Methionyl_aminopeptidase

Methionyl aminopeptidase

Methionyl aminopeptidase

Class of enzymes

Methionyl aminopeptidase (EC 3.4.11.18, 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
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This membrane-bound enzymatic activity is present in both prokaryotes and eukaryotes. Human proteins possessing this activity include METAP1, METAP2, METAP1D (mitochondrial), and RNPEPL1.

References

  1. [1]
    Yoshida A, Lin M (1972). "NH2-terminal formylmethionine- and NH2-terminal methionine-cleaving enzymes in rabbits". J. Biol. Chem. 247 (3): 952–957. doi:10.1016/S0021-9258(19)45699-8. PMID 4110013.
  2. [2]
    Tsunasawa S, Stewart JW, Sherman F (1985). "Acylamino acid-releasing enzyme from rat liver". J. Biol. Chem. 260 (9): 5382–91. doi:10.1016/S0021-9258(18)89033-0. PMID 2985590.
  3. [3]
    Freitas JO, Termignoni C, Guimarães JA (1985). "Methionine aminopeptidase associated with liver mitochondria and microsomes". Int. J. Biochem. 17 (12): 1285–1291. doi:10.1016/0020-711x(85)90049-7. PMID 3937747.
  4. [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 (2): 751–757. doi:10.1128/jb.169.2.751-757.1987. PMC 211843. PMID 3027045.
  5. [5]
    Roderick SL, Matthews BW (1988). "Crystallization of methionine aminopeptidase from Escherichia coli". J. Biol. Chem. 263 (32): 16531. doi:10.1016/S0021-9258(18)37422-2. PMID 3141408.
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