Methionine Aminopeptidase

The methionine aminopeptidases represent a novel class of metalloprotease generally having two cobalt ions in the active site. The proteins consist of two topologically similar domains folded with a ‘pita-bread’ motif. Structural analysis of various inhibitor complexes with the Escherichia coli enzyme and other members of the family have suggested a putative mechanism of catalysis related to that originally proposed for thermolysin.

3D Structure

3D Structure Overall ‘pita-bread’ fold of E. coli methionine aminopeptidase. The two metal ions are shown in red. Figure courtesy of Todd Lowther. PDB Code 2MAT.

Keywords: methionine aminopeptidase; cobalt; cancer; fumagillin; bestatin; thermolysin