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Literature summary for 3.4.21.69 extracted from

  • Steiner, S.A.; Castellino.F.J.
    Kinetic mechanism for stimulation by monovalent cations of the amidase activity of the plasma protease bovine activated protein C (1985), Biochemistry, 24, 609-617.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.43
-
 Nalpha-benzoyl-L-arginine 4-nitroanilide with Cs+ as activating cation Bos taurus
0.9
-
 Nalpha-benzoyl-L-arginine 4-nitroanilide with Na+ as activating cation Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Cs+ activates, Km: 11 mM Bos taurus
additional information the enzyme displays a strict requirement for monovalent cations in its expression of amidolytic activity towards Nalpha-benzoyl-L-arginine 4-nitroanilide Bos taurus
Na+ activates, Km: 87 mM Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
plasma
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Nalpha-benzoyl-L-Arg 4-nitroanilide + H2O amidase activity Bos taurus Nalpha-benzoyl-L-Arg + 4-nitroaniline
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.32
-
 Nalpha-benzoyl-L-arginine 4-nitroanilide with Na+ or Cs+ as activating cation Bos taurus