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 | Comment | Organism | Structure |
---|---|---|---|
bestatin | the N-terminus of bestatin is recognized by residues E121 and E264 | Escherichia coli |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | coordinated by residues H297, H301, E320, and a water molecule | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
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 |