Reaction: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides
Other names: methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP
Comments: Membrane-bound enzyme present in both prokaryotes and eukaryotes. Type example of peptidase family M24. Releases methionine from nascent peptides
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 61229-81-0
References
1. Yoshida, A. and Lin, M. NH2-terminal formylmethionine- and NH2-terminal methionine-cleaving enzymes in rabbits. J. Biol. Chem. 247 (1972) 952-957. [PMID: 4110013]
2. Tsunasawa, S., Stewart, J.W. and Sherman, F. Acylamino acid-releasing enzyme from rat liver. J. Biol. Chem. 260 (1985) 5832-5391. [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 (1985) 1285-1291. [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 (1987) 751-757. [PMID: 3027045]
5. Roderick, S.L. and Mathews, B.W. Crystallization of methionine aminopeptidase from Escherichia coli. J. Biol. Chem. 263 (1988) 16531 only. [PMID: 3141408]