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Literature summary extracted from

  • Ataie, N.J.; Hoang, Q.Q.; Zahniser, M.P.; Tu, Y.; Milne, A.; Petsko, G.A.; Ringe, D.
    Zinc coordination geometry and ligand binding affinity: the structural and kinetic analysis of the second-shell serine 228 residue and the methionine 180 residue of the aminopeptidase from Vibrio proteolyticus (2008), Biochemistry, 47, 7673-7683.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.11.10 hanging drop vapour diffusion method, at 25°C Vibrio proteolyticus

Protein Variants

EC Number Protein Variants Comment Organism
3.4.11.10 D118N mutant shows similar activity compared to the wild type enzyme Vibrio proteolyticus
3.4.11.10 M180A mutant shows severly reduced activity (approximately 100fold less active) compared to the wild type enzyme Vibrio proteolyticus
3.4.11.10 S228A mutant shows strongly reduced activity (approximately 10fold less active) compared to the wild type enzyme Vibrio proteolyticus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.10 L-leucine competitive inhibition Vibrio proteolyticus
3.4.11.10 leucine phosphonic acid competitive inhibition Vibrio proteolyticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.11.10 0.01
-
 L-Leu-4-nitroanilide mutant enzyme D118N, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C Vibrio proteolyticus
3.4.11.10 0.013
-
 L-Leu-4-nitroanilide wild type enzyme, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C Vibrio proteolyticus
3.4.11.10 0.025
-
 L-Leu-4-nitroanilide mutant enzyme S228A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C Vibrio proteolyticus
3.4.11.10 0.34
-
 L-Leu-4-nitroanilide mutant enzyme M180A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C Vibrio proteolyticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.10 Zn2+ two zinc ions in close proximity have been identified to form the metal component of the active site Vibrio proteolyticus

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.10 Vibrio proteolyticus Q01693
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.10 ammonium sulfate precipitation and Mono-Q column chromatography Vibrio proteolyticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.10 L-Leu-4-nitroanilide + H2O
-
 Vibrio proteolyticus L-Leu + 4-nitroaniline
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.11.10 AAP
-
 Vibrio proteolyticus
3.4.11.10 Aminopeptidase
-
 Vibrio proteolyticus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.11.10 0.7
-
 L-Leu-4-nitroanilide mutant enzyme M180A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C Vibrio proteolyticus
3.4.11.10 7
-
 L-Leu-4-nitroanilide mutant enzyme S228A, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C Vibrio proteolyticus
3.4.11.10 60
-
 L-Leu-4-nitroanilide mutant enzyme D118N, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C Vibrio proteolyticus
3.4.11.10 65
-
 L-Leu-4-nitroanilide wild type enzyme, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C Vibrio proteolyticus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.4.11.10 0.0019
-
 L-leucine wild type enzyme, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C Vibrio proteolyticus
3.4.11.10 0.0019
-
 leucine phosphonic acid wild type enzyme, in 50 mM Tricine buffer, 1.0 mM ZnSO4, and 200 mM KCl, at pH 8.0 and 25°C Vibrio proteolyticus