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Literature summary extracted from

  • Addlagatta, A.; Gay, L.; Matthews, B.W.
    Structural basis for the unusual specificity of Escherichia coli aminopeptidase N (2008), Biochemistry, 47, 5303-5311.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.2 expressed in Escherichia coli BL21 (DE3) cells Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.11.2 in complex with the amino acids L-arginine, L-lysine, L-phenylalanine, L-tryptophan, and L-tyrosine, hanging drop vapour diffusion method Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.11.2 membrane
-
 Escherichia coli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.4.11.2 Zn2+ contains zinc Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.2 Escherichia coli P04825
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.11.2 cobalt-affinity resin chromatography Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.4.11.2 0.044
-
 using L-Phe-L-Phe as substrate, in 25 mM sodium phosphate at pH 7.5 Escherichia coli
3.4.11.2 0.046
-
 using L-Tyr-L-Phe as substrate, in 25 mM sodium phosphate at pH 7.5 Escherichia coli
3.4.11.2 0.142
-
 using L-Lys-L-Phe as substrate, in 25 mM sodium phosphate at pH 7.5 Escherichia coli
3.4.11.2 0.154
-
 using L-Ala-L-Phe as substrate, in 25 mM sodium phosphate at pH 7.5 Escherichia coli
3.4.11.2 0.214
-
 using L-Arg-L-Phe as substrate, in 25 mM sodium phosphate at pH 7.5 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.2 L-Ala-L-Phe + H2O
-
 Escherichia coli L-Ala + L-Phe
-
 ?
3.4.11.2 L-Arg-L-Phe + H2O
-
 Escherichia coli L-Arg + L-Phe
-
 ?
3.4.11.2 L-Lys-L-Phe + H2O
-
 Escherichia coli L-Lys + L-Phe
-
 ?
3.4.11.2 L-Phe-L-Phe + H2O
-
 Escherichia coli L-Phe + L-Phe
-
 ?
3.4.11.2 L-Tyr-L-Phe + H2O
-
 Escherichia coli L-Tyr + L-Phe
-
 ?
3.4.11.2 additional information no activity with L-Asp-L-Phe Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.11.2 aminopeptidase N the enzyme has unusual specificity, cleaving adjacent to the large, nonpolar amino acids Phe and Tyr but also cleaving next to the polar residues Lys and Arg Escherichia coli
3.4.11.2 ePepN
-
 Escherichia coli