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Chemical Compound Review

UNAGEP     2-[(2R,3R,4R,5R,6R)-3- acetamido-2-[[[(2R...

Synonyms: EP-UDPGlCNAC, CHEBI:68507, AC1L593J, C04631, 70222-94-5, ...
 
 
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Disease relevance of Udp-N-acetylglucosamine-enolpyruvate

 

High impact information on Udp-N-acetylglucosamine-enolpyruvate

 

Biological context of Udp-N-acetylglucosamine-enolpyruvate

 

Analytical, diagnostic and therapeutic context of Udp-N-acetylglucosamine-enolpyruvate

References

  1. Identification and characterization of amino acid residues essential for the active site of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from Staphylococcus aureus. Nishida, S., Kurokawa, K., Matsuo, M., Sakamoto, K., Ueno, K., Kita, K., Sekimizu, K. J. Biol. Chem. (2006) [Pubmed]
  2. Spectroscopic properties of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase. Axley, M.J., Fairman, R., Yanchunas, J., Villafranca, J.J., Robertson, J.G. Biochemistry (1997) [Pubmed]
  3. Identification and characterization of UDP-N-acetylenolpyruvylglucosamine reductase (MurB) from the Gram-positive pathogen Streptococcus pneumoniae. Sylvester, D.R., Alvarez, E., Patel, A., Ratnam, K., Kallender, H., Wallis, N.G. Biochem. J. (2001) [Pubmed]
  4. 3,5-dioxopyrazolidines, novel inhibitors of UDP-N- acetylenolpyruvylglucosamine reductase (MurB) with activity against gram-positive bacteria. Yang, Y., Severin, A., Chopra, R., Krishnamurthy, G., Singh, G., Hu, W., Keeney, D., Svenson, K., Petersen, P.J., Labthavikul, P., Shlaes, D.M., Rasmussen, B.A., Failli, A.A., Shumsky, J.S., Kutterer, K.M., Gilbert, A., Mansour, T.S. Antimicrob. Agents Chemother. (2006) [Pubmed]
  5. A structural variation for MurB: X-ray crystal structure of Staphylococcus aureus UDP-N-acetylenolpyruvylglucosamine reductase (MurB). Benson, T.E., Harris, M.S., Choi, G.H., Cialdella, J.I., Herberg, J.T., Martin, J.P., Baldwin, E.T. Biochemistry (2001) [Pubmed]
  6. Characterization of NADP+ binding to perdeuterated MurB: backbone atom NMR assignments and chemical-shift changes. Constantine, K.L., Mueller, L., Goldfarb, V., Wittekind, M., Metzler, W.J., Yanchunas, J., Robertson, J.G., Malley, M.F., Friedrichs, M.S., Farmer, B.T. J. Mol. Biol. (1997) [Pubmed]
  7. Overexpression, purification, and mechanistic study of UDP-N-acetylenolpyruvylglucosamine reductase. Benson, T.E., Marquardt, J.L., Marquardt, A.C., Etzkorn, F.A., Walsh, C.T. Biochemistry (1993) [Pubmed]
  8. Pool levels of UDP N-acetylglucosamine and UDP N-acetylglucosamine-enolpyruvate in Escherichia coli and correlation with peptidoglycan synthesis. Mengin-Lecreulx, D., Flouret, B., van Heijenoort, J. J. Bacteriol. (1983) [Pubmed]
  9. Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release. Eschenburg, S., Priestman, M., Schönbrunn, E. J. Biol. Chem. (2005) [Pubmed]
  10. Crystallization and preliminary X-ray crystallographic studies of UDP-N-acetylenolpyruvylglucosamine reductase. Benson, T.E., Walsh, C.T., Hogle, J.M. Protein Sci. (1994) [Pubmed]
 
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