Protein processing within the secretory pathway.
Endoproteolytic cleavage of hormone and neuropeptide precursors, as well as many complex proteins, such as coagulation factors and viral glycoproteins, is a key process in the generation of bioactive polypeptides. These cleavages typically occur at the dibasic amino acid residues Lys-Arg or Arg-Arg. The enzymes responsible for the processing belong to a newly discovered family of serine proteases related to the bacterial subtilisins. These include PACE (furin), PC1/PC3, PC2 and PACE4, which have all been characterized functionally and structurally.
Genetics Institute, Cambridge, Massachusetts.
A
A
Rehemtulla
R J
RJ
Kaufman
D000595:Amino Acid Sequence; D000818:Animals; D001709:Biotechnology; D045683:Furin; D006801:Humans; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D009490:Neurosecretory Systems / Q000378:metabolism; D043484:Proprotein Convertases; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases / Q000378:metabolism; D013381:Subtilisins / Q000378:metabolism
D008565:Membrane Proteins; D011506:Proteins; D029701:Saccharomyces cerevisiae Proteins; D043484:Proprotein Convertases; D012697:Serine Endopeptidases; D013381:Subtilisins; C058751:KEX2 protein, S cerevisiae; C468731:FURIN protein, human; D045683:Furin