ArticleScientific reports2023
E. coli allantoinase is activated by the downstream metabolic enzyme, glycerate kinase, and stabilizes the putative allantoin transporter by direct binding.
Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
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- A short peptide derived from late embryogenesis abundant proteins enhances acid tolerance in Escherichia coli via modulation of two-component regulatory systems.The FEBS journal · 2026Article
- A hidden reservoir of antibiotic resistance genes: transferable plasmids in community air and wastewater.Frontiers in microbiology · 2026Article
- Integrated genomic and transcriptomic Insights into methanol tolerance mechanisms in Methylobacterium extorquens AM1, identifying key targets for strain engineering.Journal of biological engineering · 2025Article
- Dual Regulation of theJournal of microbiology and biotechnology · 2025Article
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- Novel aspects of ethylene glycol catabolism.Applied microbiology and biotechnology · 2024Review
- A multi-scale expression and regulation knowledge base for Escherichia coli.Nucleic acids research · 2023Article
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Authors and funding
10 authors at 5 institutions in 4 countries.
Funding
Abstract
Allantoin is a good source of ammonium for many organisms, and in Escherichia coli it is utilized under anaerobic conditions. We provide evidence that allantoinase (AllB) is allosterically activated by direct binding of the allantoin catabolic enzyme, glycerate 2-kinase (GlxK) in the presence of glyoxylate. Glyoxylate is known to be an effector of the AllR repressor which regulates the allantoin utilization operons in E. coli. AllB has low affinity for allantoin, but its activation by GlxK leads to increased affinity for its substrate. We also show that the predicted allantoin transporter YbbW (re-named AllW) has allantoin specificity and the protein-protein interaction with AllB. Our results show that the AllB-dependent allantoin degradative pathway is subject to previously unrecognized regulatory mechanisms involving direct protein-protein interactions.
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