Methionyl aminopeptidase

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Methionyl aminopeptidase
EC number
CAS number 61229-81-0
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Methionyl aminopeptidase (EC, methionine aminopeptidase, peptidase M, L-methionine aminopeptidase, MAP) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides

This membrane-bound enzymatic activity is present in both prokaryotes and eukaryotes. Proteins possessing this activity include METAP1 and METAP2.


  1. ^ Yoshida A, Lin M (1972). "NH2-terminal formylmethionine- and NH2-terminal methionine-cleaving enzymes in rabbits". J. Biol. Chem. 247: 952–957. PMID 4110013. 
  2. ^ Tsunasawa S, Stewart JW, Sherman F (1985). "Acylamino acid-releasing enzyme from rat liver". J. Biol. Chem. 260: 5382–91. PMID 2985590. 
  3. ^ Freitas JO, Termignoni C, Guimarães JA (1985). "Methionine aminopeptidase associated with liver mitochondria and microsomes". Int. J. Biochem. 17: 1285–1291. PMID 3937747. 
  4. ^ Ben-Bassat A, Bauer K, Chang SY, Myambo K, Boosman A, Chang S (1987). "Processing of the initiation methionine from proteins: properties of Escherichia coli methionine aminopeptidase and its gene structure". J. Bacteriol. 169: 751–757. PMC 211843Freely accessible. PMID 3027045. 
  5. ^ Roderick SL, Matthews BW (1988). "Crystallization of methionine aminopeptidase from Escherichia coli". J. Biol. Chem. 263: 16531–16531. PMID 3141408. 

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