ArticleThe Journal of biological chemistry2010
Substrate specificity of human carboxypeptidase A6.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.
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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
22 citing papers in PubMed, 1 synthesis or guideline pooled it, 40 citations in OpenAlex.
- Limitations of Mass Spectrometry-Based Peptidomic Approaches.Journal of the American Society for Mass Spectrometry · 2015Pooled it
- Origins, Technological Advancement, and Applications of Peptidomics.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Quantitative Peptidomics: General Considerations.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Acquisition of new function through gene duplication in the metallocarboxypeptidase family.Scientific reports · 2023Article
- Enhanced Production of ECM Proteins for Pharmaceutical Applications Using Mammalian Cells and Sodium Heparin Supplementation.Pharmaceutics · 2022Article
- Proteolytic Cleavage of Bioactive Peptides and Protease-Activated Receptors in Acute and Post-Colitis.International journal of molecular sciences · 2021Article
- Substrate Specificity and Structural Modeling of Human Carboxypeptidase Z: A Unique Protease with a Frizzled-Like Domain.International journal of molecular sciences · 2020Article
- Mast cell peptidases (carboxypeptidase A and chymase)-mediated hydrolysis of human angiotensin-(1-12) substrate.Biochemical and biophysical research communications · 2019Article
- Carboxypeptidase A6 Promotes the Proliferation and Migration of Hepatocellular Carcinoma by Up-regulating AKT Signaling Pathway.Current medical science · 2019Article
- The carboxy-terminus, a key regulator of protein function.Critical reviews in biochemistry and molecular biology · 2019Review
- A Caenorhabditis elegans Mass Spectrometric Resource for Neuropeptidomics.Journal of the American Society for Mass Spectrometry · 2018Article
- 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
- A Group of Weakly Bound to Neurons Extracellular Metallopeptidases (NEMPs).Neurochemical research · 2016Article
- Article
- Novel carboxypeptidase A6 (CPA6) mutations identified in patients with juvenile myoclonic and generalized epilepsy.PloS one · 2015Article
- Carboxypeptidases in disease: insights from peptidomic studies.Proteomics. Clinical applications · 2014Review
- 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
- Naturally occurring carboxypeptidase A6 mutations: effect on enzyme function and association with epilepsy.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Carboxypeptidase A6 (CPA6) is an extracellular matrix-bound metallocarboxypeptidase (CP) that has been implicated in Duane syndrome, a neurodevelopmental disorder in which the lateral rectus extraocular muscle is not properly innervated. Consistent with a role in Duane syndrome, CPA6 is expressed in a number of chondrocytic and nervous tissues during embryogenesis. To better characterize the enzymatic function and specificity of CPA6 and to compare this with other CPs, CPA6 was expressed in HEK293 cells and purified. Kinetic parameters were determined using a panel of synthetic carboxypeptidase substrates, indicating a preference of CPA6 for large hydrophobic C-terminal amino acids and only very weak activity toward small amino acids and histidine. A quantitative peptidomics approach using a mixture of peptides representative of the neuropeptidome allowed the characterization of CPA6 preferences at the P1 substrate position and suggested that small and acidic P1 residues significantly inhibit CPA6 cleavage. Finally, a comparison of available kinetic data for CPA enzymes shows a gradient of specificity across the subfamily, from the very restricted specificity of CPA2 to the very broad activity of CPA4. Structural data and modeling for all CPA/B subfamily members suggests the structural basis for the unique specificities observed for each member of the CPA/B subfamily of metallocarboxypeptidases.
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Registered trials
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.