ArticleThe Journal of biological chemistry2011
Carboxypeptidase O is a glycosylphosphatidylinositol-anchored intestinal peptidase with acidic amino acid specificity.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 39 citations in OpenAlex.
- Amino Acid Digestibility of Extruded Chickpea and Yellow Pea Protein is High and Comparable in Moderately Stunted South Indian Children with Use of a Dual Stable Isotope Tracer Method.The Journal of nutrition · 2020Trial
- Understanding the Genetic Landscape of Gestational Diabetes: Insights into the Causes and Consequences of Elevated Glucose Levels in Pregnancy.Metabolites · 2024Review
- Trophic Position of the White Worm (International journal of molecular sciences · 2024Article
- Acquisition of new function through gene duplication in the metallocarboxypeptidase family.Scientific reports · 2023Article
- Crystal structure and mechanism of human carboxypeptidase O: Insights into its specific activity for acidic residues.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Carboxypeptidase O is a lipid droplet-associated enzyme able to cleave both acidic and polar C-terminal amino acids.PloS one · 2018Article
- Potential contribution of the neurodegenerative disorders risk loci to cognitive performance in an elderly male gout population.Medicine · 2017Article
- Substrate specificity of human metallocarboxypeptidase D: Comparison of the two active carboxypeptidase domains.PloS one · 2017Article
- The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids.Molecular biology of the cell · 2014Article
- Carboxypeptidases in disease: insights from peptidomic studies.Proteomics. Clinical applications · 2014Review
- Cytosolic carboxypeptidase 5 removes α- and γ-linked glutamates from tubulin.The Journal of biological chemistry · 2013Article
- Proteome-derived peptide libraries to study the substrate specificity profiles of carboxypeptidases.Molecular & cellular proteomics : MCP · 2013Article
- Quantitative peptidomics of Purkinje cell degeneration mice.PloS one · 2013Article
- A structural and functional analysis of Nna1 in Purkinje cell degeneration (pcd) mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
- Cytosolic carboxypeptidase 1 is involved in processing α- and β-tubulin.The Journal of biological chemistry · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The first metallocarboxypeptidase (CP) was identified in pancreatic extracts more than 80 years ago and named carboxypeptidase A (CPA; now known as CPA1). Since that time, seven additional mammalian members of the CPA subfamily have been described, all of which are initially produced as proenzymes, are activated by endoproteases, and remove either C-terminal hydrophobic or basic amino acids from peptides. Here we describe the enzymatic and structural properties of carboxypeptidase O (CPO), a previously uncharacterized and unique member of the CPA subfamily. Whereas all other members of the CPA subfamily contain an N-terminal prodomain necessary for folding, bioinformatics and expression of both human and zebrafish CPO orthologs revealed that CPO does not require a prodomain. CPO was purified by affinity chromatography, and the purified enzyme was able to cleave proteins and synthetic peptides with greatest activity toward acidic C-terminal amino acids unlike other CPA-like enzymes. CPO displayed a neutral pH optimum and was inhibited by common metallocarboxypeptidase inhibitors as well as citrate. CPO was modified by attachment of a glycosylphosphatidylinositol membrane anchor to the C terminus of the protein. Immunocytochemistry of Madin-Darby canine kidney cells stably expressing CPO showed localization to vesicular membranes in subconfluent cells and to the plasma membrane in differentiated cells. CPO is highly expressed in intestinal epithelial cells in both zebrafish and human. These results suggest that CPO cleaves acidic amino acids from dietary proteins and peptides, thus complementing the actions of well known digestive carboxypeptidases CPA and CPB.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.