Ontology highlight
ABSTRACT:
SUBMITTER: Szmola R
PROVIDER: S-EPMC3023477 | biostudies-literature | 2011 Jan
REPOSITORIES: biostudies-literature
Szmola Richárd R Bence Melinda M Carpentieri Andrea A Szabó András A Costello Catherine E CE Samuelson John J Sahin-Tóth Miklós M
The Journal of biological chemistry 20101122 3
Human digestive carboxypeptidases CPA1, CPA2, and CPB1 are secreted by the pancreas as inactive proenzymes containing a 94-96-amino acid-long propeptide. Activation of procarboxypeptidases is initiated by proteolytic cleavage at the C-terminal end of the propeptide by trypsin. Here, we demonstrate that subsequent cleavage of the propeptide by chymotrypsin C (CTRC) induces a nearly 10-fold increase in the activity of trypsin-activated CPA1 and CPA2, whereas CPB1 activity is unaffected. Other huma ...[more]