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Literature summary extracted from

  • Suzuki, H.; Kamatani, S.; Kumagai, H.
    Purification and characterization of aminopeptidase B from Escherichia coli K-12 (2001), Biosci. Biotechnol. Biochem., 65, 1549-1558.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.6 Cd2+ inhibits Cd2+-saturated enzyme, inhibits the Ni2+-saturated enzyme Escherichia coli
3.4.11.6 Co2+ inhibits Cd2+-saturated enzyme, inhibits the Ni2+-saturated enzyme Escherichia coli
3.4.11.6 EDTA complete loss of activity after dialysis with EDTA Escherichia coli
3.4.11.6 Fe2+ inhibits the Ni2+-saturated enzyme Escherichia coli
3.4.11.6 Ni2+ inhibits Cd2+-saturated enzyme Escherichia coli
3.4.11.6 Zn2+ inhibits Cd2+-saturated enzyme, inhibits the Ni2+-saturated enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.11.6 4.9
-
 Leu-4-nitroanilide pH 7.5, 37°C Escherichia coli
3.4.11.6 7.8
-
 Cys-Gly pH 7.5, 37°C Escherichia coli
3.4.11.6 13.5
-
 Leu-Gly pH 7.5, 37°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.6 Cd2+ activates Escherichia coli
3.4.11.6 Co2+ activates. Enzyme contains 0.00063 atoms per subunit, wild-type enzyme Escherichia coli
3.4.11.6 KCl enhances activity, maximal activation at 50 mM Escherichia coli
3.4.11.6 Mn2+ activates. Enzyme contains 0.0026 atoms per subunit, wild-type enzyme Escherichia coli
3.4.11.6 NaCl enhances activity Escherichia coli
3.4.11.6 NH4Cl enhances activity, maximal activation at 100 mM Escherichia coli
3.4.11.6 Ni2+ activates Escherichia coli
3.4.11.6 Zn2+ enzyme contains 0.036 atoms per subunit, wild-type enzyme Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.6 Escherichia coli
-
 K 12
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.6
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.6 Ala-4-nitroanilide + H2O 4.6% of the activity with Leu-4-nitroanilide Escherichia coli Ala + 4-nitroaniline
-
 ?
3.4.11.6 alpha-Glu-4-nitroanilide + H2O 564% of the activity with Leu-4-nitroanilide Escherichia coli Glu + 4-nitroaniline
-
 ?
3.4.11.6 Arg-4-nitroanilide + H2O 2.5% of the activity with Leu-4-nitroanilide Escherichia coli Arg + 4-nitroaniline
-
 ?
3.4.11.6 Cys-Gly + H2O 4210% of the activity with Leu-4-nitroanilide Escherichia coli Cys + Gly
-
 ?
3.4.11.6 Gly-4-nitroanilide + H2O 1.3% of the activity with Leu-4-nitroanilide Escherichia coli Gly + 4-nitroaniline
-
 ?
3.4.11.6 Leu-4-nitroanilide + H2O
-
 Escherichia coli Leu + 4-nitroaniline
-
 ?
3.4.11.6 Leu-Gly + H2O 1200% of the activity with Leu-4-nitroanilide Escherichia coli Leu + Gly
-
 ?
3.4.11.6 Met-4-nitroanilide + H2O 40.6% of the activity with Leu-4-nitroanilide Escherichia coli Met + 4-nitroaniline
-
 ?
3.4.11.6 Val-4-nitroanilide + H2O 1.2% of the activity with Leu-4-nitroanilide Escherichia coli Val + 4-nitroaniline
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.11.6 additional information
-
 stabilized against heat in the presence of Mn2+ or Co2+ Escherichia coli
3.4.11.6 55
-
 EDTA-dialyzed enzyme is completely inactivated within 2 min. The enzyme of which the divalent cation has has been replaced with Mn2+ or Co2+ is quite stable up to 10 min. The Mn2+-dialyzed sample gradually loses its activity, only 75% of its original levels remains after 10 min Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.11.6 307
-
 Leu-4-nitroanilide pH 7.5, 37°C Escherichia coli
3.4.11.6 6630
-
 Leu-Gly pH 7.5, 37°C Escherichia coli
3.4.11.6 10700
-
 Cys-Gly pH 7.5, 37°C Escherichia coli