| 词条 | Methionyl aminopeptidase |
| 释义 |
| Name = Methionyl aminopeptidase | EC_number = 3.4.11.18 | CAS_number = 61229-81-0 | IUBMB_EC_number = 3/4/11/18 | GO_code = | image = | width = | caption = }}Methionyl aminopeptidase ({{EC number|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 This membrane-bound enzymatic activity is present in both prokaryotes and eukaryotes. Proteins possessing this activity include METAP1 and METAP2. References1. ^{{cite journal | vauthors = Yoshida A, Lin M | title = NH2-terminal formylmethionine- and NH2-terminal methionine-cleaving enzymes in rabbits | journal = J. Biol. Chem. | volume = 247 | pages = 952–957 | year = 1972 | pmid = 4110013 }} 2. ^{{cite journal | vauthors = Tsunasawa S, Stewart JW, Sherman F | title = Acylamino acid-releasing enzyme from rat liver | journal = J. Biol. Chem. | volume = 260 | pages = 5382–91| year = 1985 | pmid = 2985590 }} 3. ^{{cite journal | vauthors = Freitas JO, Termignoni C, Guimarães JA | title = Methionine aminopeptidase associated with liver mitochondria and microsomes | journal = Int. J. Biochem. | volume = 17 | pages = 1285–1291 | year = 1985 | pmid = 3937747 }} 4. ^{{cite journal | vauthors = Ben-Bassat A, Bauer K, Chang SY, Myambo K, Boosman A, Chang S | title = Processing of the initiation methionine from proteins: properties of Escherichia coli methionine aminopeptidase and its gene structure | journal = J. Bacteriol. | volume = 169 | pages = 751–757 | year = 1987 | pmid = 3027045 | pmc=211843}} 5. ^{{cite journal | vauthors = Roderick SL, Matthews BW | title = Crystallization of methionine aminopeptidase from Escherichia coli | journal = J. Biol. Chem. | volume = 263 | pages = 16531-16531 | year = 1988 | pmid = 3141408 }} External links
1 : EC 3.4.11 |
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