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Literature summary for 3.4.23.B3 extracted from

  • Powell, D.J.; Bur, D.; Wlodawer, A.; Gustchina, A.; Dunn, B.M.; Kay, J.
    The aspartic proteinase from equine infectious anaemia virus (1998), Adv. Exp. Med. Biol., 436, 41-45.
    View publication on PubMed
Search for more literature for 3.4.23.B3

Protein Variants

Protein Variants Comment Organism
I54G the ability of the mutant enzyme to cleave the pseudosymmetrical peptide substrate Ac-Tyr-Arg-Ala-Arg-Val-Phe-4-nitrophenylalanyl-Val-Arg-Ala-Ala-Lys is more than an order of magnitude lower than that of the wild-type enzyme equine infectious anemia virus
I54G/Y48H specificity constant is only 3fold lower than that measured for the single mutant I54G enzyme, towards the long, pseudosymmetrical peptide substrate Ac-Tyr-Arg-Ala-Arg-Val-Phe-4-nitrophenylalanyl-Val-Arg-Ala-Ala-Lys. The potency of the shorter HBY-793 inhibitor is reduced by 60fold compared to the Ki values measured against the wild-type or the I54G mutant enzyme equine infectious anemia virus

Inhibitors

Inhibitors Comment Organism Structure
HBY-793
-
 equine infectious anemia virus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information equine infectious anemia virus the enzyme is essential for processing gag and gal-pol polyproteins in order to generate new infectious viral particles ?
-
 ?

Organism

Organism UniProt Comment Textmining
equine infectious anemia virus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is essential for processing gag and gal-pol polyproteins in order to generate new infectious viral particles equine infectious anemia virus ?
-
 ?