Protein processing within the secretory pathway.

A Rehemtulla; R J Kaufman

doi:10.1016/0958-1669(92)90086-x

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PubMed · 1368940

Protein processing within the secretory pathway.

A Rehemtulla·R J Kaufman

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Abstract

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.

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Amino Acid Sequence Animals Biotechnology Furin Humans Membrane Proteins Molecular Sequence Data Neurosecretory Systems Proprotein Convertases Protein Processing, Post-Translational Proteins Saccharomyces cerevisiae Proteins Serine Endopeptidases Subtilisins Journal Article Review

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A Rehemtulla, R J Kaufman. 1992. Protein processing within the secretory pathway.. https://doi.org/10.1016/0958-1669(92)90086-x

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