ArticleBiochemistry2012
Human UDP-α-D-xylose synthase and Escherichia coli ArnA conserve a conformational shunt that controls whether xylose or 4-keto-xylose is produced.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Structural instability impairs function of the UDP-xylose synthase 1 Ile181Asn variant associated with short-stature genetic syndrome in humans.FEBS letters · 2026Article
- Structural characterisation of nucleotide sugar short-chain dehydrogenases/reductases from the thermophilic pseudomurein-containing methanogen Methanothermobacter thermautotrophicus ΔH.The FEBS journal · 2026Article
- Structural Basis for Targeting the Bifunctional Enzyme ArnA.Biomolecules · 2025Article
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- Article
- Cryo-EM Structure of Recombinantly Expressed hUGDH Unveils a Hidden, Alternative Allosteric Inhibitor.Biochemistry · 2025Article
- Decarboxylation in Natural Products Biosynthesis.JACS Au · 2024Review
- Targeting the Conformational Change in ArnA Dehydrogenase for Selective Inhibition of Polymyxin Resistance.Biochemistry · 2023Article
- Mechanistic characterization of UDP-glucuronic acid 4-epimerase.The FEBS journal · 2021Article
- The glycan alphabet is not universal: a hypothesis.Microbial genomics · 2020Article
- Crystallographic snapshots of UDP-glucuronic acid 4-epimerase ligand binding, rotation, and reduction.The Journal of biological chemistry · 2020Article
- Deciphering the enzymatic mechanism of sugar ring contraction in UDP-apiose biosynthesis.Nature catalysis · 2019Article
- Facile and Stereo-Selective Synthesis of UDP-α-D-xylose and UDP-β-L-arabinose Using UDP-Sugar Pyrophosphorylase.Frontiers in chemistry · 2018Article
- Isotope Probing of the UDP-Apiose/UDP-Xylose Synthase Reaction: Evidence of a Mechanism via a Coupled Oxidation and Aldol Cleavage.Angewandte Chemie (International ed. in English) · 2017Article
- Synthesis of UDP-apiose in Bacteria: The marine phototroph Geminicoccus roseus and the plant pathogen Xanthomonas pisi.PloS one · 2017Article
- Functional Characterization of UDP-apiose Synthases from Bryophytes and Green Algae Provides Insight into the Appearance of Apiose-containing Glycans during Plant Evolution.The Journal of biological chemistry · 2016Article
- Characterization of Early Enzymes Involved in TDP-Aminodideoxypentose Biosynthesis en Route to Indolocarbazole AT2433.Chembiochem : a European journal of chemical biology · 2015Article
- Crystal structure of the capsular polysaccharide synthesizing protein CapE of Staphylococcus aureus.Bioscience reports · 2013Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Human UDP-α-D-xylose synthase (hUXS) is a member of the short-chain dehydrogenase/reductase family of nucleotide-sugar modifying enzymes. hUXS contains a bound NAD(+) cofactor that it recycles by first oxidizing UDP-α-D-glucuronic acid (UGA), and then reducing the UDP-α-D-4-keto-xylose (UX4O) to produce UDP-α-D-xylose (UDX). Despite the observation that purified hUXS contains a bound cofactor, it has been reported that exogenous NAD(+) will stimulate enzyme activity. Here we show that a small fraction of hUXS releases the NADH and UX4O intermediates as products during turnover. The resulting apoenzyme can be rescued by exogenous NAD(+), explaining the apparent stimulatory effect of added cofactor. The slow release of NADH and UX4O as side products by hUXS is reminiscent of the Escherichia coli UGA decarboxylase (ArnA), a related enzyme that produces NADH and UX4O as products. We report that ArnA can rebind NADH and UX4O to slowly make UDX. This means that both enzymes share the same catalytic machinery, but differ in the preferred final product. We present a bifurcated rate equation that explains how the substrate is shunted to the distinct final products. Using a new crystal structure of hUXS, we identify the structural elements of the shunt and propose that the local unfolding of the active site directs reactants toward the preferred products. Finally, we present evidence that the release of NADH and UX4O involves a cooperative conformational change that is conserved in both enzymes.
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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.