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Article

Crystal structures of the elusive Rhizobium etli L-asparaginase reveal a peculiar active site.

Nature communications - 18 Nov 2021

Loch Joanna I, Imiolczyk Barbara, Sliwiak Joanna, Wantuch Anna, Bejger Magdalena, Gilski Miroslaw, Jaskolski Mariusz

Abstract excerpt

Rhizobium etli, a nitrogen-fixing bacterial symbiont of legume plants, encodes an essential L-asparaginase (ReAV) with no sequence homology to known enzymes with this activity. High-resolution crystal structures of ReAV show indeed a structurally distinct, dimeric enzyme, with some resemblance to glutaminases and β-lactamases. However, ReAV has no glutaminase or lactamase activity, and at pH 9 its allosteric...

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PMID: 34795296
DOI: 10.1038/s41467-021-27105-x
PMCID: PMC8602277

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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