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Journal articles on the topic 'UDP-glucose pyrophosphorylase'

Author: Grafiati

Published: 4 June 2021

Last updated: 11 February 2022

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1

Kleczkowski, Leszek A., Matt Geisler, Elisabeth Fitzek, and Malgorzata Wilczynska. "A common structural blueprint for plant UDP-sugar-producing pyrophosphorylases." Biochemical Journal 439, no. 3 (October 13, 2011): 375–81. http://dx.doi.org/10.1042/bj20110730.

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Plant pyrophosphorylases that are capable of producing UDP-sugars, key precursors for glycosylation reactions, include UDP-glucose pyrophosphorylases (A- and B-type), UDP-sugar pyrophosphorylase and UDP-N-acetylglucosamine pyrophosphorylase. Although not sharing significant homology at the amino acid sequence level, the proteins share a common structural blueprint. Their structures are characterized by the presence of the Rossmann fold in the central (catalytic) domain linked to enzyme-specific N-terminal and C-terminal domains, which may play regulatory functions. Molecular mobility between these domains plays an important role in substrate binding and catalysis. Evolutionary relationships and the role of (de)oligomerization as a regulatory mechanism are discussed.

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2

Silva, Elisabete, Ana Rita Marques, Arsénio Mendes Fialho, Ana Teresa Granja, and Isabel Sá-Correia. "Proteins Encoded by Sphingomonas elodea ATCC 31461 rmlA and ugpG Genes, Involved in Gellan Gum Biosynthesis, Exhibit both dTDP- and UDP-Glucose Pyrophosphorylase Activities." Applied and Environmental Microbiology 71, no. 8 (August 2005): 4703–12. http://dx.doi.org/10.1128/aem.71.8.4703-4712.2005.

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ABSTRACT The commercial gelling agent gellan is a heteropolysaccharide produced by Sphingomonas elodea ATCC 31461. In this work, we carried out the biochemical characterization of the enzyme encoded by the first gene (rmlA) of the rml 4-gene cluster present in the 18-gene cluster required for gellan biosynthesis (gel cluster). Based on sequence homology, the putative rml operon is presumably involved in the biosynthesis of dTDP-rhamnose, the sugar necessary for the incorporation of rhamnose in the gellan repeating unit. Heterologous RmlA was purified as a fused His6-RmlA protein from extracts prepared from Escherichia coli IPTG (isopropyl-β-d-thiogalactopyranoside)-induced cells, and the protein was proven to exhibit dTDP-glucose pyrophosphorylase (Km of 12.0 μM for dTDP-glucose) and UDP-glucose pyrophosphorylase (Km of 229.0 μM for UDP-glucose) activities in vitro. The N-terminal region of RmlA exhibits the motif G-X-G-T-R-X2-P-X-T, which is highly conserved among bacterial XDP-sugar pyrophosphorylases. The motif E-E-K-P, with the conserved lysine residue (K163) predicted to be essential for glucose-1-phosphate binding, was observed. The S. elodea ATCC 31461 UgpG protein, encoded by the ugpG gene which maps outside the gel cluster, was previously identified as the UDP-glucose pyrophosphorylase involved in the formation of UDP-glucose, also required for gellan synthesis. In this study, we demonstrate that UgpG also exhibits dTDP-glucose pyrophosphorylase activity in vitro and compare the kinetic parameters of the two proteins for both substrates. DNA sequencing of ugpG gene-adjacent regions and sequence similarity studies suggest that this gene maps with others involved in the formation of sugar nucleotides presumably required for the biosynthesis of another cell polysaccharide(s).

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3

Prakash, Ohm, Jana Führing, John Post, Sharon Shepherd, Thomas Eadsforth, David Gray, Roman Fedorov, and Françoise Routier. "Identification of Leishmania major UDP-Sugar Pyrophosphorylase Inhibitors Using Biosensor-Based Small Molecule Fragment Library Screening." Molecules 24, no. 5 (March 12, 2019): 996. http://dx.doi.org/10.3390/molecules24050996.

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Leishmaniasis is a neglected disease that is caused by different species of the protozoan parasite Leishmania, and it currently affects 12 million people worldwide. The antileishmanial therapeutic arsenal remains very limited in number and efficacy, and there is no vaccine for this parasitic disease. One pathway that has been genetically validated as an antileishmanial drug target is the biosynthesis of uridine diphosphate-glucose (UDP-Glc), and its direct derivative UDP-galactose (UDP-Gal). De novo biosynthesis of these two nucleotide sugars is controlled by the specific UDP-glucose pyrophosphorylase (UGP). Leishmania parasites additionally express a UDP-sugar pyrophosphorylase (USP) responsible for monosaccharides salvage that is able to generate both UDP-Gal and UDP-Glc. The inactivation of the two parasite pyrophosphorylases UGP and USP, results in parasite death. The present study reports on the identification of structurally diverse scaffolds for the development of USP inhibitors by fragment library screening. Based on this screening, we selected a small set of commercially available compounds, and identified molecules that inhibit both Leishmania major USP and UGP, with a half-maximal inhibitory concentration in the 100 µM range. The inhibitors were predicted to bind at allosteric regulation sites, which were validated by mutagenesis studies. This study sets the stage for the development of potent USP inhibitors.

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4

Signorini, M., C. Ferrari, E. Mariotti, F. Dallocchio, and C. M. Bergamini. "Inactivation of skeletal-muscle UDP-glucose pyrophosphorylase by reaction with carboxylate-directed reagents." Biochemical Journal 264, no. 3 (December 15, 1989): 799–804. http://dx.doi.org/10.1042/bj2640799.

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Skeletal-muscle UDP-glucose pyrophosphorylase is inactivated by reaction with 2-ethoxy-N-(ethoxy-carbonyl)-1,2-dihydroquinoline (EEDQ) and 1-(3-dimethylaminopropyl-3-ethylcarbodi-imide (EDAC), two reagents specific for carboxylate groups. The former reagent is a more effective inactivator than EDAC. Although no evidence of reversible enzyme-reagent complexes of the affinity-labelling type was obtained by kinetic analysis of the inactivation, the selective protection of UDP-glucose pyrophosphorylase activity against inactivation by EEDQ in the presence of uridine substrates is indicative of an active-site-directed effect. The results are consistent with the hypothesis that EEDQ modifies a single carboxylate group located in a hydrophobic domain close to the substrate-binding site, leading to enzyme inactivation. In contrast, the reaction between UDP-glucose pyrophosphorylase and EDAC appears to involve a different region of the enzyme.

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5

Rodríguez-Díaz, Jesús, and María J. Yebra. "Enhanced UDP-glucose and UDP-galactose by homologous overexpression of UDP-glucose pyrophosphorylase in Lactobacillus casei." Journal of Biotechnology 154, no. 4 (July 2011): 212–15. http://dx.doi.org/10.1016/j.jbiotec.2011.05.015.

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6

Kleczkowski, Leszek A., Françoise Martz, and Malgorzata Wilczynska. "Factors affecting oligomerization status of UDP-glucose pyrophosphorylase." Phytochemistry 66, no. 24 (December 2005): 2815–21. http://dx.doi.org/10.1016/j.phytochem.2005.09.034.

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7

Kusunoki, M., Y. Kitagawa, H. Naitou, Y. Katsube, Y. Sakamoto, K. Tanizawa, and T. Fukui. "Left-handed β-helix protein UDP-glucose pyrophosphorylase." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (August 8, 1996): C110—C111. http://dx.doi.org/10.1107/s0108767396094731.

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8

Chen, Rongzhi, Xiao Zhao, Zhe Shao, Lili Zhu, and Guangcun He. "Multiple isoforms of UDP-glucose pyrophosphorylase in rice." Physiologia Plantarum 129, no. 4 (April 2007): 725–36. http://dx.doi.org/10.1111/j.1399-3054.2007.00865.x.

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9

Kleczkowski, Leszek A. "Glucose activation and metabolism through UDP-glucose pyrophosphorylase in plants." Phytochemistry 37, no. 6 (December 1994): 1507–15. http://dx.doi.org/10.1016/s0031-9422(00)89568-0.

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10

Lamerz, Anne-Christin, Sebastian Damerow, Barbara Kleczka, Martin Wiese, Ger van Zandbergen, Jens Lamerz, Alexander Wenzel, et al. "Deletion of UDP-glucose pyrophosphorylase reveals a UDP-glucose independent UDP-galactose salvage pathway in Leishmania major." Glycobiology 20, no. 7 (March 24, 2010): 872–82. http://dx.doi.org/10.1093/glycob/cwq045.

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11

HIGUITA, Juan-Carlos, Alberto ALAPE-GIRÓN, Monica THELESTAM, and Abram KATZ. "A point mutation in the UDP-glucose pyrophosphorylase gene results in decreases of UDP-glucose and inactivation of glycogen synthase." Biochemical Journal 370, no. 3 (March 15, 2003): 995–1001. http://dx.doi.org/10.1042/bj20021320.

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The regulatory role of UDP-glucose in glycogen biogenesis was investigated in fibroblasts containing a point mutation in the UDP-glucose pyrophosphorylase gene and, consequently, chronically low UDP-glucose levels (Qc). Comparisons were made with cells having the intact gene and restored UDP-glucose levels (G3). Glycogen was always very low in Qc cells. [14C]Glucose incorporation into glycogen was decreased and unaffected by insulin in Qc cells, whereas insulin stimulated glucose incorporation by 50% in G3 cells. Glycogen synthase (GS) activity measured in vitro was virtually absent and the amount of enzyme in Qc cells was decreased by about 50%. The difference in GS activity between cells persisted even when G3 cells were devoid of glycogen. Incubation of G3 cell extracts with either exogenous UDP-glucose or glycogen resulted in increases in GS activity. Incubation of Qc cell extracts with exogenous UDP-glucose had no effect on GS activity; however, incubation with glycogen fully restored enzyme activity. Incubation of G3 cell extracts with radioactive UDP-glucose resulted in substantial binding of ligand to immunoprecipitated GS, whereas no binding was detected in Qc immunoprecipitates. Incubation of Qc cell extracts with exogenous glycogen fully restored UDP-glucose binding in the immunoprecipitate. These data suggest that chronically low UDP-glucose levels in cells result in inactivation of GS, owing to loss of the ability of GS to bind UDP-glucose.

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12

Nakano, Kenichi, Yasuko Omura, Mitsuo Tagaya, and Toshio Fukui. "UDP-Glucose Pyrophosphorylase from Potato Tuber: Purification and Characterization1." Journal of Biochemistry 106, no. 3 (September 1989): 528–32. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a122886.

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13

Kleczkowski, Leszek A., Matt Geisler, Iwona Ciereszko, and Henrik Johansson. "UDP-Glucose Pyrophosphorylase. An Old Protein with New Tricks." Plant Physiology 134, no. 3 (March 2004): 912–18. http://dx.doi.org/10.1104/pp.103.036053.

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14

Martínez, Lucila I., Claudia V. Piattoni, Sergio A. Garay, Daniel E. Rodrígues, Sergio A. Guerrero, and Alberto A. Iglesias. "Redox regulation of UDP-glucose pyrophosphorylase from Entamoeba histolytica." Biochimie 93, no. 2 (February 2011): 260–68. http://dx.doi.org/10.1016/j.biochi.2010.09.019.

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15

Elling, Lothar, and Maria-Regina Kula. "Purification of UDP-glucose pyrophosphorylase from germinated barley (malt)." Journal of Biotechnology 34, no. 2 (May 1994): 157–63. http://dx.doi.org/10.1016/0168-1656(94)90085-x.

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16

Sharma, Monica, Swati Sharma, Pallab Ray, and Anuradha Chakraborti. "Targeting Streptococcus pneumoniae UDP-glucose pyrophosphorylase (UGPase): in vitro validation of a putative inhibitor." Drug Target Insights 14, no. 1 (October 7, 2020): 26–33. http://dx.doi.org/10.33393/dti.2020.2103.

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Background: Genome plasticity of Streptococcus pneumoniae is responsible for the reduced efficacy of various antibiotics and capsular polysaccharide based vaccines. Therefore targets independent of capsular types are sought to control the pneumococcal pathogenicity. UcrDP-glucose pyrophosphorylase (UGPase) is one such desired candidate being responsible for the synthesis of UDP-glucose, a sugar-precursor in capsular biosynthesis and metabolic Leloir pathway. Being crucial to pneumococcal pathobiology, the effect of UGPase inhibition on virulence was evaluated in vitro. Methods: A putative inhibitor (UDP) was evaluated for effective inhibitory concentration in S. pneumoniae and A549 cells, its efficacy and toxicity. Effect of UDP on adherence and phagocytosis was measured in human respiratory epithelial (A549 and HEp-2) and macrophage (THP1 and J774.A.1) cell lines respectively. Results: A differential effective inhibitory concentration of UDP for UGPase inhibition was observed in S. pneumoniae and A549 cells i.e. 5 µM and 100 µM respectively. UDP treatments lowered percent cytotoxicity in pneumococcal infected monolayers and didn't exert adverse effects on viabilities. S. pneumoniae adherence to host cells was decreased significantly with UDP treatments. UDP induced the secretion of IL-1β, TNF-α, IL-6, and IL-8 and increased pneumococcal phagocytosis. Conclusion: Our study shows UDP mediated decrease in the virulence of S. pneumoniae and demonstrates UDP as an effective inhibitor of pneumococcal UGPase.

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17

Flores-Dı́az, Marietta, Alberto Alape-Girón, Bengt Persson, Piero Pollesello, Michael Moos, Christoph von Eichel-Streiber, Monica Thelestam, and Inger Florin. "Cellular UDP-Glucose Deficiency Caused by a Single Point Mutation in the UDP-Glucose Pyrophosphorylase Gene." Journal of Biological Chemistry 272, no. 38 (September 19, 1997): 23784–91. http://dx.doi.org/10.1074/jbc.272.38.23784.

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18

McCoy, Jason G., Eduard Bitto, Craig A. Bingman, Gary E. Wesenberg, Ryan M. Bannen, Dmitry A. Kondrashov, and George N. Phillips. "Structure and Dynamics of UDP–Glucose Pyrophosphorylase from Arabidopsis thaliana with Bound UDP–Glucose and UTP." Journal of Molecular Biology 366, no. 3 (February 2007): 830–41. http://dx.doi.org/10.1016/j.jmb.2006.11.059.

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19

Sowokinos, J. R., J. P. Spychalla, and S. L. Desborough. "Pyrophosphorylases in Solanum tuberosum (IV. Purification, Tissue Localization, and Physicochemical Properties of UDP-Glucose Pyrophosphorylase)." Plant Physiology 101, no. 3 (March 1, 1993): 1073–80. http://dx.doi.org/10.1104/pp.101.3.1073.

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20

Katsube, Takuya, Yasuaki Kazuta, Hiroyuki Mori, Kenichi Nakano, Katsuyuki Tanizawa, and Toshio Fukui. "UDP-Glucose Pyrophosphorylase from Potato Tuber: cDNA Cloning and Sequencing1." Journal of Biochemistry 108, no. 2 (August 1990): 321–26. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a123200.

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21

Soares, Jose Sergio M., Agustina Gentile, Valeria Scorsato, Aline da C. Lima, Eduardo Kiyota, Marcelo Leite dos Santos, Claudia V. Piattoni, Steven C. Huber, Ricardo Aparicio, and Marcelo Menossi. "Oligomerization, Membrane Association, andin VivoPhosphorylation of Sugarcane UDP-glucose Pyrophosphorylase." Journal of Biological Chemistry 289, no. 48 (October 15, 2014): 33364–77. http://dx.doi.org/10.1074/jbc.m114.590125.

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22

Chivasa, Stephen, Daniel F. A. Tomé, and Antoni R. Slabas. "UDP-Glucose Pyrophosphorylase Is a Novel Plant Cell Death Regulator." Journal of Proteome Research 12, no. 4 (March 12, 2013): 1743–53. http://dx.doi.org/10.1021/pr3010887.

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23

Elling, Lothar. "Kinetic characterization of UDP-glucose pyrophosphorylase from germinated barley (malt)." Phytochemistry 42, no. 4 (July 1996): 955–60. http://dx.doi.org/10.1016/0031-9422(96)00089-1.

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24

Kim, Hun, Jongkeun Choi, Truc Kim, Neratur K. Lokanath, Sung Chul Ha, Se Won Suh, Hye-Yeon Hwang, and Kyeong Kyu Kim. "Structural basis for the reaction mechanism of UDP-glucose pyrophosphorylase." Molecules and Cells 29, no. 4 (March 15, 2010): 397–405. http://dx.doi.org/10.1007/s10059-010-0047-6.

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25

Yang, Yueqin, Hariprasad Vankayalapati, Manshu Tang, Yingbo Zheng, Yingri Li, Cong Ma, and Kent Lai. "Discovery of Novel Inhibitors Targeting Multi-UDP-hexose Pyrophosphorylases as Anticancer Agents." Molecules 25, no. 3 (February 3, 2020): 645. http://dx.doi.org/10.3390/molecules25030645.

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To minimize treatment toxicities, recent anti-cancer research efforts have switched from broad-based chemotherapy to targeted therapy, and emerging data show that altered cellular metabolism in cancerous cells can be exploited as new venues for targeted intervention. In this study, we focused on, among the altered metabolic processes in cancerous cells, altered glycosylation due to its documented roles in cancer tumorigenesis, metastasis and drug resistance. We hypothesize that the enzymes required for the biosynthesis of UDP-hexoses, glycosyl donors for glycan synthesis, could serve as therapeutic targets for cancers. Through structure-based virtual screening and kinetic assay, we identified a drug-like chemical fragment, GAL-012, that inhibit a small family of UDP-hexose pyrophosphorylases-galactose pyro-phosphorylase (GALT), UDP-glucose pyrophosphorylase (UGP2) and UDP-N-acetylglucosamine pyrophosphorylase (AGX1/UAP1) with an IC50 of 30 µM. The computational docking studies supported the interaction of GAL-012 to the binding sites of GALT at Trp190 and Ser192, UGP2 at Gly116 and Lys127, and AGX1/UAP1 at Asn327 and Lys407, respectively. One of GAL-012 derivatives GAL-012-2 also demonstrated the inhibitory activity against GALT and UGP2. Moreover, we showed that GAL-012 suppressed the growth of PC3 cells in a dose-dependent manner with an EC50 of 75 µM with no effects on normal skin fibroblasts at 200 µM. Western blot analysis revealed reduced expression of pAKT (Ser473), pAKT (Thr308) by 77% and 72%, respectively in the treated cells. siRNA experiments against the respective genes encoding the pyrophosphorylases were also performed and the results further validated the proposed roles in cancer growth inhibition. Finally, synergistic relationships between GAL-012 and tunicamycin, as well as bortezomib (BTZ) in killing cultured cancer cells were observed, respectively. With its unique scaffold and relatively small size, GAL-012 serves as a promising early chemotype for optimization to become a safe, effective, multi-target anti-cancer drug candidate which could be used alone or in combination with known therapeutics.

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26

Boels, Ingeborg C., Ana Ramos, Michiel Kleerebezem, and Willem M. de Vos. "Functional Analysis of the Lactococcus lactis galU and galE Genes and Their Impact on Sugar Nucleotide and Exopolysaccharide Biosynthesis." Applied and Environmental Microbiology 67, no. 7 (July 1, 2001): 3033–40. http://dx.doi.org/10.1128/aem.67.7.3033-3040.2001.

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ABSTRACT We studied the UDP-glucose pyrophosphorylase (galU) and UDP-galactose epimerase (galE) genes of Lactococcus lactis MG1363 to investigate their involvement in biosynthesis of UDP-glucose and UDP-galactose, which are precursors of glucose- and galactose-containing exopolysaccharides (EPS) in L. lactis. The lactococcal galU gene was identified by a PCR approach using degenerate primers and was found by Northern blot analysis to be transcribed in a monocistronic RNA. The L. lactis galU gene could complement an Escherichia coli galU mutant, and overexpression of this gene in L. lactis under control of the inducible nisA promoter resulted in a 20-fold increase in GalU activity. Remarkably, this resulted in approximately eightfold increases in the levels of both UDP-glucose and UDP-galactose. This indicated that the endogenous GalE activity is not limiting and that the GalU activity level in wild-type cells controls the biosynthesis of intracellular UDP-glucose and UDP-galactose. The increased GalU activity did not significantly increase NIZO B40 EPS production. Disruption of the galE gene resulted in poor growth, undetectable intracellular levels of UDP-galactose, and elimination of EPS production in strain NIZO B40 when cells were grown in media with glucose as the sole carbon source. Addition of galactose restored wild-type growth in the galE disruption mutant, while the level of EPS production was approximately one-half the wild-type level.

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27

Fujita, Ken-Ichi, Teruhiko Tanigawa, Kiyotaka Machida, Toshio Tanaka, and Makoto Taniguchi. "Synthesis of uridine 5′-monophosphate glucose as an inhibitor of UDP-glucose pyrophosphorylase." Journal of Fermentation and Bioengineering 86, no. 2 (January 1998): 145–48. http://dx.doi.org/10.1016/s0922-338x(98)80052-4.

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28

Yang, Ting, and Maor Bar-Peled. "Identification of a novel UDP-sugar pyrophosphorylase with a broad substrate specificity in Trypanosoma cruzi." Biochemical Journal 429, no. 3 (July 14, 2010): 533–43. http://dx.doi.org/10.1042/bj20100238.

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The diverse types of glycoconjugates synthesized by trypanosomatid parasites are unique compared with the host cells. These glycans are required for the parasite survival, invasion or evasion of the host immune system. Synthesis of those glycoconjugates requires a constant supply of nucleotide-sugars (NDP-sugars), yet little is known about how these NDP-sugars are made and supplied. In the present paper, we report a functional gene from Trypanosoma cruzi that encodes a nucleotidyltransferase, which is capable of transforming different types of sugar 1-phosphates and NTP into NDP-sugars. In the forward reaction, the enzyme catalyses the formation of UDP-glucose, UDP-galactose, UDP-xylose and UDP-glucuronic acid, from their respective monosaccharide 1-phosphates in the presence of UTP. The enzyme could also convert glucose 1-phosphate and TTP into TDP-glucose, albeit at lower efficiency. The enzyme requires bivalent ions (Mg2+ or Mn2+) for its activity and is highly active between pH 6.5 and pH 8.0, and at 30–42 °C. The apparent Km values for the forward reaction were 177 μM (glucose 1-phosphate) and 28.4 μM (UTP) respectively. The identification of this unusual parasite enzyme with such broad substrate specificities suggests an alternative pathway that might play an essential role for nucleotide-sugar biosynthesis and for the regulation of the NDP-sugar pool in the parasite.

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29

Padilla, Leandro, Susanne Morbach, Reinhard Krämer, and Eduardo Agosin. "Impact of Heterologous Expression of Escherichia coli UDP-Glucose Pyrophosphorylase on Trehalose and Glycogen Synthesis in Corynebacterium glutamicum." Applied and Environmental Microbiology 70, no. 7 (July 2004): 3845–54. http://dx.doi.org/10.1128/aem.70.7.3845-3854.2004.

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ABSTRACT Trehalose is a disaccharide with a wide range of applications in the food industry. We recently proposed a strategy for trehalose production based on improved strains of the gram-positive bacterium Corynebacterium glutamicum. This microorganism synthesizes trehalose through two major pathways, OtsBA and TreYZ, by using UDP-glucose and ADP-glucose, respectively, as the glucosyl donors. In this paper we describe improvement of the UDP-glucose supply through heterologous expression in C. glutamicum of the UDP-glucose pyrophosphorylase gene from Escherichia coli, either expressed alone or coexpressed with the E. coli ots genes (galU otsBA synthetic operon). The impact of such expression on trehalose accumulation and excretion, glycogen accumulation, and the growth pattern of new recombinant strains is described. Expression of the galU otsBA synthetic operon resulted in a sixfold increase in the accumulated and excreted trehalose relative to that in a wild-type strain. Surprisingly, single expression of galU also resulted in an increase in the accumulated trehalose. This increase in trehalose synthesis was abolished upon deletion of the TreYZ pathway. These results proved that UDP-glucose has an important role not only in the OtsBA pathway but also in the TreYZ pathway.

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30

Niewoehner, C. B., and B. Neil. "Mechanism of delayed hepatic glycogen synthesis after an oral galactose load vs. an oral glucose load in adult rats." American Journal of Physiology-Endocrinology and Metabolism 263, no. 1 (July 1, 1992): E42—E49. http://dx.doi.org/10.1152/ajpendo.1992.263.1.e42.

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We have compared the effects of administration of oral galactose or glucose (1 g/kg) to 24-h fasted rats to examine the mechanism by which galactose regulates its own incorporation into liver glycogen in vivo. Liver glycogen increased to a maximum more slowly after galactose than after glucose administration (0.14 vs. 0.29 mumol.g liver-1.min-1). Glycogen accumulation after the galactose load was 70% of that after the glucose load (149 vs. 214 mumol), and the net increase in liver glycogen represented the same proportion (24 vs. 22%) of added carbohydrate after urinary loss of galactose was accounted for. Slower glycogen accumulation after galactose vs. glucose loading could not be explained by galactosuria, by differences in the active forms of synthase or phosphorylase, by end product (glycogen) inhibition of synthase phosphatase, or by different concentrations of the known allosteric effectors of synthase R plus I and phosphorylase a. Similar increases in glucose 6-phosphate were observed after both hexoses. AMP and ADP increased only transiently after galactose administration, and ATP, UTP, and Pi concentrations were unchanged. The UDP-glucose concentration decreased, whereas the UDP-galactose concentration increased two- to threefold after galactose but not glucose administration. The UDP-glucose pyrophosphorylase reaction is inhibited competitively by UDP-galactose. This could explain the decreased UDP-glucose concentration and the reduced rate of glycogen synthesis after galactose was given.

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31

De Luca, Claudio, Manfred Lansing, Fabiana Crescenzi, Irene Martini, Gwo-Jenn Shen, Michael O'Regan, and Chi-Huey Wong. "Overexpression, one-step purification and characterization of UDP-glucose dehydrogenase and UDP-N-acetylglucosamine pyrophosphorylase." Bioorganic & Medicinal Chemistry 4, no. 1 (January 1996): 131–41. http://dx.doi.org/10.1016/0968-0896(95)00159-x.

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32

Borovkov, Alex Y., Phillip E. McClean, and Gary A. Secor. "Organization and transcription of the gene encoding potato UDP-glucose pyrophosphorylase." Gene 186, no. 2 (February 1997): 293–97. http://dx.doi.org/10.1016/s0378-1119(96)00724-x.

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33

Führing, Jana, Sebastian Damerow, Roman Fedorov, Julia Schneider, Anja-Katharina Münster-Kühnel, and Rita Gerardy-Schahn. "Octamerization is essential for enzymatic function of human UDP-glucose pyrophosphorylase." Glycobiology 23, no. 4 (December 18, 2012): 426–37. http://dx.doi.org/10.1093/glycob/cws217.

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34

Zhu, Bao-Hua, Hong-Ping Shi, Guan-Pin Yang, Na-Na Lv, Miao Yang, and Ke-Hou Pan. "Silencing UDP-glucose pyrophosphorylase gene in Phaeodactylum tricornutum affects carbon allocation." New Biotechnology 33, no. 1 (January 2016): 237–44. http://dx.doi.org/10.1016/j.nbt.2015.06.003.

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35

KOO, Hyun Min, Seok-Won YIM, Chang-Seung LEE, Yu Ryang PYUN, and Yu Sam KIM. "Cloning, Sequencing, and Expression of UDP-Glucose Pyrophosphorylase Gene fromAcetobacter xylinumBRC5." Bioscience, Biotechnology, and Biochemistry 64, no. 3 (January 2000): 523–29. http://dx.doi.org/10.1271/bbb.64.523.

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36

Steiner, Thomas, Anne-Christin Lamerz, Petra Hess, Constanze Breithaupt, Stephan Krapp, Gleb Bourenkov, Robert Huber, Rita Gerardy-Schahn, and Uwe Jacob. "Open and Closed Structures of the UDP-glucose Pyrophosphorylase fromLeishmania major." Journal of Biological Chemistry 282, no. 17 (February 15, 2007): 13003–10. http://dx.doi.org/10.1074/jbc.m609984200.

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37

Othman, R., H. L. Chong, and A. M. H. Zeti. "Cloning and recombinant expression of UDP-glucose pyrophosphorylase from Eucheuma denticulatum." Journal of Biotechnology 150 (November 2010): 483. http://dx.doi.org/10.1016/j.jbiotec.2010.09.736.

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38

Ragheb, Jack A., and Robert P. Dottin. "Structure and sequence of a UDP glucose pyrophosphorylase gene ofDictyostelium discoideum." Nucleic Acids Research 15, no. 9 (1987): 3891–906. http://dx.doi.org/10.1093/nar/15.9.3891.

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39

Entwistle, G., and T. A. Rees. "Enzymic capacities of amyloplasts from wheat (Triticum aestivum) endosperm." Biochemical Journal 255, no. 2 (October 15, 1988): 391–96. http://dx.doi.org/10.1042/bj2550391.

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Lysates of protoplasts from the endosperm of developing grains of wheat (Triticum aestivum) were fractionated on density gradients of Nycodenz to give amyloplasts. Enzyme distribution on the gradients suggested that: (i) starch synthase and ADP-glucose pyrophosphorylase are confined to the amyloplasts; (ii) pyrophosphate: fructose-6-phosphate 1-phosphotransferase and UDP-glucose pyrophosphorylase are confined to the cytosol; (iii) a significant proportion (23-45%) of each glycolytic enzyme, from phosphoglucomutase to pyruvate kinase inclusive, is in the amyloplast. Starch synthase, ADP-glucose pyrophosphorylase and each of the glycolytic enzymes showed appreciable latency when assayed in unfractionated lysates of protoplasts. No activity of fructose-1,6-bisphosphatase was found in amyloplasts or in homogenates of endosperm. Antibody to plastidic fructose-1,6-bisphosphatase did not react positively, in an immunoblot analysis, with any protein in extracts of wheat endosperm. It is argued that wheat endosperm lacks significant plastidic fructose-1,6-bisphosphatase and that carbon for starch synthesis does not enter the amyloplast as a C-3 compound but probably as hexose phosphate.

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40

Goulard, F., M. Diouris, E. Deslandes, and J. Y. Floc'h. "An HPLC method for the assay of UDP-glucose pyrophosphorylase and UDP-glucose-4-epimerase in Solieria chordalis (Rhodophyceae)." Phytochemical Analysis 12, no. 6 (2001): 363–65. http://dx.doi.org/10.1002/pca.604.

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41

Sener, Keriman, Zuojun Shen, David S. Newburg, and Edward L. Jarroll. "Amino sugar phosphate levels in Giardia change during cyst wall formation." Microbiology 150, no. 5 (May 1, 2004): 1225–30. http://dx.doi.org/10.1099/mic.0.26898-0.

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The parasite Giardia intestinalis exists as a trophozoite (vegetative) that infects the human small intestine, and a cyst (infective) that is shed in host faeces. Cyst viability in the environment depends upon a protective cyst wall, which consists of proteins and a unique β(1-3) GalNAc homopolymer. UDP-GalNAc, the precursor for this polysaccharide, is synthesized from glucose by an enzyme pathway that involves amino sugar phosphate intermediates. Using a novel method of microanalysis by capillary electrophoresis, the levels of amino sugar phosphate intermediates in trophozoites before encystment, during a period of active encystment and after the peak of encystment were measured. These levels were used to deduce metabolic control of amino sugar phosphates associated with encystment. Levels of amino sugar phosphate intermediates increased during encystment, and then decreased to nearly non-encysting levels. The most pronounced increase was in glucosamine 6-phosphate, which is the first substrate unique in this pathway, and which is the positive effector for the pathway's putative rate-controlling enzyme, UDP-GlcNAc pyrophosphorylase. Moreover, more UDP-GalNAc than UDP-GlcNAc, its direct precursor, was detected at 24 h. It is postulated that the enhanced UDP-GalNAc is a result of enhanced synthesis of UDP-GlcNAc by the pyrophosphorylase, and its preferential conversion to UDP-GalNAc. These results suggest that kinetics of amino sugar phosphate synthesis in encysting Giardia favours the direction that supports cyst wall synthesis. The enzymes involved in synthesis of UDP-GalNAc and its conversion to cyst wall might be potential targets for therapeutic inhibitors of Giardia infection.

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42

Degeest, Bart, Frederik Vaningelgem, Andrew P. Laws, and Luc De Vuyst. "UDP-N-Acetylglucosamine 4-Epimerase Activity Indicates the Presence of N-Acetylgalactosamine in Exopolysaccharides of Streptococcus thermophilus Strains." Applied and Environmental Microbiology 67, no. 9 (September 1, 2001): 3976–84. http://dx.doi.org/10.1128/aem.67.9.3976-3984.2001.

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ABSTRACT The monomer composition of the exopolysaccharides (EPS) produced byStreptococcus thermophilus LY03 and S. thermophilus Sfi20 were evaluated by high-pressure liquid chromatography with amperometric detection and nuclear magnetic resonance spectroscopy. Both strains produced the same EPS composed of galactose, glucose, and N-acetylgalactosamine. Further, it was demonstrated that the activity of the precursor-producing enzyme UDP-N-acetylglucosamine 4-epimerase, converting UDP-N-acetylglucosamine into UDP-N-acetylgalactosamine, is responsible for the presence of N-acetylgalactosamine in the EPS repeating units of both strains. The activity of UDP-N-acetylglucosamine 4-epimerase was higher in bothS. thermophilus strains than in a non-EPS-producing control strain. However, the level of this activity was not correlated with EPS yields, a result independent of the carbohydrate source applied in the fermentation process. On the other hand, both the amounts of EPS and the carbohydrate consumption rates were influenced by the type of carbohydrate source used during S. thermophilus Sfi20 fermentations. A correlation between activities of the enzymes α-phosphoglucomutase, UDP-glucose pyrophosphorylase, and UDP-galactose 4-epimerase and EPS yields was seen. These experiments confirm earlier observed results for S. thermophilus LY03, although S. thermophilusSfi20 preferentially consumed glucose for EPS production instead of lactose in contrast to the former strain.

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Reynolds, Thomas H., Yunbae Pak, Thurl E. Harris, Jill Manchester, Eugene J. Barrett, and John C. Lawrence. "Effects of Insulin and Transgenic Overexpression of UDP-glucose Pyrophosphorylase on UDP-glucose and Glycogen Accumulation in Skeletal Muscle Fibers." Journal of Biological Chemistry 280, no. 7 (December 13, 2004): 5510–15. http://dx.doi.org/10.1074/jbc.m413614200.

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44

Berbis, M., Jose Sanchez-Puelles, F. Canada, and Jesus Jimenez-Barbero. "Structure and Function of Prokaryotic UDP-Glucose Pyrophosphorylase, A Drug Target Candidate." Current Medicinal Chemistry 22, no. 14 (April 24, 2015): 1687–97. http://dx.doi.org/10.2174/0929867322666150114151248.

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Meng, M., M. Geisler, H. Johansson, J. Harholt, H. V. Scheller, E. J. Mellerowicz, and L. A. Kleczkowski. "UDP-Glucose Pyrophosphorylase is not Rate Limiting, but is Essential in Arabidopsis." Plant and Cell Physiology 50, no. 5 (April 13, 2009): 998–1011. http://dx.doi.org/10.1093/pcp/pcp052.

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Vella, John, and Les Copeland. "UDP-glucose pyrophosphorylase from the plant fraction of nitrogen-fixing soybean nodules." Physiologia Plantarum 78, no. 1 (January 1990): 140–46. http://dx.doi.org/10.1034/j.1399-3054.1990.780123.x.

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Führing, Jana, Johannes T. Cramer, Françoise H. Routier, Anne-Christin Lamerz, Petra Baruch, Rita Gerardy-Schahn, and Roman Fedorov. "Catalytic Mechanism and Allosteric Regulation of UDP-Glucose Pyrophosphorylase from Leishmania major." ACS Catalysis 3, no. 12 (November 19, 2013): 2976–85. http://dx.doi.org/10.1021/cs4007777.

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48

Coleman, Heather D., Thomas Canam, Kyu-Young Kang, David D. Ellis, and Shawn D. Mansfield. "Over-expression of UDP-glucose pyrophosphorylase in hybrid poplar affects carbon allocation." Journal of Experimental Botany 58, no. 15-16 (December 2007): 4257–68. http://dx.doi.org/10.1093/jxb/erm287.

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Lightcap, Eric S., and Perry A. Frey. "μ-Monothiopyrophosphate as a Substrate for Inorganic Pyrophosphatase and UDP-Glucose Pyrophosphorylase." Archives of Biochemistry and Biophysics 335, no. 1 (November 1996): 183–90. http://dx.doi.org/10.1006/abbi.1996.0496.

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Zavala, Agustín, Verónica Kovacec, Gustavo Levín, Albertina Moglioni, María Victoria Miranda, Ernesto García, Laura Bonofiglio, and Marta Mollerach. "Screening assay for inhibitors of a recombinant Streptococcus pneumoniae UDP-glucose pyrophosphorylase." Journal of Enzyme Inhibition and Medicinal Chemistry 32, no. 1 (January 1, 2017): 203–7. http://dx.doi.org/10.1080/14756366.2016.1247055.

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