Cloned (Comment) | Organism |
---|---|
- |
Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
hanging drop vapor diffusion method. X-ray crystal structure of the D285N mutant complexed with beta-Asp-His | Escherichia coli |
Protein Variants | Comment | Organism |
---|---|---|
D285A | kcat/Km for beta-Asp-Leu is 85000fold lower than wild-type value | Escherichia coli |
D285N | kcat/Km for beta-Asp-Leu is 5667fold lower than wild-type value | Escherichia coli |
E77D | kcat/Km for beta-Asp-Leu is 137837fold lower than wild-type value | Escherichia coli |
E77Q | kcat/Km for beta-Asp-Leu is 14571fold lower than wild-type value | Escherichia coli |
R169K | kcat/Km for beta-Asp-Leu is 378fold lower than wild-type value | Escherichia coli |
R169M | kcat/Km for beta-Asp-Leu is 1672131fold lower than wild-type value | Escherichia coli |
R233K | kcat/Km for beta-Asp-Leu is 192fold lower than wild-type value | Escherichia coli |
R233M | kcat/Km for beta-Asp-Leu is 170fold lower than wild-type value | Escherichia coli |
S289A | kcat/Km for beta-Asp-Leu is 30000fold lower than wild-type value | Escherichia coli |
Y137A | kcat/Km for beta-Asp-Leu is 927fold lower than wild-type value | Escherichia coli |
Y137F | kcat/Km for beta-Asp-Leu is 850fold lower than wild-type value | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.09 | - |
beta-Asp-Leu | Ni/Ni reconstituted enzyme, pH 8.1, 30°C | Escherichia coli | |
0.23 | - |
beta-Asp-Phe | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
0.36 | - |
beta-Asp-Leu | Cd/Cd reconstituted enzyme, pH 8.1, 30°C | Escherichia coli | |
0.5 | - |
beta-Asp-Leu | mutant enzyme D285A, pH 8.1, 30°C | Escherichia coli | |
0.62 | - |
beta-Asp-Leu | Co/Co reconstituted enzyme, pH 8.1, 30°C | Escherichia coli | |
0.8 | - |
beta-Asp-Leu | mutant enzyme E77Q, pH 8.1, 30°C | Escherichia coli | |
0.91 | - |
beta-Asp-Lys | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
0.98 | - |
beta-Asp-Leu | mutant enzyme D285N, pH 8.1, 30°C | Escherichia coli | |
1.02 | - |
beta-Asp-Leu | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
1.02 | - |
beta-Asp-Leu | Zn/Zn reconstituted enzyme, pH 8.1, 30°C | Escherichia coli | |
1.4 | - |
beta-Asp-Leu | mutant enzyme Y137F, pH 8.1, 30°C | Escherichia coli | |
1.7 | - |
beta-Asp-Leu | mutant enzyme Y137A, pH 8.1, 30°C | Escherichia coli | |
2.7 | - |
beta-Asp-Leu | mutant enzyme S289A, pH 8.1, 30°C | Escherichia coli | |
3.7 | - |
beta-Asp-His | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
3.7 | - |
beta-Asp-Ala | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
5 | - |
alpha-Asp-Leu | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
6.9 | - |
beta-Asp-Leu | mutant enzyme E77D, pH 8.1, 30°C | Escherichia coli | |
18 | - |
beta-Asp-Gly | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
20 | - |
beta-Asp-Leu | mutant enzyme R233K, pH 8.1, 30°C | Escherichia coli | |
34 | - |
beta-Asp-Leu | mutant enzyme R169K, pH 8.1, 30°C | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | the active site consists of a binuclear metal center positioned at the C-terminal end of a (beta/alpha)8-barrel domain | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P39377 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
alpha-Asp-Leu + H2O | - |
Escherichia coli | L-Asp + L-Leu | - |
? | |
beta-Asp-Ala + H2O | - |
Escherichia coli | Asp + Ala | - |
? | |
beta-Asp-Gly + H2O | - |
Escherichia coli | Asp + Gly | - |
? | |
beta-Asp-His + H2O | - |
Escherichia coli | Asp + His | - |
? | |
beta-Asp-Leu + H2O | - |
Escherichia coli | Asp + Leu | - |
? | |
beta-Asp-Lys + H2O | - |
Escherichia coli | Asp + Lys | - |
? | |
beta-Asp-Phe + H2O | - |
Escherichia coli | Asp + Phe | - |
? |
Synonyms | Comment | Organism |
---|---|---|
IAD | - |
Escherichia coli |
isoaspartyl dipeptidase | - |
Escherichia coli |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00062 | - |
beta-Asp-Leu | mutant enzyme D285A, pH 8.1, 30°C | Escherichia coli | |
0.0051 | - |
beta-Asp-Leu | mutant enzyme E77D, pH 8.1, 30°C | Escherichia coli | |
0.0056 | - |
beta-Asp-Leu | mutant enzyme E77Q, pH 8.1, 30°C | Escherichia coli | |
0.017 | - |
beta-Asp-Leu | mutant enzyme D285N, pH 8.1, 30°C | Escherichia coli | |
0.18 | - |
beta-Asp-Leu | mutant enzyme Y137F, pH 8.1, 30°C | Escherichia coli | |
0.19 | - |
beta-Asp-Leu | mutant enzyme Y137A, pH 8.1, 30°C | Escherichia coli | |
0.93 | - |
beta-Asp-Gly | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
9 | - |
beta-Asp-Leu | mutant enzyme R169K, pH 8.1, 30°C | Escherichia coli | |
9 | - |
beta-Asp-Leu | mutant enzyme S289A, pH 8.1, 30°C | Escherichia coli | |
9.2 | - |
beta-Asp-Leu | Ni/Ni reconstituted enzyme, pH 8.1, 30°C | Escherichia coli | |
11.9 | - |
beta-Asp-Leu | Cd/Cd reconstituted enzyme, pH 8.1, 30°C | Escherichia coli | |
13 | - |
beta-Asp-Leu | mutant enzyme R233K, pH 8.1, 30°C | Escherichia coli | |
15.7 | - |
alpha-Asp-Leu | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
16.9 | - |
beta-Asp-Phe | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
20.8 | - |
beta-Asp-His | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
34 | - |
beta-Asp-Leu | Co/Co reconstituted enzyme, pH 8.1, 30°C | Escherichia coli | |
58 | - |
beta-Asp-Lys | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
104 | - |
beta-Asp-Leu | wild-type enzyme, pH 8.1, 30°C | Escherichia coli | |
104 | - |
beta-Asp-Leu | Zn/Zn reconstituted enzyme, pH 8.1, 30°C | Escherichia coli | |
213 | - |
beta-Asp-Ala | wild-type enzyme, pH 8.1, 30°C | Escherichia coli |