MAP E.coli

Methionine Aminopeptidase is a metalloenzyme, meaning it requires metal ions for its catalytic activity. The active site of MAP contains two adjacent divalent metal ions, typically cobalt (Co²⁺) or nickel (Ni²⁺), connected by a water molecule or hydroxide ion . These metal ions are essential for the enzyme’s function, as they facilitate the hydrolysis of the peptide bond at the N-terminal methionine.

Recombinant expression of Methionine Aminopeptidase in Escherichia coli (E. coli) involves the insertion of the gene encoding MAP into an E. coli expression system. This allows for the production of large quantities of the enzyme for research and industrial applications. The recombinant MAP is typically fused to a His-tag at the N-terminus, which aids in its purification using affinity chromatography techniques .

The recombinant E. coli Methionine Aminopeptidase has been characterized to have a molecular mass of approximately 31 kDa . It is a single, non-glycosylated polypeptide chain containing 284 amino acids . The enzyme exhibits high specificity for substrates with a methionine residue at the N-terminus and non-bulky, uncharged amino acids at the penultimate position .

Methionine Aminopeptidase is widely used in various biochemical and biotechnological applications. Its ability to remove the N-terminal methionine from recombinant proteins makes it valuable in protein engineering and production. Additionally, MAP is a potential target for the development of antibacterial drugs, as the NME process is essential for bacterial survival .