The Enzyme Database

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EC 3.4.11.18     
Accepted name: methionyl aminopeptidase
Reaction: Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides
Other name(s): methionine aminopeptidase; peptidase M; L-methionine aminopeptidase; MAP
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).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, 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. [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 Matthews, B.W. Crystallization of methionine aminopeptidase from Escherichia coli. J. Biol. Chem. 263:16531 (1988). [PMID: 3141408]
[EC 3.4.11.18 created 1990]
 
 


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