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Literature summary extracted from

  • Derst, C.; Henseling, J.; Rohm, K.H.
    Engineering the substrate specificity of Escherichia coli asparaginase. II. Selective reduction of glutaminase activity by amino acid replacements at position 248 (2000), Protein Sci., 9, 2009-2017.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.5.1.1 medicine the use of asparaginase II as a drug for the treatment of acute lymphoblastic leukemia is complicated by the significant glutaminase side activity of the enzyme. Selective reduction in glutaminase activity in variant B248A and other N248 variants Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.1 G11V 518fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value Escherichia coli
3.5.1.1 G57A 3.8fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 5.2fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value Escherichia coli
3.5.1.1 G57L 346fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value Escherichia coli
3.5.1.1 G57V 48.8fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 37fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value Escherichia coli
3.5.1.1 G88A 8300fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value Escherichia coli
3.5.1.1 N248A 5.9fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 4657fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 15 kJ per mol for L-glutamine, 4 kJ per mol for L-aspartic beta-hydroxamate and 7 kJ per mol for L-asparagine Escherichia coli
3.5.1.1 N248D 10.18fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 49fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 10 kJ per mol for L-glutamine and 6 kJ per mol for L-aspartic beta-hydroxamate Escherichia coli
3.5.1.1 N248E 4.4fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 34.4fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 9 kJ per mol for L-glutamine and 4 kJ per mol for L-aspartic beta-hydroxamate Escherichia coli
3.5.1.1 N248G 7.5fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 116fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 12 kJ per mol for L-glutamine and 5 kJ per mol for L-aspartic beta-hydroxamate Escherichia coli
3.5.1.1 N248Q 5.9fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 6.2fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 10 kJ per mol for L-glutamine and 4 kJ per mol for L-aspartic beta-hydroxamate Escherichia coli
3.5.1.1 Q59A 163fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 930fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 17 kJ per mol for L-glutamine and 13 kJ per mol for L-aspartic beta-hydroxamate Escherichia coli
3.5.1.1 Q59E 15.4fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 93fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 7 kJ per mol for L-glutamine and 11 kJ per mol for L-aspartic beta-hydroxamate Escherichia coli
3.5.1.1 Q59G 105fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 465fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value. Loss in transition state stabilization is 15 kJ per mol for L-glutamine and 12 kJ per mol for L-aspartic beta-hydroxamate Escherichia coli
3.5.1.1 V27L 1.13fold increase in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 4.4fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value Escherichia coli
3.5.1.1 V27M 1.5fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value, 11.6fold decrease in the ratio of turnover number to Km-value for L-aspartic acid beta-hydroxamate as substrate compared to wild-type value Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.1 0.011
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme V27L Escherichia coli
3.5.1.1 0.015
-
 Asn pH 7.0, 25°C, wild-type enzyme Escherichia coli
3.5.1.1 0.015
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme V27M Escherichia coli
3.5.1.1 0.035
-
 L-Gln pH 7.0, 25°C, wild-type enzyme Escherichia coli
3.5.1.1 0.035
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, wild-type enzyme Escherichia coli
3.5.1.1 0.037
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme Q59E Escherichia coli
3.5.1.1 0.04
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme G88A Escherichia coli
3.5.1.1 0.05
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme G57V Escherichia coli
3.5.1.1 0.05
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme G88I Escherichia coli
3.5.1.1 0.056
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme N248D Escherichia coli
3.5.1.1 0.069
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme G57A Escherichia coli
3.5.1.1 0.07
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme G11V Escherichia coli
3.5.1.1 0.082
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme G57L Escherichia coli
3.5.1.1 0.095
-
 Asn pH 7.0, 25°C, mutant enzyme N248A Escherichia coli
3.5.1.1 0.13
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme G11L Escherichia coli
3.5.1.1 0.14
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme N248W Escherichia coli
3.5.1.1 0.15
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme N248Q Escherichia coli
3.5.1.1 0.19
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme N248A Escherichia coli
3.5.1.1 0.21
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme N248G Escherichia coli
3.5.1.1 1.8
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme Q59G Escherichia coli
3.5.1.1 1.9
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme Q59A Escherichia coli
3.5.1.1 2 3 L-Gln pH 7.0, 25°C, mutant enzyme Q59E Escherichia coli
3.5.1.1 2.4
-
 L-Gln pH 7.0, 25°C, mutant enzyme G57V Escherichia coli
3.5.1.1 3.5
-
 L-Gln pH 7.0, 25°C, mutant enzyme N248D Escherichia coli
3.5.1.1 4
-
 L-Gln pH 7.0, 25°C, mutant enzyme V27M Escherichia coli
3.5.1.1 4.4
-
 L-Gln pH 7.0, 25°C, mutant enzyme V27L Escherichia coli
3.5.1.1 5.7
-
 L-Gln pH 7.0, 25°C, mutant enzyme G57A Escherichia coli
3.5.1.1 6
-
 L-Gln pH 7.0, 25°C, mutant enzyme N248G Escherichia coli
3.5.1.1 10
-
 L-Gln pH 7.0, 25°C, mutant enzyme Q59A Escherichia coli
3.5.1.1 16
-
 L-Gln pH 7.0, 25°C, mutant enzyme N248A Escherichia coli
3.5.1.1 21
-
 L-Gln pH 7.0, 25°C, mutant enzyme N248Q Escherichia coli
3.5.1.1 50
-
 L-Gln pH 7.0, 25°C, mutant enzyme Q59G Escherichia coli
3.5.1.1 70
-
 L-Gln pH 7.0, 25°C, mutant enzyme N248E Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 Escherichia coli
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.1 L-Asn + H2O
-
 Escherichia coli L-Asp + NH3
-
 ?
3.5.1.1 L-aspartyl-beta-hydroxamate + H2O
-
 Escherichia coli L-Asp + hydroxylamine
-
 ?
3.5.1.1 L-Gln + H2O
-
 Escherichia coli L-Glu + NH3
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.1 asparaginase II
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.1 additional information
-
 additional information turnover numbers for L-aspartyl-beta-hydroxamate with mutant enzyme G11L and G88I are below 0.01 per sec Escherichia coli
3.5.1.1 0.001
-
 L-Gln pH 7.0, 25°C, mutant enzyme Q59A Escherichia coli
3.5.1.1 0.0024
-
 L-Gln pH 7.0, 25°C, mutant enzyme Q59E Escherichia coli
3.5.1.1 0.0029
-
 L-Gln pH 7.0, 25°C, mutant enzyme N248A Escherichia coli
3.5.1.1 0.004
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme G88A Escherichia coli
3.5.1.1 0.0046
-
 L-Gln pH 7.0, 25°C, mutant enzyme N248G Escherichia coli
3.5.1.1 0.006
-
 L-Gln pH 7.0, 25°C, mutant enzyme G57V Escherichia coli
3.5.1.1 0.0068
-
 L-Gln pH 7.0, 25°C, mutant enzyme N248D Escherichia coli
3.5.1.1 0.01
-
 L-Gln pH 7.0, 25°C, mutant enzyme G57A Escherichia coli
3.5.1.1 0.01
-
 L-Gln pH 7.0, 25°C, mutant enzyme Q59G Escherichia coli
3.5.1.1 0.019
-
 L-Gln pH 7.0, 25°C, mutant enzyme N248E Escherichia coli
3.5.1.1 0.032
-
 L-Gln pH 7.0, 25°C, mutant enzyme N248Q Escherichia coli
3.5.1.1 0.032
-
 L-Gln pH 7.0, 25°C, mutant enzyme V27M Escherichia coli
3.5.1.1 0.091
-
 L-Gln pH 7.0, 25°C, mutant enzyme V27L Escherichia coli
3.5.1.1 0.11
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme G11V Escherichia coli
3.5.1.1 0.143
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme Q59G Escherichia coli
3.5.1.1 0.2
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme G57L Escherichia coli
3.5.1.1 0.33
-
 L-Gln pH 7.0, 25°C, wild-type enzyme Escherichia coli
3.5.1.1 0.46
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme N248D Escherichia coli
3.5.1.1 0.86
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme G57V Escherichia coli
3.5.1.1 2
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme Q59E Escherichia coli
3.5.1.1 7
-
 Asn pH 7.0, 25°C, mutant enzyme N248A Escherichia coli
3.5.1.1 9.7
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme Q59A Escherichia coli
3.5.1.1 10.3
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme V27L Escherichia coli
3.5.1.1 10.8
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme V27M Escherichia coli
3.5.1.1 15.4
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme G57A Escherichia coli
3.5.1.1 21
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme N248Q Escherichia coli
3.5.1.1 23
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme N248G Escherichia coli
3.5.1.1 24
-
 Asn pH 7.0, 25°C, wild-type enzyme Escherichia coli
3.5.1.1 26
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme N248W Escherichia coli
3.5.1.1 27
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, mutant enzyme N248A Escherichia coli
3.5.1.1 29
-
 L-aspartyl-beta-hydroxamate pH 7.0, 25°C, wild-type enzyme Escherichia coli