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Literature summary for 3.4.22.2 extracted from

  • Menard, R.; Khouri, H.E.; Plouffe, C.; Dupras, R.; Ripoll, D.; Vernet, T.; Tessier, D.C.; Laliberte, F.; Thomas, D.Y.; Storer, A.C.
    A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papain (1990), Biochemistry, 29, 6706-6713.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
wild-type papain and D158N variant produced in a baculovirus insect cell expression system Carica papaya

Protein Variants

Protein Variants Comment Organism
D158N clear kinetic and pH depndence differences from the wild-type enzyme Carica papaya

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.4
-
benzyloxycarbonyl-L-Phe-L-Arg 4-methylcoumarin-7-amide recombinant wild-type enzyme Carica papaya
0.42
-
benzyloxycarbonyl-L-Phe-L-Arg 4-methylcoumarin-7-amide commercial enzyme preparation Carica papaya
1.8
-
benzyloxycarbonyl-L-citrullyl-L-Arg 4-methylcoumarin-7-amide mutant enzyme D158N Carica papaya

Organism

Organism UniProt Comment Textmining
Carica papaya
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Carica papaya

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-L-citrullyl-L-Arg-7-amido-4-methylcoumarin + H2O
-
Carica papaya benzyloxycarbonyl-L-citrullyl-L-Arg + 7-amino-4-methylcoumarin
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
-
Carica papaya benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
?
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin-7-amide + H2O
-
Carica papaya ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
51
-
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin recombinant wild-type enzyme Carica papaya
52
-
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin commercial enzyme preparation Carica papaya