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Literature summary for 3.4.23.21 extracted from

  • Hofmann, T.; Hodges, R.S.; James, M.N.G.
    Effect of pH on the activities of penicillopepsin and Rhizopus pepsin and a proposal for the productive substrate binding mode in penicillopepsin (1984), Biochemistry, 23, 635-643.
    View publication on PubMed
Search for more literature for 3.4.23.21

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.23
-
 Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala pH 6.0 Rhizopus sp.
1.1
-
 Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala pH 2.0 Rhizopus sp.

Organism

Organism UniProt Comment Textmining
Rhizopus sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ac-Ala-Ala-(4-nitro)Phe-Ala-Ala + H2O
-
 Rhizopus sp. ?
-
 ?
Ac-Ala-Ala-Lys-(4-nitro)Phe-Ala-Ala + H2O
-
 Rhizopus sp. Ac-Ala-Ala-Lys + (4-nitro)Phe-Ala-Ala
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Rhizopus sp.