EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.1.3.3 | L142R mutant, complexed with beta-hydroxypyruvate, hanging drop vapor diffusion method | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.1.3.3 | L142R | increased activity towards L-aspartate-beta-semialdehyde | Escherichia coli |
4.1.3.3 | L142R/Y190D/E192A | less efficient than wild-type enzyme | Escherichia coli |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
4.1.3.3 | L-lysine | 50% inhibition at 0.2 mM, inhibits wild-type enzyme, but not mutant enzymes | Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.1.3.3 | Escherichia coli | P0A6L4 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.1.3.3 | - |
Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.1.3.3 | additional information | One point mutation (L142R) is sufficient to create an enzyme that can complement a bacterial auxotroph lacking the gene for dihydrodipicolinate synthase, EC 4.2.1.52. The mutant enzyme catalyzes the reaction: L-aspartate 4-semialdehyde + pyruvate = dihydrodipicolinate + 2 H2O | Escherichia coli | ? | - |
? | |
4.1.3.3 | N-Acetylneuraminic acid | - |
Escherichia coli | N-Acetyl-D-mannosamine + pyruvate | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.1.3.3 | 6.8 | - |
N-acetylneuraminic acid | pH 7.2, 25°C, L142R/Y190D/E192A mutant | Escherichia coli | |
4.1.3.3 | 7.7 | - |
N-acetylneuraminic acid | pH 7.2, 25°C, wild-type | Escherichia coli | |
4.1.3.3 | 12.1 | - |
N-acetylneuraminic acid | pH 7.2, 25°C, L142R mutant | Escherichia coli |