ArticleProtein science : a publication of the Protein Society2024
Characterizing lysine acetylation of glucokinase.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 5 citations in OpenAlex.
- Crystal structures of Escherichia coli glucokinase acetylation-mimicking variants and insights into the impact of acetylation.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Article
- Crystal structures of Escherichia coli glucokinase and insights into phosphate binding.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Functional consequences of lysine acetylation of phosphofructokinase isozymes.The FEBS journal · 2025Article
- Lysine Phoshoglycerylation Is Widespread in Bacteria and Overlaps with Acylation.Microorganisms · 2024Article
- Characterizing lysine acetylation of glucokinase.Protein science : a publication of the Protein Society · 2024Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Glucokinase (GK) catalyzes the phosphorylation of glucose to form glucose-6-phosphate as the substrate of glycolysis for energy production. Acetylation of lysine residues in Escherichia coli GK has been identified at multiple sites by a series of proteomic studies, but the impact of acetylation on GK functions remains largely unknown. In this study, we applied the genetic code expansion strategy to produce site-specifically acetylated GK variants which naturally exist in cells. Enzyme assays and kinetic analyses showed that lysine acetylation decreases the GK activity, mostly resulting from acetylation of K214 and K216 at the entrance of the active site, which impairs the binding of substrates. We also compared results obtained from the glutamine substitution method and the genetic acetyllysine incorporation approach, showing that glutamine substitution is not always effective for mimicking acetylated lysine. Further genetic studies as well as in vitro acetylation and deacetylation assays were performed to determine acetylation and deacetylation mechanisms, which showed that E. coli GK could be acetylated by acetyl-phosphate without enzymes and deacetylated by CobB deacetylase.
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Registered trials
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