EC Number | Crystallization (Comment) | Organism |
---|---|---|
5.1.1.3 | hanging drop vapor diffusion method, crystal structure of apo-enzyme and enzyme complexed with a substrate analog, D-glutamine, by multiwavelength anomalous dispersion method using a thimerosal-bound MurI crystal, determined at 2.3 A resolution | Aquifex pyrophilus |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
5.1.1.3 | D7S | turnover number is decreased by 170fold compared to wild-type enzyme in the D to L reaction, it is decreased by about 6fold compared to wild-type enzyme in the L to D reaction | Aquifex pyrophilus |
5.1.1.3 | E147N | turnover number is decreased by 100fold compared to wild-type enzyme in the D to L reaction, it is decreased by about 7fold compared to wild-type enzyme in the L to D reaction | Aquifex pyrophilus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
5.1.1.3 | D-Gln | competitive | Aquifex pyrophilus |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.1.3 | 0.35 | - |
D-glutamate | pH 8.5, mutant enzyme D7S | Aquifex pyrophilus | |
5.1.1.3 | 0.55 | - |
D-glutamate | pH 8.5, wild-type enzyme | Aquifex pyrophilus | |
5.1.1.3 | 3 | - |
D-glutamate | pH 8.5, mutant enzyme E147N | Aquifex pyrophilus | |
5.1.1.3 | 3.2 | - |
L-glutamate | pH 8.5, mutant enzyme E147N | Aquifex pyrophilus | |
5.1.1.3 | 3.3 | - |
L-glutamate | pH 8.5, wild-type enzyme | Aquifex pyrophilus | |
5.1.1.3 | 11 | - |
L-glutamate | pH 8.5, mutant enzyme D7S | Aquifex pyrophilus |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.1.3 | L-glutamate | Aquifex pyrophilus | the enzyme is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell walls | D-glutamate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.1.3 | Aquifex pyrophilus | P56868 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.1.3 | L-glutamate | the enzyme is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell walls | Aquifex pyrophilus | D-glutamate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
5.1.1.3 | dimer | each monomer consists of two alpha/beta fold domains | Aquifex pyrophilus |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.1.3 | 0.00034 | - |
D-glutamate | pH 8.5, mutant enzyme D7S | Aquifex pyrophilus | |
5.1.1.3 | 0.0023 | - |
L-glutamate | pH 8.5, mutant enzyme E147N | Aquifex pyrophilus | |
5.1.1.3 | 0.0047 | - |
L-glutamate | pH 8.5, mutant enzyme E147N | Aquifex pyrophilus | |
5.1.1.3 | 0.037 | - |
L-glutamate | pH 8.5, mutant enzyme D7S | Aquifex pyrophilus | |
5.1.1.3 | 0.056 | - |
D-glutamate | pH 8.5, wild-type enzyme | Aquifex pyrophilus | |
5.1.1.3 | 0.21 | - |
L-glutamate | pH 8.5, wild-type enzyme | Aquifex pyrophilus |
EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.1.3 | 50 | - |
D-Gln | - |
Aquifex pyrophilus |