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Literature summary extracted from

  • Stamper, C.; Bennett, B.; Edwards, T.; Holz, R.C.; Ringe, D.; Petsko, G.
    Inhibition of the aminopeptidase from Aeromonas proteolytica by L-leucinephosphonic acid. Spectroscopic and crystallographic characterization of the transition state of peptide hydrolysis (2001), Biochemistry, 40, 7035-7046.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.11.10 10 mg/ml purified enzyme, complexed with inhibitor L-leucinephosphonic acid from a 4fold molar excess, with precipitation solution containing Tris, pH 8.0, 10 mM KSCN, 0.4 M NaCl, 4 days, X-ray diffraction structure determination and analysis at 2.1 A resolution Vibrio proteolyticus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.10 L-leucine 4-nitroanilide
-
Vibrio proteolyticus
3.4.11.10 L-leucinephosphonic acid competitive, interacts with both metal ions in the dinuclear active site, inhibition mechanism Vibrio proteolyticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.11.10 additional information
-
additional information kinetics with metal-bound enzyme variants Vibrio proteolyticus
3.4.11.10 0.01
-
L-leucine 4-nitroanilide pH 8.0, 25°C Vibrio proteolyticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.10 Co2+ 2 Co2+ bound at the dinuclear active site, can be substituted by Zn2+, binding mode Vibrio proteolyticus
3.4.11.10 Zn2+ 2 Zn2+ bound at the dinuclear active site, can be substituted by Co2+, binding mode 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
-
Vibrio proteolyticus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.11.10 Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids. active site structure and mechanism Vibrio proteolyticus

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.11.10 120
-
purified Zn2+-bound enzyme Vibrio proteolyticus

Substrates and Products (Substrate)

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

EC Number Synonyms Comment Organism
3.4.11.10 AAP
-
Vibrio proteolyticus
3.4.11.10 Aeromonas proteolytica aminopeptidase
-
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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.11.10 4320
-
L-leucine 4-nitroanilide pH 8.0, 25°C 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 additional information
-
additional information kinetics with metal-bound enzyme variants Vibrio proteolyticus
3.4.11.10 0.0055
-
L-leucine 4-nitroanilide enzyme with 2 Co2+ or Zn2+ bound, pH 8.0, 25°C Vibrio proteolyticus
3.4.11.10 0.0066
-
L-leucinephosphonic acid metal free enzyme, pH 8.0, 25°C Vibrio proteolyticus