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.

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

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.23 Aspartic endopeptidases

                3.4.23.B4 Feline immunodeficiency virus protease

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Results	in table
3	AA Sequence
5	Application
1	CAS Registry Number
5	Cloned(Commentary)
8	Crystallization (Commentary)
2	General Information
39	IC50 Value
64	Inhibitors
7	Ki Value [mM]
30	KM Value [mM]
2	Metals/Ions
2	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
29	Organism
3	pH Optimum
1	pH Stability
3	Posttranslational Modification
53	Protein Variants
3	Purification (Commentary)
4	Reaction
1	Reaction Type
25	Reference
52	Substrates and Products (Substrate)
5	Subunits
22	Synonyms
2	Temperature Optimum [°C]
1	Temperature Stability [°C]
26	Turnover Number [1/s]

Reaction

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Reaction on EC 3.4.23.B4 - Feline immunodeficiency virus protease

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

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

3 entries

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 the HIV-1 protease the feline immunodeficiency virus protease does not cleave the peptide KSGNFVVNGLVK at the Phe-Val bond. Asn in P2 may be inhibitory

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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

structure-function relationship and analysis, Asp30 is the catalytic residue

feline immunodeficiency virus

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668799

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

structure-function relationship and analysis, Asp30 is the catalytic residue

feline immunodeficiency virus FIV

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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

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