Methionyl aminopeptidase explained

Methionyl aminopeptidase
Ec Number:	3.4.11.18
Cas Number:	61229-81-0

Methionyl aminopeptidase (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. Human proteins possessing this activity include METAP1, METAP2, METAP1D (mitochondrial), and RNPEPL1.

Notes and References

1. Yoshida A, Lin M . NH₂-terminal formylmethionine- and NH₂-terminal methionine-cleaving enzymes in rabbits . J. Biol. Chem. . 247 . 952–957 . 1972 . 3 . 10.1016/S0021-9258(19)45699-8 . 4110013 . free .
2. Tsunasawa S, Stewart JW, Sherman F . Acylamino acid-releasing enzyme from rat liver . J. Biol. Chem. . 260 . 5382–91. 1985 . 9 . 10.1016/S0021-9258(18)89033-0 . 2985590 . free .
3. Freitas JO, Termignoni C, Guimarães JA . Methionine aminopeptidase associated with liver mitochondria and microsomes . Int. J. Biochem. . 17 . 1285–1291 . 1985 . 12 . 10.1016/0020-711x(85)90049-7 . 3937747 .
4. Ben-Bassat A, Bauer K, Chang SY, Myambo K, Boosman A, Chang S . Processing of the initiation methionine from proteins: properties of Escherichia coli methionine aminopeptidase and its gene structure . J. Bacteriol. . 169 . 751–757 . 1987 . 2 . 10.1128/jb.169.2.751-757.1987 . 3027045 . 211843.
5. Roderick SL, Matthews BW . Crystallization of methionine aminopeptidase from Escherichia coli . J. Biol. Chem. . 263 . 16531 . 1988 . 32 . 10.1016/S0021-9258(18)37422-2 . 3141408 . free .