Enzymatic analysis of uridine diphosphate N-acetyl-d -glucosamine

Analytical Biochemistry

Volumn 381, Issue 1, 2008, Pages 94-100

  Namboori, Seema C ^a   Graham, David E ^a  

^a UNIVERSITY OF TEXAS AT AUSTIN   (United States)

Author keywords

Endpoint assay; Fluorescence; Oxidoreductase; Posttranslational glycosylation; Sugar nucleotide; UDP N acetyl d glucosamine

Indexed keywords

ENZYMES; ESCHERICHIA COLI; FLUORESCENCE; GLUCOSAMINE; LANTHANUM COMPOUNDS; NUCLEOTIDES; YEAST;

EQUIVALENT CONCENTRATIONS; FLUOROMETRIC METHOD; HIGH-THROUGHPUT ANALYSIS; METHANOCOCCUS MARIPALUDIS; N-ACETYL-D-GLUCOSAMINE; OXIDOREDUCTASES; SUGAR NUCLEOTIDES; TIME-SERIES EXPERIMENTS;

TIME SERIES ANALYSIS;

REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SUGAR NUCLEOTIDE; URIDINE DIPHOSPHATE N ACETYLGLUCOSAMINE;

ARTICLE; CATALYST; CHROMATOGRAPHY; ENZYME ANALYSIS; ESCHERICHIA COLI; FLUOROMETRY; HELA CELL; NUCLEOTIDE SEQUENCE; OXIDATION; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE;

ESCHERICHIA COLI; METHANOCOCCUS MARIPALUDIS; SACCHAROMYCES CEREVISIAE;

EID: 49049114041     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2008.06.034     Document Type: Article

References (36)

1. In: Varki A., Cummings R., Esko J., Freeze H., Hart G., and Marth J. (Eds). Essentials of Glycobiology (1999), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
2. Zachara N.E., and Hart G.W. Cell signaling the essential role of O-GlcNAc. Biochim. Biophys. Acta 1761 (2006) 599-617
3. Mengin-Lecreulx D., Siegel E., and van Heijenoort J. Variations in UDP-N-acetylglucosamine and UDP-N-acetylmuramyl-pentapeptide pools in Escherichia coli after inhibition of protein synthesis. J. Bacteriol. 171 (1989) 3282-3287
4. Taylor R.P., Parker G.J., Hazel M.W., Soesanto Y., Fuller W., Yazzie M.J., and McClain D.A. Glucose deprivation stimulates O-GlcNAc modification of proteins through up-regulation of O-linked N-acetylglucosaminyltransferase. J. Biol. Chem. 283 (2008) 6050-6057
5. Räbinä J., Mäki M., Savilahti E.M., Järvinen N., Penttilä L., and Renkonen R. Analysis of nucleotide sugars from cell lysates by ion-pair solid-phase extraction and reversed-phase high-performance liquid chromatography. Glycoconj. J. 18 (2001) 799-805
6. Kochanowski N., Blanchard F., Cacan R., Chirat F., Guedon E., Marc A., and Goergen J.L. Intracellular nucleotide and nucleotide sugar contents of cultured CHO cells determined by a fast, sensitive, and high-resolution ion-pair RP-HPLC. Anal. Biochem. 348 (2006) 243-251
7. Tomiya N., Ailor E., Lawrence S.M., Betenbaugh M.J., and Lee Y.C. Determination of nucleotides and sugar nucleotides involved in protein glycosylation by high-performance anion-exchange chromatography: sugar nucleotide contents in cultured insect cells and mammalian cells. Anal. Biochem. 293 (2001) 129-137
8. Ritter J.B., Genzel Y., and Reichl U. High-performance anion-exchange chromatography using on-line electrolytic eluent generation for the determination of more than 25 intermediates from energy metabolism of mammalian cells in culture. J. Chromatogr. B 843 (2006) 216-226
9. Blake D.A., and Goldstein I.J. Resolution of nucleotide sugars and oligosaccharides by lectin affinity chromatography. Anal. Biochem. 102 (1980) 103-109
10. Turnock D.C., and Ferguson M.A.J. Sugar nucleotide pools of Trypanosoma brucei, Trypanosoma cruzi, and Leishmania major. Eukaryotic Cell 6 (2007) 1450-1463
11. Creuzenet C., Belanger M., Wakarchuk W.W., and Lam J.S. Expression, purification, and biochemical characterization of WbpP, a new UDP-GlcNAc C4 epimerase from Pseudomonas aeruginosa serotype O6. J. Biol. Chem. 275 (2000) 19060-19067
12. Sener K., Shen Z., Newburg D.S., and Jarroll E.L. Amino sugar phosphate levels in Giardia change during cyst wall formation. Microbiology 150 (2004) 1225-1230
13. Sweet C.R., Ribeiro A.A., and Raetz C.R.H. Oxidation and transamination of the 3′′-position of UDP-N-acetylglucosamine by enzymes from Acidithiobacillus ferrooxidans: role in the formation of lipid A molecules with four amide-linked acyl chains. J. Biol. Chem. 279 (2004) 25400-25410
14. Burrows L.L., Charter D.F., and Lam J.S. Molecular characterization of the Pseudomonas aeruginosa serotype O5 (PAO1) B-band lipopolysaccharide gene cluster. Mol. Microbiol. 22 (1996) 481-495
15. Westman E.L., McNally D.J., Rejzek M., Miller W.L., Kannathasan V.S., Preston A., Maskell D.J., Field R.A., Brisson J.-R., and Lam J.S. Identification and biochemical characterization of two novel UDP-2, 3-diacetamido-2, 3-dideoxy-α-d-glucuronic acid 2-epimerases from respiratory pathogens. Biochem. J. 405 (2007) 123-130
16. Melançon C.E., Yu W.-L., and Liu H.-W. TDP-mycaminose biosynthetic pathway revised and conversion of desosamine pathway to mycaminose pathway with one gene. J. Am. Chem. Soc. 127 (2005) 12240-12241
17. Namboori S.C., and Graham D.E. Acetamido sugar biosynthesis in the Euryarchaea. J. Bacteriol. 190 (2008) 2987-2996
18. Helgadóttir S., Rosas-Sandoval G., Söll D., and Graham D.E. Biosynthesis of phosphoserine in the Methanococcales. J. Bacteriol. 189 (2007) 575-582
19. Bader M. A systematic approach to standard addition methods in instrumental analysis. J. Chem. Educ. 57 (1980) 703-706
20. Zhang H., Zhou Y., Bao H., and Liu H.-W. Vi antigen biosynthesis in Salmonella typhi: characterization of UDP-N-acetylglucosamine C-6 dehydrogenase (TviB) and UDP-N-acetylglucosaminuronic acid C-4 epimerase (TviC). Biochemistry 45 (2006) 8163-8173
21. Chan S.Y., and Appling D.R. Regulation of S-adenosylmethionine levels in Saccharomyces cerevisiae. J. Biol. Chem. 278 (2003) 43051-43059
22. Miller W.L., Wenzel C.Q., Daniels C., Larocque S., Brisson J.-R., and Lam J.S. Biochemical characterization of WbpA, a UDP-N-acetyl-d-glucosamine 6-dehydrogenase involved in O-antigen biosynthesis in Pseudomonas aeruginosa PAO1. J. Biol. Chem. 279 (2004) 37551-37558
23. Müller T., and Schmidt R.R. Thymidine diphospho-6-deoxy-α-d-ribo-3-hexulose: synthesis of a central intermediate in the biosynthesis of di- and trideoxysugars. Angew. Chem. Intl. Ed. Engl. 34 (1995) 1328-1329
24. 2+-dependent phospho-α-glucosidase from Bacillus subtilis. Structure 12 (2004) 1619-1629
25. Roskoski R.J. Determination of pyridine nucleotides by fluorescence and other optical techniques. In: Dolphin D., Avramović O., and Poulson R. (Eds). Pyridine Nucleotide Coenzymes (1987), John Wiley, New York 173-188
26. Oppenheimer N.J. Chemical stability and reactivity of pyridine nucleotide coenzymes. In: Dolphin D., Avramović O., and Poulson R. (Eds). Pyridine Nucleotide Coenzymes (1987), John Wiley, New York 323-365
27. Neidhardt F.C. Chemical composition of Escherichia coli. In: Neidhardt F.C. (Ed). Escherichia coli and Salmonella typhimurium: cellular and Molecular Biology (1987), American Society for Microbiology, Washington, DC 3-6
28. Milewski S., Gabriel I., and Olchowy J. Enzymes of UDP-GlcNAc biosynthesis in yeast. Yeast 23 (2006) 1-14
29. Lesage G., and Bussey H. Cell wall assembly in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 70 (2006) 317-343
30. Bulik D.A., Olczak M., Lucero H.A., Osmond B.C., Robbins P.W., and Specht C.A. Chitin synthesis in Saccharomyces cerevisiae in response to supplementation of growth medium with glucosamine and cell wall stress. Eukaryotic Cell 2 (2003) 886-900
31. Sherman F. Getting started with yeast. Methods Enzymol. 350 (2002) 3-41
32. Wickson-Ginzburg M., and Solomon A.K. Electrolyte metabolism in HeLa cells. J. Gen. Physiol. 46 (1963) 1303-1315
33. Haltiwanger R.S., Grove K., and Philipsberg G.A. Modulation of O-linked N-acetylglucosamine levels on nuclear and cytoplasmic proteins in vivo using the peptide O-GlcNAc-β-N-acetylglucosaminidase inhibitor O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino-N-phenylcarbamate. J. Biol. Chem. 273 (1998) 3611-3617
34. Ritter J.B., Genzel Y., and Reichl U. Simultaneous extraction of several metabolites of energy metabolism and related substances in mammalian cells: optimization using experimental design. Anal. Biochem. 373 (2008) 349-369
35. Marshall S., Nadeau O., and Yamasaki K. Dynamic actions of glucose and glucosamine on hexosamine biosynthesis in isolated adipocytes. J. Biol. Chem. 279 (2004) 35313-35319
36. Michal G., Möllering H., and Siedel J. Chemical design of indicator reactions for the visible range. In: Bergmeyer H.U., et al. (Ed). Methods of Enzymatic Analysis (1983), Verlag Chemie, Weinheim, Germany 197-232