title: N-Terminal Methionine Processing.
abstract: Protein synthesis is initiated by methionine in eukaryotes and by formylmethionine in prokaryotes. N-terminal methionine can be co-translationally cleaved by the enzyme methionine aminopeptidase (MAP). When recombinant proteins are expressed in bacterial and mammalian expression systems, there is a simple universal rule that predicts whether the initiating methionine will be processed by MAP based on the size of the residue adjacent (penultimate) to the N-methionine. In general, if the side chains of the penultimate residues have a radius of gyration of 1.29 Å or less, methionine is cleaved. © 2017 by John Wiley & Sons, Inc.
authors.affiliation: Protein Expression Laboratory, NIAMS/NIH, Bethesda, Maryland.
authors.forename: Paul T
authors.initials: PT
authors.lastname: Wingfield
mesh_terms: D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics; D008715:Methionine / Q000378:metabolism*; D063208:Methionyl Aminopeptidases / Q000378:metabolism*; D014176:Protein Biosynthesis; D046188:Protein Modification, Translational; D011994:Recombinant Proteins / Q000096:biosynthesis*; D013379:Substrate Specificity
chemical_list: D011994:Recombinant Proteins; D008715:Methionine; D063208:Methionyl Aminopeptidases
keywords: N-terminal methionine; exopeptidase activity; methionine aminopepidases; protein synthesis