EC 3.4.11.18 - Methionyl aminopeptidase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 3.4.11.18

Names

Accepted name:
methionyl aminopeptidase
Other names:
L-methionine aminopeptidase
MAP
methionine aminopeptidase
peptidase M
Systematic name:
-

Reaction

Cofactor

Comments:

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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , MEROPS , UniPathway
Protein domains and families: PROSITE:PDOC00575
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004239
CAS Registry Number: 61229-81-0
UniProtKB/Swiss-Prot: (174) [show] [UniProt]

References

  1. Yoshida, A. and Lin, M.
    NH2-terminal formylmethionine- and NH2-terminal methionine-cleaving enzymes in rabbits.
    J. Biol. Chem. 247: 952-957 (1972). [PMID: 4110013]
  2. Tsunasawa, S., Stewart, J.W. and Sherman, F.
    Acylamino acid-releasing enzyme from rat liver.
    J. Biol. Chem. 260: 5832-5391 (1985). [PMID: 2985590]
  3. Freitas, J.O., Jr, Termignoni, C. and Guimaraes, J.A.
    Methionine aminopeptidase associated with liver mitochondria and microsomes.
    Int. J. Biochem. 17: 1285-1291 (1985). [PMID: 3937747]
  4. Ben-Bassat, A., Bauer, K., Chang, S.-Y., Myambo, K., Boosman, A. and Chang, S.
    Processing of the initiation methionine from proteins: properties of Escherichia coli methionine aminopeptidase and its gene structure.
    J. Bacteriol. 169: 751-757 (1987). [PMID: 3027045]
  5. Roderick, S.L. and Mathews, B.W.
    Crystallization of methionine aminopeptidase from Escherichia coli.
    Biol. Chem. 263: 16531 (1988). [PMID: 3141408]

[EC 3.4.11.18 created 1990]