Methionyl aminopeptidase

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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

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 enzyme is present in both prokaryotes and eukaryotes.

References[edit]

  1. ^ Yoshida, A. and Lin, M. (1972). "NH2-terminal formylmethionine- and NH2-terminal methionine-cleaving enzymes in rabbits". J. Biol. Chem. 247: 952–957. PMID 4110013. 
  2. ^ Tsunasawa, S., Stewart, J.W. and Sherman, F. (1985). "Acylamino acid-releasing enzyme from rat liver". J. Biol. Chem. 260: 5832–5391. PMID 2985590. 
  3. ^ Freitas, J.O., Jr., Termignoni, C. and Guimaraes, J.A. (1985). "Methionine aminopeptidase associated with liver mitochondria and microsomes". Int. J. Biochem. 17: 1285–1291. PMID 3937747. 
  4. ^ Ben-Bassat, A., Bauer, K., Chang, S.-Y., Myambo, K., Boosman, A. and 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. PMID 3027045. 
  5. ^ Roderick, S.L. and Mathews, B.W. (1988). "Crystallization of methionine aminopeptidase from Escherichia coli". J. Biol. Chem. 263: 16531–16531. PMID 3141408. 

External links[edit]