CATH Classification

Domain Context

CATH Clusters

Superfamily Creatinase/methionine aminopeptidase superfamily
Functional Family Methionine aminopeptidase 2

Enzyme Information

3.4.11.18
Methionyl aminopeptidase.
based on mapping to UniProt P50579
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)

P50579
MAP2_HUMAN
Homo sapiens
Methionine aminopeptidase 2

PDB Structure

PDB 1YW7
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Discovery and optimization of anthranilic acid sulfonamides as inhibitors of methionine aminopeptidase-2: a structural basis for the reduction of albumin binding.
Sheppard, G.S., Wang, J., Kawai, M., Fidanze, S.D., BaMaung, N.Y., Erickson, S.A., Barnes, D.M., Tedrow, J.S., Kolaczkowski, L., Vasudevan, A., Park, D.C., Wang, G.T., Sanders, W.J., Mantei, R.A., Palazzo, F., Tucker-Garcia, L., Lou, P., Zhang, Q., Park, C.H., Kim, K.H., Petros, A., Olejniczak, E., Nettesheim, D., Hajduk, P., Henkin, J., Lesniewski, R., Davidsen, S.K., Bell, R.L.
J.Med.Chem.
CATH-Gene3D is a Global Biodata Core Resource Learn more...