ArticleThe Journal of biological chemistry2010
Leishmania UDP-sugar pyrophosphorylase: the missing link in galactose salvage?
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 54 citations in OpenAlex.
- The post-reactive structures ofMicrobiology spectrum · 2025Article
- Role of EhLINE1_ORF1p outside retrotransposition: Downregulation causes growth defects inJournal of biosciences · 2025Article
- Consumption of Galactose byPathogens (Basel, Switzerland) · 2022Article
- Identification ofMolecules (Basel, Switzerland) · 2019Article
- CRISPR/Cas9 and glycomics tools forThe Journal of biological chemistry · 2019Article
- UDP-glycosyltransferase genes in trypanosomatid genomes have diversified independently to meet the distinct developmental needs of parasite adaptations.BMC evolutionary biology · 2018Article
- Facile and Stereo-Selective Synthesis of UDP-α-D-xylose and UDP-β-L-arabinose Using UDP-Sugar Pyrophosphorylase.Frontiers in chemistry · 2018Article
- UDP-Sugar Producing Pyrophosphorylases: Distinct and Essential Enzymes With Overlapping Substrate Specificities, ProvidingFrontiers in plant science · 2018Review
- Substrate Specificity and Inhibitor Sensitivity of Plant UDP-Sugar Producing Pyrophosphorylases.Frontiers in plant science · 2017Article
- Depletion of UDP-Glucose and UDP-Galactose Using a Degron System Leads to Growth Cessation of Leishmania major.PLoS neglected tropical diseases · 2015Article
- Sugar activation and glycosylation in Plasmodium.Malaria journal · 2015Review
- Leishmania major UDP-sugar pyrophosphorylase salvages galactose for glycoconjugate biosynthesis.International journal for parasitology · 2015Article
- A quaternary mechanism enables the complex biological functions of octameric human UDP-glucose pyrophosphorylase, a key enzyme in cell metabolism.Scientific reports · 2015Article
- Metabolic reprogramming during purine stress in the protozoan pathogen Leishmania donovani.PLoS pathogens · 2014Article
- Biosynthesis of GDP-fucose and other sugar nucleotides in the blood stages of Plasmodium falciparum.The Journal of biological chemistry · 2013Article
- Biochemical and biophysical characterization of the sialyl-/hexosyltransferase synthesizing the meningococcal serogroup W135 heteropolysaccharide capsule.The Journal of biological chemistry · 2013Article
- Characterization of recombinant UDP- and ADP-glucose pyrophosphorylases and glycogen synthase to elucidate glucose-1-phosphate partitioning into oligo- and polysaccharides in Streptomyces coelicolor.Journal of bacteriology · 2012Article
- Biosynthetic origin and mechanism of formation of the aminoribosyl moiety of peptidyl nucleoside antibiotics.Journal of the American Chemical Society · 2011Article
- Characterization, localization, essentiality, and high-resolution crystal structure of glucosamine 6-phosphate N-acetyltransferase from Trypanosoma brucei.Eukaryotic cell · 2011Article
- UDP-sugar pyrophosphorylase: a new old mechanism for sugar activation.Plant physiology · 2011Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Leishmania parasite glycocalyx is rich in galactose-containing glycoconjugates that are synthesized by specific glycosyltransferases that use UDP-galactose as a glycosyl donor. UDP-galactose biosynthesis is thought to be predominantly a de novo process involving epimerization of the abundant nucleotide sugar UDP-glucose by the UDP-glucose 4-epimerase, although galactose salvage from the environment has been demonstrated for Leishmania major. Here, we present the characterization of an L. major UDP-sugar pyrophosphorylase able to reversibly activate galactose 1-phosphate into UDP-galactose thus proving the existence of the Isselbacher salvage pathway in this parasite. The ordered bisubstrate mechanism and high affinity of the enzyme for UTP seem to favor the synthesis of nucleotide sugar rather than their pyrophosphorolysis. Although L. major UDP-sugar pyrophosphorylase preferentially activates galactose 1-phosphate and glucose 1-phosphate, the enzyme is able to act on a variety of hexose 1-phosphates as well as pentose 1-phosphates but not hexosamine 1-phosphates and hence presents a broad in vitro specificity. The newly identified enzyme exhibits a low but significant homology with UDP-glucose pyrophosphorylases and conserved in particular is the pyrophosphorylase consensus sequence and residues involved in nucleotide and phosphate binding. Saturation transfer difference NMR spectroscopy experiments confirm the importance of these moieties for substrate binding. The described leishmanial enzyme is closely related to plant UDP-sugar pyrophosphorylases and presents a similar substrate specificity suggesting their common origin.
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