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Literature summary for 3.4.21.4 extracted from
- Structural basis for the design of novel Schiff base metal chelate inhibitors of trypsin (2010), Bioorg. Med. Chem., 18, 2076-2080.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| m-amidinosalicylidene-L-alaninato(aqua)copper(II) hydrochloride | - |
Bos taurus | |
| m-guanidinosalicylidene-L-alaninato(aqua)copper(II) | - |
Bos taurus |  |
| additional information | design and synthesis of Schiff base metal chelate inhibitors of trypsin, structural basis, overview. The binding mode of the guanidino groups of m-guanidinosalicylidene-L-alaninato(aqua)copper(II) hydrochloride and [N,N'-bis(m-guanidinosalicylidene)ethylenediaminato]copper(II) to Asp189 in the S1 pocket of trypsin is markedly different from of the amidino group of m-amidinosalicylidene-L-alaninato(aqua)copper(II) hydrochloride. The active site residues of trypsin play a crucial role in the binding affinity to the trypsin molecule. | Bos taurus | |
| [N,N'-bis(m-amidinosalicylidene)ethylenediaminato]copper(II) | - |
Bos taurus | |
| [N,N'-bis(m-guanidinosalicylidene)ethylenediaminato]copper(II) | - |
Bos taurus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
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Release 2023.1 (January 2023)
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