ArticleArchives of biochemistry and biophysics2011
Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli.
Article in Archives of biochemistry and biophysics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 53 citations in OpenAlex.
- The Substrate Versatility of ΔMolecules (Basel, Switzerland) · 2026Article
- The Proline Dehydrogenase GeneInternational journal of molecular sciences · 2025Article
- The new insight into the role of hydroxyproline in metabolism of cancer cells.Frontiers in cell and developmental biology · 2025Review
- Pangenome comparison ofbioRxiv : the preprint server for biology · 2023Article
- Proline Dehydrogenase and Pyrroline 5 Carboxylate Dehydrogenase fromPathogens (Basel, Switzerland) · 2023Article
- Enhancement of acid tolerance of Escherichia coli by introduction of molecule chaperone CbpA from extremophile.World journal of microbiology & biotechnology · 2023Article
- Computational insights on the hydride and proton transfer mechanisms of L-proline dehydrogenase.PloS one · 2023Article
- Structure-affinity relationships of reversible proline analog inhibitors targeting proline dehydrogenase.Organic & biomolecular chemistry · 2022Article
- The Roles of Coenzyme Q in Disease: Direct and Indirect Involvement in Cellular Functions.International journal of molecular sciences · 2021Review
- Evidence for Proline Catabolic Enzymes in the Metabolism of Thiazolidine Carboxylates.Biochemistry · 2021Article
- Photoinduced Covalent Irreversible Inactivation of Proline Dehydrogenase by S-Heterocycles.ACS chemical biology · 2021Article
- Metabolic Targets of Coenzyme Q10 in Mitochondria.Antioxidants (Basel, Switzerland) · 2021Review
- Protein expression in the obligate hydrocarbon-degrading psychrophile Oleispira antarctica RB-8 during alkane degradation and cold tolerance.Environmental microbiology · 2020Article
- Role of Proline in Pathogen and Host Interactions.Antioxidants & redox signaling · 2019Review
- Structural Biology of Proline Catabolic Enzymes.Antioxidants & redox signaling · 2019Review
- The Proline Cycle As a Potential Cancer Therapy Target.Biochemistry · 2018Article
- Structural Basis for the Substrate Inhibition of Proline Utilization A by Proline.Molecules (Basel, Switzerland) · 2017Article
- Article
- Structure, function, and mechanism of proline utilization A (PutA).Archives of biochemistry and biophysics · 2017Review
- Identification of a Conserved Histidine As Being Critical for the Catalytic Mechanism and Functional Switching of the Multifunctional Proline Utilization A Protein.Biochemistry · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The multifunctional proline utilization A (PutA) flavoenzyme from Escherichia coli performs the oxidation of proline to glutamate in two catalytic steps using separate proline dehydrogenase (PRODH) and Δ(1)-pyrroline-5-carboxylate (P5C) dehydrogenase domains. In the first reaction, the oxidation of proline is coupled to the reduction of ubiquinone (CoQ) by the PRODH domain, which has a β(8)α(8)-barrel structure that is conserved in bacterial and eukaryotic PRODH enzymes. The structural requirements of the benzoquinone moiety were examined by steady-state kinetics using CoQ analogs. PutA displayed activity with all the analogs tested; the highest k(cat)/K(m) was obtained with CoQ(2). The kinetic mechanism of the PRODH reaction was investigated use a variety of steady-state approaches. Initial velocity patterns measured using proline and CoQ(1), combined with dead-end and product inhibition studies, suggested a two-site ping-pong mechanism for PutA. The kinetic parameters for PutA were not strongly influenced by solvent viscosity suggesting that diffusive steps do not significantly limit the overall reaction rate. In summary, the kinetic data reported here, along with analysis of the crystal structure data for the PRODH domain, suggest that the proline:ubiquinone oxidoreductase reaction of PutA occurs via a rapid equilibrium ping-pong mechanism with proline and ubiquinone binding at two distinct sites.
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.