ArticleInternational journal of molecular sciences2018
Imine Deaminase Activity and Conformational Stability of UK114, the Mammalian Member of the Rid Protein Family Active in Amino Acid Metabolism.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Site-directed mutagenesis reveals the interplay between stability, structure, and enzymatic activity in RidA from Capra hircus.Protein science : a publication of the Protein Society · 2024Article
- Tetrahydrofolate levels influence 2-aminoacrylate stress inJournal of bacteriology · 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
- Article
- Rid7C, a Member of the YjgF/YER057c/UK114 (Rid) Protein Family, Is a Novel Endoribonuclease That Regulates the Expression of a Specialist RNA Polymerase Involved in Differentiation in Nonomuraea gerenzanensis.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
- RidA Proteins Protect against Metabolic Damage by Reactive Intermediates.Microbiology and molecular biology reviews : MMBR · 2020Review
- 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
- Cj1388 Is a RidA Homolog and Is Required for Flagella Biosynthesis and/or Function inFrontiers in microbiology · 2019Article
- The Rid family member RutC of Escherichia coli is a 3-aminoacrylate deaminase.The Journal of biological chemistryArticle
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reactive intermediate deaminase (Rid) protein family is a recently discovered group of enzymes that is conserved in all domains of life and is proposed to play a role in the detoxification of reactive enamines/imines. UK114, the mammalian member of RidA subfamily, was identified in the early 90s as a component of perchloric acid-soluble extracts from goat liver and exhibited immunomodulatory properties. Multiple activities were attributed to this protein, but its function is still unclear. This work addressed the question of whether UK114 is a Rid enzyme. Biochemical analyses demonstrated that UK114 hydrolyzes α-imino acids generated by l- or d-amino acid oxidases with a preference for those deriving from Ala > Leu = l-Met > l-Gln, whereas it was poorly active on l-Phe and l-His. Circular Dichroism (CD) analyses of UK114 conformational stability highlighted its remarkable resistance to thermal unfolding, even at high urea concentrations. The half-life of heat inactivation at 95 °C, measured from CD and activity data, was about 3.5 h. The unusual conformational stability of UK114 could be relevant in the frame of a future evaluation of its immunogenic properties. In conclusion, mammalian UK114 proteins are RidA enzymes that may play an important role in metabolism homeostasis also in these organisms.
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