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Literature summary for 3.4.11.2 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
Search for more literature for 3.4.11.2

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P04825
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
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
ePepN
-
 Escherichia coli