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
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calicivirus
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lopinavir
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lentivirus
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virions
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medicine
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molecular biology
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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
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Posttranslational Modification
Posttranslational Modification on EC 3.4.23.B4 - Feline immunodeficiency virus protease
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proteolytic modification
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the enzyme is expressed in vivo as part of the Gag/Pol polyprotein and, after autoprocessing out of the polyprotein, has a unit length of 116 amino acids, N-terminal Tyr, C-terminal Met
proteolytic modification
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the enzyme performs autolytic processing of precursor protein
proteolytic modification
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the enzyme performs autolytic processing of precursor protein
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