ArticleThe Journal of biological chemistry
The Rid family member RutC of Escherichia coli is a 3-aminoacrylate deaminase.
Article in The Journal of biological chemistry. 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, 7 citations in OpenAlex.
- Biochemical and structural characterization of a reactive intermediate deaminase A homolog from Streptococcus sanguinis.Scientific reports · 2025Article
- Functional characterization of theApplied and environmental microbiology · 2024Article
- RidA proteins contribute to fitness ofMicrobial cell (Graz, Austria) · 2024Article
- Modulators of a robust and efficient metabolism: Perspective and insights from the Rid superfamily of proteins.Advances in microbial physiology · 2023Review
- DadY (PA5303) is required for fitness ofMicrobial cell (Graz, Austria) · 2022Article
- Serendipity Reveals the Function and Physiological Role of a Large Family of Proteins.Journal of bacteriology · 2022Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The Rid protein family (PF14588, IPR006175) is divided into nine subfamilies, of which only the RidA subfamily has been characterized biochemically. RutC, the founding member of one subfamily, is encoded in the pyrimidine utilization (rut) operon that encodes a pathway that allows Escherichia coli to use uracil as a sole nitrogen source. Results reported herein demonstrate that RutC has 3-aminoacrylate deaminase activity and facilitates one of the reactions previously presumed to occur spontaneously in vivo. RutC was active with several enamine-imine substrates, showing similarities and differences in substrate specificity with the canonical member of the Rid superfamily, Salmonella enterica RidA. Under standard laboratory conditions, a Rut pathway lacking RutC generates sufficient nitrogen from uracil for growth of E. coli. These results support a revised model of the Rut pathway and provide evidence that Rid proteins may modulate metabolic fitness, rather than catalyzing essential functions.
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Registered trials
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