Removal of N-terminal methionine from haemoglobin nascent peptides by a membrane-bound rat liver methionine aminopeptidase.
A membrane-bound aminopeptidase able to remove methionine from haemoglobin nascent peptides is described. The enzyme also hydrolyses methionine from methionyl-lysyl-bradykinin but not lysine from lysyl-bradykinin. The tripeptide Met-Ala-Ser is poorly hydrolysed. This aminopeptidase also splits amino acid 2-naphthylamides, being, however, less specific with respect to these synthetic substrates.
D000577:Amides / Q000378:metabolism; D000626:Aminopeptidases / Q000378:metabolism*; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D002848:Chromatography, DEAE-Cellulose; D006454:Hemoglobins / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008715:Methionine / Q000378:metabolism*; D063208:Methionyl Aminopeptidases; D009281:Naphthalenes / Q000378:metabolism; D010455:Peptides / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D000577:Amides; D006454:Hemoglobins; D009281:Naphthalenes; D010455:Peptides; D008715:Methionine; D000626:Aminopeptidases; D063208:Methionyl Aminopeptidases