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Literature summary for 3.4.11.2 extracted from

  • Ito, K.; Nakajima, Y.; Onohara, Y.; Takeo, M.; Nakashima, K.; Matsubara, F.; Ito, T.; Yoshimoto, T.
    Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition (2006), J. Biol. Chem., 281, 33664-33676.
    View publication on PubMed
Search for more literature for 3.4.11.2

Crystallization (Commentary)

Crystallization (Comment) Organism
ligand-free protein and complex with bestatin at 1.5 and 1.6 A resolution, respectively. The enzyme is composed of an N-terminal beta-domain, a catalytic domain, a middle beta-domain, and a C-terminal alpha-domain. Residues E298 and Y381 located near the zinc ion, are involved in peptide cleavage. Residue M260 functions as a cushion to accept substrates with different N-terminal resiude sizes Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
bestatin the N-terminus of bestatin is recognized by residues E121 and E264 Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ coordinated by residues H297, H301, E320, and a water molecule Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
Release of an N-terminal amino acid, Xaa-/-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide residues E298 and Y381 located near the zinc ion, are involved in peptide cleavage. Residue M260 functions as a cushion to accept substrates with different N-terminal resiude sizes Escherichia coli
a