EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
5.1.1.3 | D10N | 1015fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 3.9fold increase in Km-value for L-glutamate compared to wild-type enzyme. 1079fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 4.6fold increase in Km-value for D-glutamate compared to wild-type enzyme | Limosilactobacillus fermentum |
5.1.1.3 | D36N | 3.4fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 106fold increase in Km-value for L-glutamate compared to wild-type enzyme. 3.1fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 158fold increase in Km-value for D-glutamate compared to wild-type enzyme | Limosilactobacillus fermentum |
5.1.1.3 | E152Q | 1.8fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 3.1fold increase in Km-value for L-glutamate compared to wild-type enzyme. 3.1fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 13.5fold increase in Km-value for D-glutamate compared to wild-type enzyme | Limosilactobacillus fermentum |
5.1.1.3 | H186N | 1533fold decrease of turnover number for L-glutamate compared to wild-type enzyme, 3.4fold increase in Km-value for L-glutamate compared to wild-type enzyme. 731fold decrease of turnover number for D-glutamate compared to wild-type enzyme, 17.3fold increase in Km-value for D-glutamate compared to wild-type enzyme | Limosilactobacillus fermentum |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.1.3 | 0.26 | - |
D-glutamate | pH 8, 30°C, wild-type enzyme | Limosilactobacillus fermentum | |
5.1.1.3 | 0.33 | - |
L-glutamate | pH 8, 30°C, wild-type enzyme | Limosilactobacillus fermentum | |
5.1.1.3 | 1.1 | - |
L-glutamate | pH 8, 30°C, mutant enzyme H186N | Limosilactobacillus fermentum | |
5.1.1.3 | 1.2 | - |
D-glutamate | pH 8, 30°C, mutant enzyme D10N | Limosilactobacillus fermentum | |
5.1.1.3 | 1.3 | - |
L-glutamate | pH 8, 30°C, mutant enzyme D10N | Limosilactobacillus fermentum | |
5.1.1.3 | 3.5 | - |
D-glutamate | pH 8, 30°C, mutant enzyme H152Q | Limosilactobacillus fermentum | |
5.1.1.3 | 4.5 | - |
D-glutamate | pH 8, 30°C, mutant enzyme H186N | Limosilactobacillus fermentum | |
5.1.1.3 | 5.8 | - |
L-glutamate | pH 8, 30°C, mutant enzyme H152Q | Limosilactobacillus fermentum | |
5.1.1.3 | 35 | - |
L-glutamate | pH 8, 30°C, mutant enzyme D36N | Limosilactobacillus fermentum | |
5.1.1.3 | 41 | - |
D-glutamate | pH 8, 30°C, mutant enzyme D36N | Limosilactobacillus fermentum |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.1.3 | L-glutamate | Limosilactobacillus fermentum | - |
D-glutamate | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.1.3 | Limosilactobacillus fermentum | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
5.1.1.3 | L-glutamate = D-glutamate | the enzyme uses a two-base mechanism involving a deprotonation of the substrate at the alpha-position to form an anionic intermediate, followed by a reprotonation in the opposite stereochemical sense. Cys73 is responsible for the deprotonation of D-glutamate and Cys184 is responsible for the deprotonation of L-glutamate | Limosilactobacillus fermentum |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.1.3 | L-glutamate | - |
Limosilactobacillus fermentum | D-glutamate | - |
r | |
5.1.1.3 | L-glutamate | the enzyme provides bacteria with a source of D-glutamate for use in peptidoglycan biosynthesis | Limosilactobacillus fermentum | D-glutamate | - |
? | |
5.1.1.3 | additional information | the enzyme uses a two-base mechanism involving a deprotonation of the substrate at the alpha-position to form an anionic intermediate, followed by a reprotonation in the opposite stereochemical sense. Cys73 is responsible for the deprotonation of D-glutamate and Cys184 is responsible for the deprotonation of L-glutamate | Limosilactobacillus fermentum | ? | - |
? |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
5.1.1.3 | 0.045 | - |
L-glutamate | pH 8, 30°C, mutant enzyme H186N | Limosilactobacillus fermentum | |
5.1.1.3 | 0.063 | - |
D-glutamate | pH 8, 30°C, mutant enzyme D10N | Limosilactobacillus fermentum | |
5.1.1.3 | 0.068 | - |
L-glutamate | pH 8, 30°C, mutant enzyme D10N | Limosilactobacillus fermentum | |
5.1.1.3 | 0.093 | - |
D-glutamate | pH 8, 30°C, mutant enzyme H186N | Limosilactobacillus fermentum | |
5.1.1.3 | 20 | - |
L-glutamate | pH 8, 30°C, mutant enzyme D36N | Limosilactobacillus fermentum | |
5.1.1.3 | 22 | - |
D-glutamate | pH 8, 30°C, mutant enzyme D36N and H152Q | Limosilactobacillus fermentum | |
5.1.1.3 | 38 | - |
L-glutamate | pH 8, 30°C, mutant enzyme H152Q | Limosilactobacillus fermentum | |
5.1.1.3 | 68 | - |
D-glutamate | pH 8, 30°C, wild-type enzyme | Limosilactobacillus fermentum | |
5.1.1.3 | 69 | - |
L-glutamate | pH 8, 30°C, wild-type enzyme | Limosilactobacillus fermentum |