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Literature summary for 3.4.22.28 extracted from

  • Sarkany, Z.; Polgar, L.
    The unusual catalytic triad of poliovirus protease 3C (2003), Biochemistry, 42, 516-522.
    View publication on PubMed
Search for more literature for 3.4.22.28

Protein Variants

Protein Variants Comment Organism
M27G indistinguishable from wild type enzyme Enterovirus C
M27G/C147S 430fold reduction in specificity rate constant, the bell-shaped curve for the modified enzyme is shifted towards the alkaline pH values by 0.45 units on the acidic side and by 0.9 units on the alkaline side. The reduced activity of the enzyme is primarily due to the less ordered ground state of ist reaction Enterovirus C

Organism

Organism UniProt Comment Textmining
Enterovirus C
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-aminobenzoic acid-Glu-Ala-Leu-Phe-Gln-Gly-Pro-Phe(NO2)-Ala + H2O
-
 Enterovirus C ?
-
 ?
2-aminobenzoic acid-Phe-Thr-Gln-Ser-Glu-Gly-Glu-Phe(NO2)-Ala + H2O poor substrate Enterovirus C ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
47
-
 pH 8.0, melting point of mutant enzyme M27G/C147S is 46.5, for mutant enzyme M37G it is 46.7°C Enterovirus C
48
-
 pH 8.5, melting point of mutant enzyme M27G/C147S is 47.7°C, for mutant enzyme M27G it is 48.1°C Enterovirus C
50
-
 pH 9.5, melting point of mutant enzyme M27G/C147S and M27G is 50.4, for mutant enzyme M27G it is 50.0°C Enterovirus C