Cloned (Comment) | Organism |
---|---|
expression of His-tagged wild-type enzyme and His-tagged mutant enzyme K327N in Escherichia coli | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
K327N | mutant enzyme catalyzes the deamination of L-aspartic acid alpha-amide, 13.5fold increase in Km-value for L-aspartate compared to wild-type value | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.1 | - |
L-aspartic acid | pH 8.5, 30°C, wild-type enzyme | Escherichia coli | |
28.3 | - |
L-aspartic acid | pH 8.5, 30°C, mutant enzyme K327N | Escherichia coli | |
1450 | - |
L-aspartic acid alpha-amide | pH 7.0, 30°C | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P0AC38 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-aspartate | highly selective towards L-aspartate | Escherichia coli | fumarate + NH3 | - |
r | |
L-aspartic acid alpha-amide | catalyzed by mutant enzyme K327N, no activity with wild-type enzyme | Escherichia coli | (2E)-4-amino-4-oxobut-2-enoate + NH3 | - |
? |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
deamination of L-aspartic acid alpha-amide, mutant enzyme K327N | Escherichia coli |
8.5 | - |
deamination of L-aspartate, wild-type enzyme and mutant enzyme K327N | Escherichia coli |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
7 | 9 | pH 7.0: about 40% of maximal activity, pH 9.0: about 90% of maximal activity, substrate: L-aspartate, wild-type enzyme | Escherichia coli |
7.5 | 9 | pH 7.5: about 70% of maximal activity, pH 9.0: about 85% of maximal activity, substrate: L-aspartic acid, mutant enzyme K327N | Escherichia coli |