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 |
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 |
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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.5.1.1 | Escherichia coli | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|
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 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.5.1.1 | asparaginase II | - |
Escherichia coli |
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 |