InterPro domain: IPR002467

This group of metallopeptidases belong to MEROPS peptidase family M24 (clan MG), subfamily M24A.

Methionine aminopeptidase ( 3.4.11.18 ) (MAP) catalyses the hydrolytic cleavage of the N-terminal methionine from newly synthesised polypeptides if the penultimate amino acid is small, with different tolerance to Val and Thr at this position [ 1 ]. All MAP studied to date are monomeric proteins that require cobalt ions for activity. Two subfamilies of MAP enzymes are known to exist [ 2 , 3 ]. While being evolutionary related, they only share a limited amount of sequence similarity, mostly clustered around the residues shown to be involved in cobalt-binding in Escherichia coli MAP [ 4 ]. Subfamily 1 consists of enzymes from prokaryotes as well as eukaryotic MAP-1, while the second group ( IPR002468 ) is made up of archaeal MAP and eukaryotic MAP-2.

1. Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases. Biochemistry 49, 5588-99
2. Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes. Proc. Natl. Acad. Sci. U.S.A. 92, 7714-8
3. Methionine aminopeptidase-1: the MAP of the mitochondrion? Trends Biochem. Sci. 21, 285-6
4. Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzyme. Biochemistry 32, 3907-12