Crystal structures of the elusive Rhizobium etli L-asparaginase reveal a peculiar active site.
Asparaginase
/ chemistry
Bacterial Proteins
/ chemistry
Binding Sites
/ genetics
Biocatalysis
Catalytic Domain
Cations
/ chemistry
Crystallography, X-Ray
Enzyme Stability
Hydrogen-Ion Concentration
Kinetics
Metals
/ chemistry
Models, Molecular
Mutation
Protein Binding
Protein Folding
Protein Multimerization
Rhizobium etli
/ enzymology
Temperature
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
18 11 2021
18 11 2021
Historique:
received:
29
06
2021
accepted:
01
11
2021
entrez:
19
11
2021
pubmed:
20
11
2021
medline:
28
12
2021
Statut:
epublish
Résumé
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 asparaginase activity is relatively high, with K
Identifiants
pubmed: 34795296
doi: 10.1038/s41467-021-27105-x
pii: 10.1038/s41467-021-27105-x
pmc: PMC8602277
doi:
Substances chimiques
Bacterial Proteins
0
Cations
0
Metals
0
Asparaginase
EC 3.5.1.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
6717Informations de copyright
© 2021. The Author(s).
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