ArticleFrontiers in microbiology2015
On the Ancestral UDP-Glucose Pyrophosphorylase Activity of GalF from Escherichia coli.
Article in Frontiers in microbiology, 2015. 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.
- Identification of genetic determinants that promote biofilm growth under heterotrophic conditions inBiofilm · 2026Article
- Comparative Genomics ofPathogens (Basel, Switzerland) · 2026Article
- Rapid Analysis of NAD and Other Phosphorylated Metabolites in Complex Biological Samples by Hydrophilic Interaction Liquid Chromatography Coupled with Tandem Mass Spectrometry.Analytical chemistry · 2026Article
- Identification and characterization of the functional tetrameric UDP-glucose pyrophosphorylase frommBio · 2025Article
- Anti-virulence and bactericidal activities of Stattic againstApplied and environmental microbiology · 2023Article
- Novel Chromosomal Mutations Responsible for Fosfomycin Resistance inFrontiers in microbiology · 2020Article
- Immobilization of the Highly Active UDP-Glucose Pyrophosphorylase FromFrontiers in bioengineering and biotechnology · 2020Article
- Two Homologous Enzymes of the GalU Family inInternational journal of molecular sciences · 2019Article
- On the stability of nucleoside diphosphate glucose metabolites: implications for studies of plant carbohydrate metabolism.Journal of experimental botany · 2017Article
- The diversity ofMicrobial genomics · 2016Article
- On the Kinetic and Allosteric Regulatory Properties of the ADP-Glucose Pyrophosphorylase from Rhodococcus jostii: An Approach to Evaluate Glycogen Metabolism in Oleaginous Bacteria.Frontiers in microbiology · 2016Article
- Immunoprotective Efficacy of SixFrontiers in microbiology · 2016Article
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6 authors.
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Abstract
In bacteria, UDP-glucose is a central intermediate in carbohydrate metabolism. The enzyme responsible for its synthesis is encoded by the galU gene and its deletion generates cells unable to ferment galactose. In some bacteria, there is a second gene, galF, encoding for a protein with high sequence identity to GalU. However, the role of GalF has been contradictory regarding its catalytic capability and not well understood. In this work we show that GalF derives from a catalytic (UDP-glucose pyrophosphorylase) ancestor, but its activity is very low compared to GalU. We demonstrated that GalF has some residual UDP-glucose pyrophosphorylase activity by in vitro and in vivo experiments in which the phenotype of a galU (-) strain was reverted by the over-expression of GalF and its mutant. To demonstrate its evolutionary path of "enzyme inactivation" we enhanced the catalysis by mutagenesis and showed the importance of the quaternary structure. This study provides important information to understand the structural and functional evolutionary origin of the protein GalF in enteric bacteria.
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