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Literature summary for 3.4.23.16 extracted from
- Expression and purification of HIV-1 protease utilizing a maltose binding protein (1994), Mol. Cells, 4, 79-84.
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| the enzyme is engineered in Escherichia coli as a construct in which the natural 99-residue polypeptide is preceded by an N-terminal methionine initiator | Human immunodeficiency virus 1 |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| inclusion body | inclusion bodies from Escherichia coli harboring recombinant HIV-1 | Human immunodeficiency virus 1 | 16234 | - |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 10000 | - |
x * 10000, SDS-PAGE | Human immunodeficiency virus 1 |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Human immunodeficiency virus 1 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Human immunodeficiency virus 1 |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 10000, SDS-PAGE | Human immunodeficiency virus 1 |
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Release 2023.1 (January 2023)
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