Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Huntington, K.M.; Bienvenue, D.L.; Wei, Y.; Bennett, B.; Holz, R.C.; Pei, D.
    Slow-binding inhibition of the aminopeptidase from Aeromonas proteolytica by peptide thiols: synthesis and spectroscopic characterization (1999), Biochemistry, 38, 15587-15596.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.10 additional information
-
 Vibrio proteolyticus
3.4.11.10 N-mercaptoacyl-leucyl-p-nitroaniline synthethic inhibitor, and derivatives, spectroscopic study of slow-binding inhibition, Ki: 2.5-57 nM 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 ?
-
 ?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.11.10 0.0000025 0.000057 N-mercaptoacyl-leucyl-p-nitroaniline synthethic inhibitor, and derivatives, spectroscopic study of slow-binding inhibition Vibrio proteolyticus