ReviewAmino acids2008
Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli.
Review in Amino acids, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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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.
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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.
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Who cites it
27 citing papers in PubMed, 36 citations in OpenAlex.
- Proline dehydrogenase, a rate-limiting catabolic enzyme, affecting the growth and pathogenicity of Toxoplasma gondii tachyzoites by regulating the proline metabolism and mitochondrial function of the parasite.Parasites & vectors · 2025Article
- Inhibition of a nutritional endosymbiont by glyphosate abolishes mutualistic benefit on cuticle synthesis in Oryzaephilus surinamensis.Communications biology · 2021Article
- The diverse functionality of NQO1 and its roles in redox control.Redox biology · 2021Review
- Structural Biology of Proline Catabolic Enzymes.Antioxidants & redox signaling · 2019Review
- Role of Proline in Pathogen and Host Interactions.Antioxidants & redox signaling · 2019Review
- Selective labeling and unlabeling strategies in protein solid-state NMR spectroscopy.Journal of biomolecular NMR · 2018Review
- PutA Is Required for Virulence and Regulated by PruR inFrontiers in microbiology · 2018Article
- Article
- Structure, function, and mechanism of proline utilization A (PutA).Archives of biochemistry and biophysics · 2017Review
- Transcriptome and proteome dynamics in chemostat culture reveal how Campylobacter jejuni modulates metabolism, stress responses and virulence factors upon changes in oxygen availability.Environmental microbiology · 2017Article
- Identification of a Conserved Histidine As Being Critical for the Catalytic Mechanism and Functional Switching of the Multifunctional Proline Utilization A Protein.Biochemistry · 2017Article
- A novel bifunctional transcriptional regulator of riboflavin metabolism in Archaea.Nucleic acids research · 2017Article
- A Novel Transcriptional Regulator Related to Thiamine Phosphate Synthase Controls Thiamine Metabolism Genes in Archaea.Journal of bacteriology · 2017Article
- Metabolic network capacity of Escherichia coli for Krebs cycle-dependent proline hydroxylation.Microbial cell factories · 2015Article
- Proline metabolism increases katG expression and oxidative stress resistance in Escherichia coli.Journal of bacteriology · 2015Article
- Article
- Evidence for hysteretic substrate channeling in the proline dehydrogenase and Δ1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA).The Journal of biological chemistry · 2014Article
- Article
- Proline utilization by Bacillus subtilis: uptake and catabolism.Journal of bacteriology · 2012Article
- Small-angle X-ray scattering studies of the oligomeric state and quaternary structure of the trifunctional proline utilization A (PutA) flavoprotein from Escherichia coli.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The control of gene expression by enzymes provides a direct pathway for cells to respond to fluctuations in metabolites and nutrients. One example is the proline utilization A (PutA) protein from Escherichia coli. PutA is a membrane-associated enzyme that catalyzes the oxidation of L: -proline to glutamate using a flavin containing proline dehydrogenase domain and a NAD(+) dependent Delta(1)-pyrroline-5-carboxylate dehydrogenase domain. In some Gram-negative bacteria such as E. coli, PutA is also endowed with a ribbon-helix-helix DNA-binding domain and acts as a transcriptional repressor of the proline utilization genes. PutA switches between transcriptional repressor and enzymatic functions in response to proline availability. Molecular insights into the redox-based mechanism of PutA functional switching from recent studies are reviewed. In addition, new results from cell-based transcription assays are presented which correlate PutA membrane localization with put gene expression levels. General membrane localization of PutA, however, is not sufficient to activate the put genes.
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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.