Ni2+
-
 Bacillus licheniformis
3.5.1.1 oxylate about 70% inhibition at 10 mM Bacillus licheniformis
3.5.1.1 p-chloromercuribenzoic acid
-
 Bacillus licheniformis
3.5.1.1 phenylmethylsulfonyl fluoride more than 80% residual activity at 10 mM Bacillus licheniformis
3.5.1.1 pyruvate about 70% inhibition at 10 mM Bacillus licheniformis
3.5.1.1 Urea 30% residual activity at 10 mM Bacillus licheniformis
3.5.1.1 Zn2+
-
 Bacillus licheniformis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.1 0.014
-
 L-asparagine in 50 mM Tris-HCl buffer (pH 8.6), at 37°C Bacillus licheniformis

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.1 33700
-
 4 * 33700, SDS-PAGE Bacillus licheniformis
3.5.1.1 134800
-
 gel filtration Bacillus licheniformis

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 Bacillus licheniformis
-
-
-

Purification (Commentary)

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

Storage Stability

EC Number Storage Stability Organism
3.5.1.1 -20°C, 50 mM Tris-HCl (pH 8.6), 30 days, almost no loss of activity Bacillus licheniformis

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
3.5.1.1 L-ASNase
-
 Bacillus licheniformis
3.5.1.1 L-asparaginase
-
 Bacillus licheniformis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.1 40
-
-
 Bacillus licheniformis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.5.1.1 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]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.1 2680
-
 L-asparagine in 50 mM Tris-HCl buffer (pH 8.6), at 37°C Bacillus licheniformis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.1 9
-
-
 Bacillus licheniformis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.5.1.1 6 10
-
 Bacillus licheniformis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.5.1.1 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

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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.1.1 1503
-
 L-asparagine in 50 mM Tris-HCl buffer (pH 8.6), at 37°C Bacillus licheniformis