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...
Topics
- Asparaginase
- Bacterial Proteins
- Binding Sites
- Biocatalysis
- Catalytic Domain
- Cations
- Crystallography, X-Ray
- Enzyme Stability
- Hydrogen-Ion Concentration
- Kinetics
- Metals
- Models, Molecular
- Mutation
- Protein Binding