ArticlePloS one2017
Members of the Rid protein family have broad imine deaminase activity and can accelerate the Pseudomonas aeruginosa D-arginine dehydrogenase (DauA) reaction in vitro.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 25 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
- Evidence for a Negative Correlation between Human Reactive Enamine-Imine Intermediate Deaminase A (RIDA) Activity and Cell Proliferation Rate: Role of Lysine Succinylation of RIDA.International journal of molecular sciences · 2021Article
- Rid Enhances the 6-Hydroxypseudooxynicotine Dehydrogenase Reaction in Nicotine Degradation by Agrobacterium tumefaciens S33.Applied and environmental microbiology · 2021Article
- RidA Proteins Protect against Metabolic Damage by Reactive Intermediates.Microbiology and molecular biology reviews : MMBR · 2020Review
- Two novel fish paralogs provide insights into the Rid family of imine deaminases active in pre-empting enamine/imine metabolic damage.Scientific reports · 2020Article
- Integrated Metabolomics and Transcriptomics Suggest the Global Metabolic Response to 2-Aminoacrylate Stress inMetabolites · 2019Article
- Reactive Enamines and Imines In Vivo: Lessons from the RidA Paradigm.Trends in biochemical sciences · 2019Review
- A Unique Homo-Hexameric Structure of 2-Aminomuconate Deaminase in the BacteriumFrontiers in microbiology · 2019Article
- Cj1388 Is a RidA Homolog and Is Required for Flagella Biosynthesis and/or Function inFrontiers in microbiology · 2019Article
- Analyses of variants of the Ser/Thr dehydratase IlvA provide insight into 2-aminoacrylate metabolism inThe Journal of biological chemistry · 2018Article
- PA5339, a RidA Homolog, Is Required for Full Growth in Pseudomonas aeruginosa.Journal of bacteriology · 2018Article
- Expression of Pyridoxal 5'-Phosphate-Independent Racemases Can Reduce 2-Aminoacrylate Stress in Salmonella enterica.Journal of bacteriology · 2018Article
- Imine Deaminase Activity and Conformational Stability of UK114, the Mammalian Member of the Rid Protein Family Active in Amino Acid Metabolism.International journal of molecular sciences · 2018Article
- The Rid family member RutC of Escherichia coli is a 3-aminoacrylate deaminase.The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Rid (YjgF/YER057c/UK114) protein family is a group of small, sequence diverse proteins that consists of eight subfamilies. The archetypal RidA subfamily is found in all domains, while the Rid1-7 subfamilies are present only in prokaryotes. Bacterial genomes often encode multiple members of the Rid superfamily. The best characterized member of this protein family, RidA from Salmonella enterica, is a deaminase that quenches the reactive metabolite 2-aminoacrylate generated by pyridoxal 5'-phosphate-dependent enzymes and ultimately spares certain enzymes from damage. The accumulation of 2-aminoacrylate can damage enzymes and lead to growth defects in bacteria, plants, and yeast. While all subfamily members have been annotated as imine deaminases based on the RidA characterization, experimental evidence to support this annotation exists for a single protein outside the RidA subfamily. Here we report that six proteins, spanning Rid subfamilies 1-3, deaminate a variety of imine/enamine substrates with differing specific activities. Proteins from the Rid2 and Rid3 subfamilies, but not from the RidA and Rid1 subfamilies deaminated iminoarginine, generated in situ by the Pseudomonas aeruginosa D-arginine dehydrogenase DauA. These data biochemically distinguished the subfamilies and showed Rid proteins have activity on a metabolite that is physiologically relevant in Pseudomonas and other bacteria.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.