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 P53582
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)

P53582
MAP11_HUMAN
Homo sapiens
Methionine aminopeptidase 1

PDB Structure

PDB 2B3K
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structural Basis for the Functional Differences between Type I and Type II Human Methionine Aminopeptidases(,).
Addlagatta, A., Hu, X., Liu, J.O., Matthews, B.W.
Biochemistry