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Literature summary for 3.4.23.B10 extracted from

  • Cameron, C.E.; Burstein, H.; Bizub-Bender, D.; Ridky, T.; Weber, I.T.; Wlodawer, A.; Skalka, A.M.; Leis, J.
    Identification of amino acid residues of the retroviral aspartic proteinases important for substrate specificity and catalytic efficiency (1995), Adv. Exp. Med. Biol., 362, 399-406.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
A100L less than 1% of the activity relative to wild-type enzyme with PPAVSLAMTMRR Rous sarcoma virus
DELTAN61-Q63 245% of the activity relative to wild-type enzyme with PPAVSLAMTMRR Rous sarcoma virus
I42D 62% of the activity relative to wild-type enzyme with PPAVSLAMTMRR Rous sarcoma virus
I44V 211% of the activity relative to wild-type enzyme with PPAVSLAMTMRR Rous sarcoma virus
M73V 31% of the activity relative to wild-type enzyme with PPAVSLAMTMRR Rous sarcoma virus
M73V/A100L 96% of the activity relative to wild-type enzyme with PPAVSLAMTMRR Rous sarcoma virus
Q63M 448% of the activity relative to wild-type enzyme with PPAVSLAMTMRR Rous sarcoma virus
S107N 377% of the activity relative to wild-type enzyme with PPAVSLAMTMRR Rous sarcoma virus
S38T 200% of the activity relative to wild-type enzyme with PPAVSLAMTMRR Rous sarcoma virus
V104T 229% of the activity relative to wild-type enzyme with PPAVSLAMTMRR Rous sarcoma virus

Organism

Organism UniProt Comment Textmining
Rous sarcoma virus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
PPAVSLAMTMRR + H2O
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Rous sarcoma virus PPAVS + LAMTMRR
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