ArticleActa crystallographica. Section D, Biological crystallography2014
Lysine carboxylation: unveiling a spontaneous post-translational modification.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 29 citations in OpenAlex.
- BTG13-related metalloenzymes: Atypical non-heme iron-dependent dioxygenases with unusual coordination patterns and catalytic mechanisms.Engineering microbiology · 2025Review
- Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024Review
- Rational Design of the β-Bulge Gate in a Green Fluorescent Protein Accelerates the Kinetics of Sulfate Sensing.Angewandte Chemie (International ed. in English) · 2023Article
- Re-mining serum proteomics data reveals extensive post-translational modifications upon Zika and dengue infection.Molecular omics · 2023Article
- Carbon Dioxide and the Carbamate Post-Translational Modification.Frontiers in molecular biosciences · 2022Review
- Post-translational Modifications in Brain Diseases: A Future for Biomarkers.Advances in experimental medicine and biology · 2022Article
- A methodology for carbamate post-translational modification discovery and its application inInterface focus · 2021Article
- Article
- The identification of carbon dioxide mediated protein post-translational modifications.Nature communications · 2018Article
- Coping with inevitable accidents in metabolism.Microbial biotechnology · 2017Review
- Structural analysis of the bright monomeric yellow-green fluorescent protein mNeonGreen obtained by directed evolution.Acta crystallographica. Section D, Structural biology · 2016Article
- Maternal Low Quality Protein Diet Alters Plasma Amino Acid Concentrations of Weaning Rats.Nutrients · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The carboxylation of lysine residues is a post-translational modification (PTM) that plays a critical role in the catalytic mechanisms of several important enzymes. It occurs spontaneously under certain physicochemical conditions, but is difficult to detect experimentally. Its full impact is unknown. In this work, the signature microenvironment of lysine-carboxylation sites has been characterized. In addition, a computational method called Predictor of Lysine Carboxylation (PreLysCar) for the detection of lysine carboxylation in proteins with available three-dimensional structures has been developed. The likely prevalence of lysine carboxylation in the proteome was assessed through large-scale computations. The results suggest that about 1.3% of large proteins may contain a carboxylated lysine residue. This unexpected prevalence of lysine carboxylation implies an enrichment of reactions in which it may play functional roles. The results also suggest that by switching enzymes on and off under appropriate physicochemical conditions spontaneous PTMs may serve as an important and widely used efficient biological machinery for regulation.
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