Methionyl aminopeptidase
| Methionyl aminopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.11.18 | ||||||||
| CAS no. | 61229-81-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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
This membrane-bound enzymatic activity is present in both prokaryotes and eukaryotes. Proteins possessing this activity include METAP1 and METAP2.
References
- ^ Yoshida A, Lin M (1972). "NH2-terminal formylmethionine- and NH2-terminal methionine-cleaving enzymes in rabbits". J. Biol. Chem. 247: 952–957. PMID 4110013.
- ^ Tsunasawa S, Stewart JW, Sherman F (1985). "Acylamino acid-releasing enzyme from rat liver". J. Biol. Chem. 260: 5382–91. PMID 2985590.
- ^ Freitas JO, Termignoni C, Guimarães JA (1985). "Methionine aminopeptidase associated with liver mitochondria and microsomes". Int. J. Biochem. 17: 1285–1291. PMID 3937747.
- ^ 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 211843. PMID 3027045.
- ^ Roderick SL, Matthews BW (1988). "Crystallization of methionine aminopeptidase from Escherichia coli". J. Biol. Chem. 263: 16531–16531. PMID 3141408.
External links
- Methionyl+aminopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
