ArticleMolecular & cellular proteomics : MCP2013
Proteome-derived peptide libraries to study the substrate specificity profiles of carboxypeptidases.
Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 50 citations in OpenAlex.
- Enzyme-free biochemical production of seamlessly N-to-C cyclized peptides from natural or recombinant proteins.bioRxiv : the preprint server for biology · 2025Article
- Targeting carboxypeptidase A/B activity with the phosphinic inhibitor C28 reduces the asthmatic response in a mouse model of house dust mite-induced asthma.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2025Article
- Enzyme-free biochemical production of seamlessly N-to-C cyclized peptides from natural or recombinant proteins.Methods in enzymology · 2025Article
- In-Depth Specificity Profiling of Endopeptidases Using Dedicated Mix-and-Split Synthetic Peptide Libraries and Mass Spectrometry.Analytical chemistry · 2023Article
- Interneuron odyssey: molecular mechanisms of tangential migration.Frontiers in neural circuits · 2023Review
- Review
- Dynamically upregulated mast cell CPA3 patterns in chronic obstructive pulmonary disease and idiopathic pulmonary fibrosis.Frontiers in immunology · 2022Article
- Article
- Overexpression of carboxypeptidase X M14 family member 2 predicts an unfavorable prognosis and promotes proliferation and migration of osteosarcoma.Diagnostic pathology · 2019Article
- Quantitative Multiplex Substrate Profiling of Peptidases by Mass Spectrometry.Molecular & cellular proteomics : MCP · 2019Article
- 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
- Article
- Prolylcarboxypeptidase deficiency is associated with increased blood pressure, glomerular lesions, and cardiac dysfunction independent of altered circulating and cardiac angiotensin II.Journal of molecular medicine (Berlin, Germany) · 2017Article
- Emerging challenges in the design of selective substrates, inhibitors and activity-based probes for indistinguishable proteases.The FEBS journal · 2017Review
- Substrate specificity of human metallocarboxypeptidase D: Comparison of the two active carboxypeptidase domains.PloS one · 2017Article
- Determinants of Macromolecular Specificity from Proteomics-Derived Peptide Substrate Data.Current protein & peptide science · 2017Review
- Identification of Protease Specificity by Combining Proteome-Derived Peptide Libraries and Quantitative Proteomics.Molecular & cellular proteomics : MCP · 2016Article
- Novel carboxypeptidase A6 (CPA6) mutations identified in patients with juvenile myoclonic and generalized epilepsy.PloS one · 2015Article
- C-terminomics screen for natural substrates of cytosolic carboxypeptidase 1 reveals processing of acidic protein C termini.Molecular & cellular proteomics : MCP · 2015Article
- PRIME-XS, a European infrastructure for proteomics.Molecular & cellular proteomics : MCP · 2014Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Through processing peptide and protein C termini, carboxypeptidases participate in the regulation of various biological processes. Few tools are however available to study the substrate specificity profiles of these enzymes. We developed a proteome-derived peptide library approach to study the substrate preferences of carboxypeptidases. Our COFRADIC-based approach takes advantage of the distinct chromatographic behavior of intact peptides and the proteolytic products generated by the action of carboxypeptidases, to enrich the latter and facilitate its MS-based identification. Two different peptide libraries, generated either by chymotrypsin or by metalloendopeptidase Lys-N, were used to determine the substrate preferences of human metallocarboxypeptidases A1 (hCPA1), A2 (hCPA2), and A4 (hCPA4). In addition, our approach allowed us to delineate the substrate specificity profile of mouse mast cell carboxypeptidase (MC-CPA or mCPA3), a carboxypeptidase suggested to function in innate immune responses regulation and mast cell granule homeostasis, but which thus far lacked a detailed analysis of its substrate preferences. mCPA3 was here shown to preferentially remove bulky aromatic amino acids, similar to hCPA2. This was also shown by a hierarchical cluster analysis, grouping hCPA1 close to hCPA4 in terms of its P1 primed substrate specificity, whereas hCPA2 and mCPA3 cluster separately. The specificity profile of mCPA3 may further aid to elucidate the function of this mast cell carboxypeptidase and its biological substrate repertoire. Finally, we used this approach to evaluate the substrate preferences of prolylcarboxypeptidase, a serine carboxypeptidase shown to cleave C-terminal amino acids linked to proline and alanine.
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