ArticleThe Journal of biological chemistry2013
The UDP-glucose dehydrogenase of Escherichia coli K-12 displays substrate inhibition by NAD that is relieved by nucleotide triphosphates.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
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- TSSpredator-Web: A web-application for transcription start site prediction and exploration.PloS one · 2026Article
- Convergent genomic responses of human gut bacteria to variations in industrialization.bioRxiv : the preprint server for biology · 2025Article
- Ugd Is Involved in the Synthesis of Glycans of Glycoprotein and LPS and Is Important for Cellulose Degradation inMicroorganisms · 2025Article
- Simultaneous production ofHeliyon · 2023Article
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- The molecular basis of regulation of bacterial capsule assembly by Wzc.Nature communications · 2021Article
- Substrate inhibition by the blockage of product release and its control by tunnel engineering.RSC chemical biology · 2021Article
- mRNA Engineering for the Efficient Chaperone-Mediated Co-Translational Folding of Recombinant Proteins inInternational journal of molecular sciences · 2019Article
- Network-Based Metabolism-Centered Screening of Potential Drug Targets inFrontiers in cellular and infection microbiology · 2019Article
- Distinct reaction mechanisms for hyaluronan biosynthesis in different kingdoms of life.Glycobiology · 2018Article
- A Unique Capsule Locus in the Newly Designated Actinobacillus pleuropneumoniae Serovar 16 and Development of a Diagnostic PCR Assay.Journal of clinical microbiology · 2017Article
- Hyaluronan production and molecular weight is enhanced in pathway-engineered strains of lactate dehydrogenase-deficientMetabolic engineering communications · 2016Article
- Structural Characterization of CalS8, a TDP-α-D-Glucose Dehydrogenase Involved in Calicheamicin Aminodideoxypentose Biosynthesis.The Journal of biological chemistry · 2015Article
- The role of bacterial protein tyrosine phosphatases in the regulation of the biosynthesis of secreted polysaccharides.Antioxidants & redox signaling · 2014Review
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5 authors at 1 institution in 1 country.
Funding
Abstract
UDP-glucose dehydrogenase (Ugd) generates UDP-glucuronic acid, an important precursor for the production of many hexuronic acid-containing bacterial surface glycostructures. In Escherichia coli K-12, Ugd is important for biosynthesis of the environmentally regulated exopolysaccharide known as colanic acid, whereas in other E. coli isolates, the same enzyme is required for production of the constitutive group 1 capsular polysaccharides, which act as virulence determinants. Recent studies have implicated tyrosine phosphorylation in the activation of Ugd from E. coli K-12, although it is not known if this is a feature shared by bacterial Ugd proteins. The activities of Ugd from E. coli K-12 and from the group 1 capsule prototype (serotype K30) were compared. Surprisingly, for both enzymes, site-directed Tyr → Phe mutants affecting the previously proposed phosphorylation site retained similar kinetic properties to the wild-type protein. Purified Ugd from E. coli K-12 had significant levels of NAD substrate inhibition, which could be alleviated by the addition of ATP and several other nucleotide triphosphates. Mutations in a previously identified UDP-glucuronic acid allosteric binding site decreased the binding affinity of the nucleotide triphosphate. Ugd from E. coli serotype K30 was not inhibited by NAD, but its activity still increased in the presence of ATP.
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