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Literature summary for 3.4.22.29 extracted from

  • Sarkany, Z.; Skern, T.; Polgar, L.
    Characterization of the active site thiol group of rhinovirus 2A proteinase (2000), FEBS Lett., 481, 289-292.
    View publication on PubMed
Search for more literature for 3.4.22.29

Organism

Organism UniProt Comment Textmining
Human rhinovirus sp.
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Human rhinovirus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-aminobenzoic acid-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Phe(NO2)-Ala-OH + H2O
-
 Human rhinovirus sp. ?
-
 ?
additional information the enzyme displays a charged aspartic acid, which may significantly influence the interaction between the thiol and imidazole groups Human rhinovirus sp. ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 reaction with 2-aminobenzoic acid-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Phe(NO2)-Ala-OH Human rhinovirus sp.

pH Range

pH Minimum pH Maximum Comment Organism
7 9 pH 7.0: about 50% of maximal activity, pH 9.0: about 35% of maximal activity, reaction with 2-aminobenzoic acid-Arg-Pro-Ile-Ile-Thr-Thr-Ala-Gly-Pro-Ser-Phe(NO2)-Ala-OH Human rhinovirus sp.