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Literature summary for 3.4.24.17 extracted from

  • Salowe, S.P.; Marcy, A.I.; Cuca, G.C.; Smith, C.K.; Kopka, I.E.; Hagmann, W.K.; Hermes, J.D.
    Characterization of zinc-binding sites in human stromelysin-1: stoichiometry of the catalytic domain and identification of a cysteine ligand in the proenzyme (1992), Biochemistry, 31, 4535-4540.
    View publication on PubMed
Search for more literature for 3.4.24.17

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Hydroxamate-containing peptide inhibitor
-
 Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.9
-
 Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-norleucine-NH2 wild-type enzyme form Homo sapiens
1.4
-
 Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-norleucine-NH2 truncated enzyme form Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 expression in Escherichia coli
-
Homo sapiens
-
 prostromelysin (treatment with (aminophenyl)mercuric acetate results in activation)
-

Purification (Commentary)

Purification (Comment) Organism
expression in Escherichia coli Homo sapiens
prostromelysin (treatment with (aminophenyl)mercuric acetate results in activation) Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Nle-NH2 + H2O
-
 Homo sapiens ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.9
-
 Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Nle-NH2 wild-type enzyme form Homo sapiens
1.35
-
 Arg-Pro-Lys-Pro-Gln-Gln-Phe-Phe-Gly-Leu-Nle-NH2 truncated enzyme form Homo sapiens