PCSK1 hydrolyzes Proglucagon to Glucagon-like Peptide-1

Stable Identifier
R-HSA-381798
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
secretory granule lumen
ReviewStatus
5/5
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PCSK1 hydrolyzes Proglucagon to Glucagon-like Peptide-1
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In secretory granules of intestinal L cells, proglucagon is proteolytically cleaved by prohormone convertase 1 (PC1) at two sites to yield GLP-1 (7-36) or GLP-1 (7-37). In humans almost all circulating GLP-1 is GLP-1 (7-36) amidated at the C-terminus. Experiments in knockout mice have shown that PC1 is necessary for cleavage. Carboxypeptidase E and peptidylglycine alpha-amidating monooxygenase may be involved in trimming and amidating the C-terminus.
Literature References
PubMed ID Title Journal Year
12651102 Expression, purification, and PC1-mediated processing of human proglucagon, glicentin, and major proglucagon fragment

Bonic, A, Mackin, RB

Protein Expr Purif 2003
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Input
Output
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as an event of
Catalyst Activity

serine-type endopeptidase activity of PC1:calcium cofactor [secretory granule lumen]

Physical Entity
PC1:calcium cofactor [secretory granule lumen] (Homo sapiens)
Activity
serine-type endopeptidase activity (GO:0004252)
Inferred From
Pcsk1 hydrolyzes Proglucagon to Glucagon-like Peptide-1 (7-36) (Mus musculus)
Pcsk1 hydrolyzes Proglucagon to Glucagon-like Peptide-1 (7-37) (Mus musculus)
Authored
May, B  (2009-05-19)
Reviewed
Bloom, SR  (2010-06-25)
Created
May, B  (2008-11-20)
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