ArticleProceedings of the National Academy of Sciences of the United States of America2018
Crystal structure and mechanism of human carboxypeptidase O: Insights into its specific activity for acidic residues.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- Non-Pancreatic Digestive Enzymes.Biomolecules · 2025Review
- A Novel Non-Destructive Rapid Tool for Estimating Amino Acid Composition and Secondary Structures of Proteins in Solution.Small methods · 2024Article
- Acquisition of new function through gene duplication in the metallocarboxypeptidase family.Scientific reports · 2023Article
- Isolation and Characterization of NpCI, a New Metallocarboxypeptidase Inhibitor from the Marine SnailMarine drugs · 2023Article
- Alterations in Gene Pair Correlations as Potential Diagnostic Markers for Colon Cancer.International journal of molecular sciences · 2022Article
- Enhanced Production of ECM Proteins for Pharmaceutical Applications Using Mammalian Cells and Sodium Heparin Supplementation.Pharmaceutics · 2022Article
- Structure ofLife science alliance · 2022Article
- Biochemical and genetic analysis of Ecm14, a conserved fungal pseudopeptidase.BMC molecular and cell biology · 2020Article
- Substrate Specificity and Structural Modeling of Human Carboxypeptidase Z: A Unique Protease with a Frizzled-Like Domain.International journal of molecular sciences · 2020Article
- Carboxypeptidase O is a lipid droplet-associated enzyme able to cleave both acidic and polar C-terminal amino acids.PloS one · 2018Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human metallocarboxypeptidase O (hCPO) is a recently discovered digestive enzyme localized to the apical membrane of intestinal epithelial cells. Unlike pancreatic metallocarboxypeptidases, hCPO is glycosylated and produced as an active enzyme with distinctive substrate specificity toward C-terminal (C-t) acidic residues. Here we present the crystal structure of hCPO at 1.85-Å resolution, both alone and in complex with a carboxypeptidase inhibitor (NvCI) from the marine snail
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