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: 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, 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 Mathews, B.W. Crystallization of methionine aminopeptidase from Escherichia coli. J. Biol. Chem. 263 (1988) 16531. [PMID: 89034132]
[EC 3.4.11.18 created 1990]
 
 


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