Metionilna aminopeptidaza

Metionilna aminopeptidaza (EC 3.4.11.18, metioninska aminopeptidaza, peptidaza M, L-metioninska aminopeptidaza, MAP) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju

Metionilna aminopeptidaza
Identifikatori
EC broj 3.4.11.18
CAS broj 61229-81-0
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum
Oslobađanje N-terminalne aminokiseline, preferentno metionina, sa peptida i arilamida

Ovaj za membranu vezani enzim je prisutan kod prokariota i eukariota.

Reference uredi

  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. 

Literatura uredi

Spoljašnje veze uredi