Biology:Methionyl aminopeptidase
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Short description: Class of enzymes
| Methionyl aminopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.11.18 | ||||||||
| CAS number | 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 | ||||||||
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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. Human proteins possessing this activity include METAP1, METAP2, METAP1D (mitochondrial), and RNPEPL1.
References
- ↑ "NH2-terminal formylmethionine- and NH2-terminal methionine-cleaving enzymes in rabbits". J. Biol. Chem. 247 (3): 952–957. 1972. doi:10.1016/S0021-9258(19)45699-8. PMID 4110013.
- ↑ "Acylamino acid-releasing enzyme from rat liver". J. Biol. Chem. 260 (9): 5382–91. 1985. doi:10.1016/S0021-9258(18)89033-0. PMID 2985590.
- ↑ "Methionine aminopeptidase associated with liver mitochondria and microsomes". Int. J. Biochem. 17 (12): 1285–1291. 1985. doi:10.1016/0020-711x(85)90049-7. PMID 3937747.
- ↑ "Processing of the initiation methionine from proteins: properties of Escherichia coli methionine aminopeptidase and its gene structure". J. Bacteriol. 169 (2): 751–757. 1987. doi:10.1128/jb.169.2.751-757.1987. PMID 3027045.
- ↑ "Crystallization of methionine aminopeptidase from Escherichia coli". J. Biol. Chem. 263 (32): 16531. 1988. doi:10.1016/S0021-9258(18)37422-2. PMID 3141408.
External links
- Methionyl+aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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