ArticleScientific reports2019
Opportunistic complexes of E. coli L-asparaginases with citrate anions.
Article in Scientific reports, 2019. 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, 13 citations in OpenAlex.
- L-asparaginase is a PAR2 N-terminal protease that unmasks the PAR2 tethered ligand.Cell death discovery · 2025Article
- Towards a dependable data set of structures for L-asparaginase research.Acta crystallographica. Section D, Structural biology · 2024Article
- The E. coli L-asparaginase V27T mutant: structural and functional characterization and comparison with theoretical predictions.FEBS letters · 2022Article
- Structural and biophysical aspects of l-asparaginases: a growing family with amazing diversity.IUCrJ · 2021Review
- Generalized enzymatic mechanism of catalysis by tetrameric L-asparaginases from mesophilic bacteria.Scientific reports · 2020Article
- A shared vision for macromolecular crystallography over the next five years.Structural dynamics (Melville, N.Y.) · 2019Article
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Authors and funding
3 authors at 2 institutions in 1 country.
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Abstract
Active sites of enzymes are highly optimized for interactions with specific substrates, thus binding of opportunistic ligands is usually observed only in the absence of native substrates or products. However, during growth of crystals required for structure determination enzymes are often exposed to conditions significantly divergent from the native ones, leading to binding of unexpected ligands to active sites even in the presence of substrates. Failing to recognize this possibility may lead to incorrect interpretation of experimental results and to faulty conclusions. Here, we present several examples of binding of a citrate anion to the active sites of E. coli L-asparaginases I and II, even in the presence of the native substrate, L-Asn. A part of this report focuses on a comprehensive re-interpretation of structural results published previously for complexes of type I L-asparaginase (EcAI) from E. coli. In two re-refined structures a citrate anion forms an acyl-enzyme reaction intermediate with the catalytic threonine. These results emphasize the importance of careful and critical analysis during interpretation of crystallographic data.
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