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Literature summary for 3.4.13.20 extracted from
- Homology modeling of human serum carnosinase, a potential medicinal target, and MD simulations of its allosteric activation by citrate (2006), J. Med. Chem., 49, 3269-3277.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| citrate | citrate ions are shown to bind at only three well-defined sites involving both ion pairs and hydrogen bonds. Molecular dynamics simulations evidence that citrate binding has a remarkable conformational influence on the 3D structure of carnosinase, increasing the binding affinity of carnosine to the catalytic site | Homo sapiens |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| serum carnosinase | - |
Homo sapiens |
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Release 2023.1 (January 2023)
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