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Literature summary for 3.4.11.10 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
Search for more literature for 3.4.11.10

Crystallization (Commentary)

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

Protein Variants

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

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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
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
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

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

Organism

Organism UniProt Comment Textmining
Vibrio proteolyticus Q01693
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
AAP
-
 Vibrio proteolyticus
Aminopeptidase
-
 Vibrio proteolyticus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
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
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
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
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]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
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
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