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Literature summary for 3.4.23.16 extracted from
- Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes (2002), Structure, 10, 369-381.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | HIV-1 protease is the target of some of the most effective antiviral AIDS therapy, as it facilitates viral maturation by cleaving ten asymmetric and nonhomologous sequences in the Gag and Pol polyproteins | Human immunodeficiency virus 1 |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging drop method, crystal structures of complexes of an inactive variant D25N of HIV-1 protease with six peptides that correspond to the natural substrate cleavage site | Human immunodeficiency virus 1 |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D25N | inactive mutant enzyme | Human immunodeficiency virus 1 |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Human immunodeficiency virus 1 | the enzyme facilitates viral maturation by cleaving ten asymmetric and nonhomologous sequences in the Gag and Pol polyproteins | ? | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Human immunodeficiency virus 1 | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | the enzyme facilitates viral maturation by cleaving ten asymmetric and nonhomologous sequences in the Gag and Pol polyproteins | Human immunodeficiency virus 1 | ? | - |
? | |
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