3.4.23.B5: murine leukemia virus protease
This is an abbreviated version!
For detailed information about murine leukemia virus protease, go to the full flat file.
Word Map on EC 3.4.23.B5
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3.4.23.B5
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mulvs
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readthrough
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polyproteins
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oligopeptides
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envelope
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pr65gag
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single-chain
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pseudotyped
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subsites
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amber
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cell-cell
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junction
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leukaemia
-
analysis
- 3.4.23.B5
- mulvs
-
readthrough
- polyproteins
- oligopeptides
- envelope
-
pr65gag
-
single-chain
-
pseudotyped
-
subsites
-
amber
-
cell-cell
- junction
-
leukaemia
- analysis
Reaction
processing of viral polyprotein. The retroviral protease is essential for virus replication, by processing of viral Gag and Gag-Pol polyproteins =
Synonyms
MLV PR, MLV protease, MLV retropepsin, MMLV protease, Mo-MuLV PR, Mo-MuLV protease, Moloney MLV retropepsin, Moloney murine leukemia virus protease, Moloney murine leukemia virus retropepsin, More, MuLV 4070A, MuLV proteinase, murine leukemia virus protease, viral protease, vPR
ECTree
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Inhibitors
Inhibitors on EC 3.4.23.B5 - murine leukemia virus protease
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amprenavir
NMR structural analysis of recombinant protease in complex with amprenavir. One amprenavir molecule binds to one protease dimer. Intermolecular NOE signals between amprenavir and either the methyl groups of A35, V39, V54, A57, L83 and L92 or the aromatic ring of Y90 can be identified. The structural heterogeneity induced by the asymmetry of the binding of amprenavir to the protease dimer is transmitted to distant regions
amprenavir
catalytic activity of XMRV protease is selectively blocked by the HIV protease inhibitor, amprenavir, 13.9% residual activity at 1 microM