CATH Classification

Domain Context

CATH Clusters

Superfamily Creatinase/methionine aminopeptidase superfamily
Functional Family Methionine aminopeptidase

Enzyme Information
Methionyl aminopeptidase.
based on mapping to UniProt P0AE18
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
-!- This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides. -!- The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val). -!- Belongs to peptidase family M24A.

UniProtKB Entries (1)

Escherichia coli K-12
Methionine aminopeptidase

PDB Structure

PDB 2Q93
External Links
Organism Escherichia
Primary Citation
Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop flexibility in selective inhibition of bacterial enzymes.
Ma, Z.Q., Xie, S.X., Huang, Q.Q., Nan, F.J., Hurley, T.D., Ye, Q.Z.
Bmc Struct.Biol.