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
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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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Reaction
Reaction on EC 3.4.23.B5 - murine leukemia virus protease
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processing of viral polyprotein. The retroviral protease is essential for virus replication, by processing of viral Gag and Gag-Pol polyproteins
processing of viral polyprotein. The retroviral protease is essential for virus replication, by processing of viral Gag and Gag-Pol polyproteins
structure-based molecular modeling of reaction mechanism and substrate binding
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processing of viral polyprotein. The retroviral protease is essential for virus replication, by processing of viral Gag and Gag-Pol polyproteins
substrate binding pocket residues are His37, Val39, and Ala57
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processing of viral polyprotein. The retroviral protease is essential for virus replication, by processing of viral Gag and Gag-Pol polyproteins
conversion of coproporphyrinogen III to protoporphyrinogen IX via the reaction intermediate harderoporphyrinogen. HemN contains a catalytically essential [4Fe-4S] cluster that transfers an electron to bound S-adenosyl-L-methionine, thereby producing methionine and a 5'-deoxyadenosyl radical. This radical then abstracts a hydrogen atom from the beta-carbon of the substrate propionate side chain, resulting in the formation of a coproporphyrinogenyl radical, overview
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