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carboxypeptidase C

Known as: Acid Carboxypeptidase, BGPP, Serine Carboxypeptidase I 
A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by… 
National Institutes of Health

Related topics

Related topics

11 relations
CTSA geneIn BloodProcess of secretionantagonists & inhibitors

Narrower (2)

CTSA protein, humancpy1 protein, S pombe

Broader (1)

Carboxypeptidase

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2013
Highly Cited
2013
Graphene oxide-peptide nanocomplex as a versatile fluorescence probe of protein kinase activity based on phosphorylation protection against carboxypeptidase digestion.
The research on complicated kinomics and kinase-target drug discovery requires the development of simple, cost-effective, and… 
1999
1999
A Cell-Free Assay Allows Reconstitution of Vps33p-Dependent Transport to the Yeast Vacuole/Lysosome
We report a cell-free system that measures transport-coupled maturation of carboxypeptidase Y (CPY). Yeast spheroplasts are lysed… 
Highly Cited
1995
Highly Cited
1995
C-terminal ladder sequencing via matrix-assisted laser desorption mass spectrometry coupled with carboxypeptidase Y time-dependent and concentration-dependent digestions.
The utility of matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry for the analysis of C… 
Highly Cited
1994
Highly Cited
1994
Fructan as a New Carbohydrate Sink in Transgenic Potato Plants.
Fructans are polyfructose molecules that function as nonstructural storage carbohydrates in several plant species that are… 
Review
1992
Review
1992
Biogenesis of the vacuole in Saccharomyces cerevisiae.
1990
1990
The functional efficiency of a mammalian signal peptide is directly related to its hydrophobicity.
Highly Cited
1983
Highly Cited
1983
Complete amino acid sequence of boar protamine
Highly Cited
1979
Highly Cited
1979
Enzymatic peptide synthesis. Carboxypeptidase Y catalyzed formation of peptide bonds
It is demonstrated that carboxypeptidase Y from Saccharomyces cerevisiae can catalyze the formation of peptide bonds using N… 
1977
1977
Demonstration of a pyroglutamyl residue at the N terminus of the B-chain of porcine relaxin.
Highly Cited
1972
Highly Cited
1972
[10] Enzymatic hydrolysis with carboxypeptidases.
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