EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
5.1.1.3 | C184A | mutant C73A and C184A enzymes are inactive as racemases. However they are capable of catalyzing the elimination of HCl from opposite enantiomers of threo-3-chloroglutamic acid, a process that presumably requires only one enzymic base. It appears that Cys73 is responsible for the abstraction of the C-2 hydrogen from R-Glu and Cys184 abstracts the proton from S-glutamate in the racemization reaction of the wild type enzyme | Lactobacillus sp. |
5.1.1.3 | C73A | mutant C73A and C184A enzymes are inactive as racemases. However they are capable of catalyzing the elimination of HCl from opposite enantiomers of threo-3-chloroglutamic acid, a process that presumably requires only one enzymic base. It appears that Cys73 is responsible for the abstraction of the C-2 hydrogen from R-Glu and Cys184 abstracts the proton from S-glutamate in the racemization reaction of the wild type enzyme | Lactobacillus sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
5.1.1.3 | Lactobacillus sp. | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
5.1.1.3 | L-glutamate = D-glutamate | deprotonation/protonation mechanism for racemization in which the breaking of the carbon-hydrogen bond at C-2 is partially rate-determining | Lactobacillus sp. |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
5.1.1.3 | D-Glu | - |
Lactobacillus sp. | L-Glu | - |
? |