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Literature summary for 3.4.23.49 extracted from
- An amino acid switch (Gly281-->Arg) within the hinge region of the tryptophan synthase beta subunit creates a novel cleavage site for the OmpT protease and selectively diminishes affinity toward a specific monoclonal antibody (1993), J. Biol. Chem., 268, 14912-14920.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| Tryptophan synthase + H2O | beta-subunit of E. coli enzyme, the wild-type beta-subunit is apparently very stable, the missense mutant beta(B8), carrying an amino acid switch from Gly to Arg at the residue 281, undergoes specific proteolytic cleavage, cleavage products of 30000 MW from the N-terminus and 13000 MW from the C-terminus are observed, cleavage is specific for the peptide bond Arg281-Met282 | Escherichia coli | ? | - |
? |  |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
proteolytic cleavage observed only under neutral conditions | Escherichia coli |
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Release 2023.1 (January 2023)
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