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Literature summary for 3.4.21.75 extracted from

  • Sjoeberg, M.; Wu, S.R.; Loeving, R.; Rantalainen, K.; Lindqvist, B.; Garoff, H.
    Furin cleavage of the Moloney murine leukemia virus Env precursor reorganizes the spike structure (2014), Proc. Natl. Acad. Sci. USA, 111, 6034-6039.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of enzyme mutant R466G/K468G in HEK-293T cells Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Moloney murine leukemia virus Env precursor protein + H2O Homo sapiens
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Organism

Organism UniProt Comment Textmining
Homo sapiens P09958
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Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme mutant R466G/K468G from HEK-293T cells Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Moloney murine leukemia virus Env precursor protein + H2O
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 Homo sapiens ?
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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 ?
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General Information

General Information Comment Organism
physiological function furin cleavage of the Moloney murine leukemia virus Env precursor reorganizes the spike structure, overview Homo sapiens