Abstract
The major endoproteolytic processing enzymes of the secretory pathway are the subtilisin-like proprotein convertases (SPCs). Furin (SPC1) has emerged as one of the major processing enzymes of the constitutive secretory pathway and its localization in the trans-Golgi network and mechanism of autoactivation have been studied in considerable detail. Recent gene disruption experiments and the study of naturally-occurring mutations underscore the importance of PC2 (prohormones convertase 2, or SPC2) and PC1/PC3 (prohormone convertase 1 3 , or SPC3) in the processing of a wide variety of hormone and neuropeptide precursors. The role of Carboxypeptidase E (CPE) in the removal of carboxy-terminal basic residues exposed by the endoproteases was shown to be necessary for efficient endoproteolytic processing of proinsulin and several other protein precursors. Many biologically active peptides are also amidated after their proteolytic processing by peptidylglycine α-amidating monooxygenase (PAM) and recent X-ray studies of the peptidyl α-hydroxylating monooxygenase component of PAM have shed new light on the role of copper in the mechanism of this reaction.
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