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Literature summary for 3.4.23.B10 extracted from

  • Grinde, B.; Cameron, C.E.; Leis, J.; Weber, I.T.; Wlodawer, A.; Burstein, H.; Skalka, A.M.
    Analysis of substrate interactions of the Rous sarcoma virus wild type and mutant proteases and human immunodeficiency virus-1 protease using a set of systematically altered peptide substrates (1992), J. Biol. Chem., 267, 9491-9498.
    View publication on PubMed
Search for more literature for 3.4.23.B10

Protein Variants

Protein Variants Comment Organism
R105P/G106V mutant enzyme exhibits behavior very similar to the wild-type enzyme for substitutions in the P4, P3, P2, P2', and P3' of the PPAVSLAMTMRR substrate positions. In contrast the mutants behave more like the HIV-1 protease in preference for amino acids substituted in the P1 and P1' positions Rous sarcoma virus
R105P/G106V/H65G mutant enzyme exhibits behavior very similar to the wild-type enzyme for substitutions in the P4, P3, P2, P2', and P3' of the PPAVSLAMTMRR substrate positions. In contrast the mutants behave more like the HIV-1 protease in preference for amino acids substituted in the P1 and P1' positions Rous sarcoma virus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information relative KM-values for the mutant enzymes R105P/106V and R105P/G106V/H65G with PPAVSLAMTMRR compared to the wild-type enzyme Rous sarcoma virus

Organism

Organism UniProt Comment Textmining
Rous sarcoma virus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information recombinant enzyme is purified from inclusion bodies in Escherichia coli Rous sarcoma virus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no cleavage of PPAVSLWMTMRR Rous sarcoma virus ?
-
 ?
PHAVSLAMTMRR + H2O
-
 Rous sarcoma virus PHAVS + LAMTMRR
-
 ?
PPAVALAMTMRR + H2O increase in activity of wild-type enzyme compared to PPAVSLAMTMRR Rous sarcoma virus PPAVA + LAMTMRR
-
 ?
PPAVELAMTMRR + H2O increase in activity of wild-type enzyme compared to PPAVSLAMTMRR Rous sarcoma virus PPAVE + LAMTMRR
-
 ?
PPAVHLAMTMRR + H2O increase in activity of wild-type enzyme compared to PPAVSLAMTMRR Rous sarcoma virus PPAVH + LAMTMRR
-
 ?
PPAVLLAMTMRR + H2O increase in activity of wild-type enzyme compared to PPAVSLAMTMRR Rous sarcoma virus PPAVL + LAMTMRR
-
 ?
PPAVRLAMTMRR + H2O increase in activity of wild-type enzyme compared to PPAVSLAMTMRR Rous sarcoma virus PPAVR + LAMTMRR
-
 ?
PPAVSLAMTMRR + H2O nucleocapsi-protease peptide substrate Rous sarcoma virus PPAVS + LAMTMRR
-
 ?
PPAVSLAYMRR + H2O increase in activity of wild-type enzyme compared to PPAVSLAMTMRR Rous sarcoma virus PPAVS + LAYTMRR
-
 ?
PPAVWLAMTMRR + H2O increase in activity of wild-type enzyme compared to PPAVSLAMTMRR Rous sarcoma virus PPAVW + LAMTMRR
-
 ?
PPDVSLAMTMRR + H2O slight increase in activity of wild-type enzyme compared to PPAVSLAMTMRR Rous sarcoma virus PPDVS + LAMTMRR
-
 ?
PPFVSLAMTMRR + H2O increase in activity of wild-type enzyme compared to PPAVSLAMTMRR Rous sarcoma virus PPFVS + LAMTMRR
-
 ?
PPHVSLAMTMRR + H2O increase in activity of wild-type enzyme compared to PPAVSLAMTMRR Rous sarcoma virus PPHVS + LAMTMRR
-
 ?
PPNVSLAMTMRR + H2O increase in activity of wild-type enzyme compared to PPAVSLAMTMRR Rous sarcoma virus PPNVS + LAMTMRR
-
 ?
PPRVSLAMTMRR + H2O increase in activity of wild-type enzyme compared to PPAVSLAMTMRR Rous sarcoma virus PPRVS + LAMTMRR
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information relative turnover numbers for the mutant enzymes R105P/106V and R105P/G106V/H65G with PPAVSLAMTMRR compared to the wild-type enzyme Rous sarcoma virus