Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.23.B4 extracted from

  • Elder, J.H.; Sundstrom, M.; de Rozieres, S.; de Parseval, A.; Grant, C.K.; Lin, Y.C.
    Molecular mechanisms of FIV infection (2008), Vet. Immunol. Immunopathol., 123, 3-13.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.23.B4

Application

Application Comment Organism
medicine PR is an important target for antiviral therapies since PR is reponsible for the processing of viral Gag and Gag-Pol polyproteins into individual structural and enzymatic proteins during assembly and maturation. This proteolytic step is highly specific, ordered and essential for producing mature and infectious retrovirus particles feline immunodeficiency virus

Crystallization (Commentary)

Crystallization (Comment) Organism
the two enzymes FIV protease and HIV-1 protease are strikingly similar at the crystallographic level, particularly within the substrate binding region feline immunodeficiency virus

Inhibitors

Inhibitors Comment Organism Structure
additional information inhibitors of HIV-1 protease currently employed in clinic do not inhibit FIV protease despite similarities between HIV-1 PR and FIV PR feline immunodeficiency virus

Organism

Organism UniProt Comment Textmining
feline immunodeficiency virus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information both FIV and HIV-1 PRs recognize, the P4-P4’ residues of peptide substrates via a long cavity in the middle of the protease. Both homodimeric PRs utilize an acid-base hydrolysis mechanism in which aspartic acids 30 and 30’ activate a water molecule to perform a nucleophilic attack on the amide carbonyl between the P1 and P1’ positions in various peptide substrates feline immunodeficiency virus ?
-
 ?
additional information FIV protease cleaves the FIV MA/CA cleavage junction efficiently. It does not cut the HIV-1 MA/CA cleavage junction, despite the presence of four identical residues in the P3-P3' position feline immunodeficiency virus ?
-
 ?
additional information there are three major structurally conserved regions that make up the substrate binding pockets of PR: (1) the active core region residues 30-38 for FIV (2) the flap residues 54-60 for FIV and (3) C-terminal ‘‘90’s loop’’ region residues 98-101 for FIV. Within these regions, there are 11 amino acids that differ between FIV and HIV-1 proteases. The 11 different amino acid residues in the S4-S4’ subsites of FIV protease, Ile35, Ile37, Gln54, Asn55, Met56, Ile57, Val59, Ile98, Gln99, Pro100 and Leu101, most likely account for the specificity of the substrate/inhibitor binding feline immunodeficiency virus ?
-
 ?

Subunits

Subunits Comment Organism
homodimer with each monomer consisting of 116 amino acids feline immunodeficiency virus

Synonyms

Synonyms Comment Organism
FIV protease
-
 feline immunodeficiency virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4 5
-
 feline immunodeficiency virus