From Wikipedia, the free encyclopedia
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
Search
PMC articles
PubMed articles
NCBI proteins

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

  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. ^ 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. ^ 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. ^ 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. ^ 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.
From Wikipedia, the free encyclopedia
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
Search
PMC articles
PubMed articles
NCBI proteins

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

  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. ^ 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. ^ 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. ^ 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. ^ 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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