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Details on Person Preferential cleavage of des-31,32-proinsulin over intact proinsulin by the insulin secretory granule type II endopeptidase. Implication of a favored route for prohormone processing

Class:Id	LiteratureReference:9023150
_displayName	Preferential cleavage of des-31,32-proinsulin over intact proinsulin by the insulin secretory granule type II endopeptidase. Implication of a favored route for prohormone processing
_timestamp	2017-09-27 10:24:22
author	[Person:9023151] Rhodes, C J [Person:9023177] Lincoln, B [Person:8933613] Shoelson, S E
created	[InstanceEdit:9023176] May, Bruce, 2017-09-27
journal	J. Biol. Chem.
pages	22719-27
pubMedIdentifier	1429623
title	Preferential cleavage of des-31,32-proinsulin over intact proinsulin by the insulin secretory granule type II endopeptidase. Implication of a favored route for prohormone processing
volume	267
year	1992
(literatureReference)	[Reaction:9023165] Pcsk1 (rat) cleaves human proinsulin to yield Insulin(25-56) and Insulin(57-110) [Homo sapiens] [Reaction:9023180] Pcsk2 (rat) cleaves human Insulin(57-110) to yield Insulin(90-110) and C-peptide (Insulin(57-89)) [Homo sapiens] [CatalystActivityReference:9643548] serine-type endopeptidase activity of Pcsk2 [secretory granule lumen] Preferential cleavage of des-31,32-proinsulin over intact proinsulin by the insulin secretory granule type II endopeptidase. Implication of a favored route for prohormone processing [CatalystActivityReference:9643757] serine-type endopeptidase activity of Pcsk1:Ca2+ [secretory granule lumen] Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic beta cell via two distinct site-specific endopeptidases
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No pathways have been reviewed or authored by Preferential cleavage of des-31,32-proinsulin over intact proinsulin by the insulin secretory granule type II endopeptidase. Implication of a favored route for prohormone processing (9023150)