3.4.23.B4: Feline immunodeficiency virus protease
This is an abbreviated version!
For detailed information about Feline immunodeficiency virus protease, go to the full flat file.
Word Map on EC 3.4.23.B4
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3.4.23.B4
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broad-based
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polyproteins
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retroviral
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drug-resistant
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gag-pol
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flap
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subsites
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val
-
calicivirus
-
lopinavir
-
lentivirus
-
virions
-
medicine
-
molecular biology
-
drug development
- 3.4.23.B4
-
broad-based
- polyproteins
-
retroviral
-
drug-resistant
- gag-pol
- flap
-
subsites
- val
- calicivirus
- lopinavir
- lentivirus
- virions
- medicine
- molecular biology
- drug development
Reaction
the enzyme seems to have a preference for Val in P1' and Phe in P1. In contrast to the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGVFVQNGLVK at the Phe-Val bond. Gln in P2' may be inhibitory. In contrast to HIV-1 protease the feline immunodeficiency virus protease does not cleave peptide KSGNFVVNGLVK at the Phe-Val bond. Asn in P2 may be inhibitory =
Synonyms
FCV protease, feline immunodeficiency virus protease, Feline immunodeficiency virus retropepsin, FIV PR, FIV protease, FIV retropepsin, FIV-PR, More
ECTree
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Metals Ions
Metals Ions on EC 3.4.23.B4 - Feline immunodeficiency virus protease
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NaCl
the protease activity is not inhibited with increasing NaCl concentrations up to 130 mM
NaCl
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increasing salt concentration up to 1.5 M increases the enzyme activity