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Literature summary extracted from

  • Wilkes, S.H.; Prescott, J.M.
    The slow, tight binding of bestatin and amastatin to aminopeptidases (1985), J. Biol. Chem., 260, 13154-13162.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.10 amastatin reversible, slow, tight binding, transition state analog complex, Ki: 0.58 nM, stoichiometry of inhibition 1:1 Vibrio proteolyticus
3.4.11.10 bestatin reversible, slow, tight binding, transition state analog complex, Ki: 18 nM, stoichiometry of inhibition 1:1 Vibrio proteolyticus
3.4.11.10 epibestatin Ki: 0.07 mM Vibrio proteolyticus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.11.10 Peptides + H2O Vibrio proteolyticus
-
 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.10 Vibrio proteolyticus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.10 Peptides + H2O
-
 Vibrio proteolyticus ?
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.11.10 25
-
 assay at Vibrio proteolyticus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.10 8
-
 assay at Vibrio proteolyticus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.11.10 0.000058
-
 amastatin reversible, slow, tight binding, transition state analog complex, stoichiometry of inhibition 1:1 Vibrio proteolyticus
3.4.11.10 0.07
-
 epibestatin
-
 Vibrio proteolyticus