Cloned (Comment) | Organism |
---|---|
recombinant expression of enzyme mutant R466G/K468G in HEK-293T cells | Homo sapiens |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
Moloney murine leukemia virus Env precursor protein + H2O | Homo sapiens | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P09958 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme mutant R466G/K468G from HEK-293T cells | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
Moloney murine leukemia virus Env precursor protein + H2O | - |
Homo sapiens | ? | - |
? | |
Moloney murine leukemia virus Env precursor protein + H2O | furin cleaves the Env precursor into the surface and transmembrane subunits in the cell and then the viral protease cleaves the R-peptide from TM in newvirus. Structure analysis of the open cage-like structure like that of the R-peptide precursor and of the mature protein, overview. Furin cleavage not only separates the subunits and liberates the fusion peptide at the end of TM but also allows the C-terminal domain to relocate into a peripheral position. This conformational change might explain how the C-terminal domain of surface subunit gains the potential to undergo disulfide isomerization, an event that facilitates membrane fusion | Homo sapiens | ? | - |
? |
General Information | Comment | Organism |
---|---|---|
physiological function | furin cleavage of the Moloney murine leukemia virus Env precursor reorganizes the spike structure, overview | Homo sapiens |