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Literature summary for 4.2.99.21 extracted from
- Nucleophile specificity in anthranilate synthase, aminodeoxychorismate synthase, isochorismate synthase, and salicylate synthase (2010), Biochemistry, 49, 2851-2859.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K147Q | mutation in proposed catalytic base, about 50fold decrease in activity | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | nucleophilic substitution reaction, enzyme is able to use H2O as a nucleophile. Catalytic base K147 is not solely responsible for activation of H2O as a nucleophile | Escherichia coli | ? | - |
? |  |
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Release 2023.1 (January 2023)
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