CATH Classification

Domain Context

CATH Clusters

Superfamily Creatinase/methionine aminopeptidase superfamily
Functional Family Methionine aminopeptidase

Enzyme Information

3.4.11.18
Methionyl aminopeptidase.
based on mapping to UniProt P9WK19
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)

P9WK19
MAP12_MYCTU
Mycobacterium tuberculosis H37Rv
Methionine aminopeptidase 2

PDB Structure

PDB 1Y1N
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Identification of an SH3-Binding Motif in a New Class of Methionine Aminopeptidases from Mycobacterium tuberculosis Suggests a Mode of Interaction with the Ribosome
Addlagatta, A., Quillin, M.L., Omotoso, O., Liu, J.O., Matthews, B.W.
Biochemistry
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