Exploitation of structural and regulatory diversity in glutamate racemases

Nature

Volumn 447, Issue 7146, 2007, Pages 817-822

  Lundqvist, Tomas ^a   Fisher, Stewart L ^b   Kern, Gunther ^b   Folmer, Rutger H A ^a   Xue, Yafeng ^a   Newton, D Trevor ^b   Keating, Thomas A ^b   Alm, Richard A ^b   De Jonge, Boudewijn L M ^b  

^a ASTRAZENECA R AND D   (Sweden)

^b ASTRAZENECA   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ANTIINFECTIVE AGENT; BACTERIAL ENZYME; DEXTRO AMINO ACID AMINOTRANSFERASE; DEXTRO GLUTAMIC ACID; GLUTAMATE RACEMASE; PEPTIDOGLYCAN; UNCLASSIFIED DRUG;

BACTERIUM; BIOCHEMISTRY; ENZYME ACTIVITY; INHIBITION; INHIBITOR; SUBSTRATE;

ALLOSTERISM; ANTIMICROBIAL THERAPY; ARTICLE; BACILLUS SUBTILIS; BACTERIAL CELL WALL; BIOSYNTHESIS; CRYSTAL STRUCTURE; ENTEROCOCCUS FAECALIS; ENTEROCOCCUS FAECIUM; GENE MUTATION; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; HELICOBACTER PYLORI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; OLIGOMERIZATION; PRIORITY JOURNAL; STAPHYLOCOCCUS AUREUS;

BACTERIA (MICROORGANISMS); HELICOBACTER PYLORI;

EID: 34250356440     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05689     Document Type: Article

References (27)

1. van Heijenoort, J. Recent advances in the formation of the bacterial peptidoglycan monomer unit. Nat. Prod. Rep. 18, 503-519 (2001).
2. Tanner, M. E. & Miao, S. The synthesis and stability of aziridino-glutamate, an irreversible inhibitor of glutamate racemase. Tetrahedr. Lett. 35, 4073-4076 (1994).
3. Ashiuchi, M., Yoshimura, T., Esaki, N., Ueno, H. & Soda, K. Inactivation of glutamate racemase of Pediococcus pentosaceus with L-serine O-sulfate. Biosci. Biotechnol. Biochem. 57, 1978-1979 (1993).
4. de Dios, A. et al. 4-Substituted D-glutamic acid analogues: The first potent inhibitors of glutamate racemase (MurI) enzyme with antibacterial activity. J. Med. Chem. 45, 4559-4570 (2002).
5. Glavas, S. & Tanner, M. E. The inhibition of glutamate racemase by D-N-hydroxyglutamate. Bioorg. Med. Chem. Lett. 7, 2265-2270 (1997).
6. Newsholme, P., Procopio, J., Lima, M. M. R., Pithon-Curi, T. C. & Curi, R. Glutamine and glutamate - their central role in cell metabolism and function. Cell Biochem. Funct. 21, 1-9 (2003).
7. Doublet, P., van Heijenoort, J. & Mengin-Lecreulx, D. The glutamate racemase activity from Escherichia coli is regulated by peptidoglycan precursor UDP-N-acetylmuramoyl-L-alanine. Biochemistry 33, 5285-5290 (1994).
8. Ho, H.-T. et al. UDP-N-acetylmuramyl-L-alanine functions as an activator in the regulation of the Escherichia coli glutamate racemase activity. Biochemistry 34, 2464-2470 (1995).
9. Doublet, P., van Heijenoort, J. & Mengin-Lecreulx, D. Regulation of the glutamate racemase of Escherichia coli investigated by site-directed mutagenesis. Microb. Drug Resist. Mechanisms Epidemiol. Dis. 2, 43-49 (1996).
10. Fisher, L. M., Albery, W. J. & Knowles, J. R. Energetics of proline racemase: racemization of unlabeled proline in the unsaturated, saturated, and oversaturated regimes. Biochemistry 25, 2529-2537 (1986).
11. Mengin-Lecreulx, D., Flouret, B. & van Heijenoort, J. Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli. J. Bacteriol. 151, 1109-1117 (1982).
12. Fotheringham, I. G., Bledig, S. A. & Taylor, P. P. Characterization of the genes encoding D-amino acid transaminase and glutamate racemase, two D-glutamate biosynthetic enzymes of Bacillus sphaericus ATCC 10208. J. Bacteriol. 180, 4319-4323 (1998).
13. Pucci, M. J., Thanassi, J. A., Ho, H. T., Falk, P. J. & Dougherty, T. J. Staphylococcus haemolyticus contains two D-glutamic acid biosynthetic activities, a glutamate racemase and a D-amino acid transaminase. J. Bacteriol. 177, 336-342 (1995).
14. Song, J. H. et al. Identification of essential genes in Streptococcus pneumoniae by allelic replacement mutagenesis. Mol. Cells 19, 365-374 (2005).
15. Wang, L. & Zamudio, C. A method for predicting operons in prokaryotes. US patent number US2005/0026189A1 (2005).
16. Ruzheinikov, S. N. et al. Substrate-induced conformational changes in Bacillus subtilis glutamate racemase and their implications for drug discovery. Structure 13, 1707-1713 (2005).
17. Glavas, S. & Tanner, M. E. Active site residues of glutamate racemase. Biochemistry 40, 6199-6204 (2001).
18. Hwang, K. Y. et al. Structure and mechanism of glutamate racemase from Aquifex pyrophilus. Nature Struct. Biol. 6, 422-426 (1999).
19. McGovern, S. L., Helfand, B. T., Feng, B. & Shoichet, B. K. A specific mechanism of nonspecific inhibition. J. Med. Chem. 46, 4265-4272 (2003).
20. Seidler, J., McGovern, S. L., Doman, T. N. & Shoichet, B. K. Identification and prediction of promiscuous aggregating inhibitors among known drugs. J. Med. Chem. 46, 4477-4486 (2003).
21. Ghosh, N. K. & Fishman, W. H. On the mechanism of inhibition of intestinal alkaline phosphatase by L-phenylalanine. J. Biol. Chem. 241, 2516-2522 (1966).
22. Hardy, J. A. & Wells, J. A. Searching for new allosteric sites in enzymes. Curr. Opin. Struct. Biol. 14, 706-715 (2004).
23. Wiesmann, C. et al. Allosteric inhibition of protein tyrosine phosphatase 1B. Nature Struct. Mol. Biol. 11, 730-737 (2004).
24. Pargellis, C. et al. Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site. Nature Struct. Biol. 9, 268-272 (2002).
25. Oikonomakos, N. G., Skamnaki, V. T., Tsitsanou, K. E., Gavalas, N. G. & Johnson, L. N. A new allosteric site in glycogen phosphorylase b as a target for drug interactions. Struct. Fold. Des. 8, 575-584 (2000).
26. Hardy, J. A., Lam, J., Nguyen, J. T., O'Brien, T. & Wells, J. A. Discovery of an allosteric site in the caspases. Proc. Natl Acad. Sci. USA 101, 12461-12466 (2004).
27. Anderson, M. et al. Crystals of MurI from Gram negative, Gram positive, and atypical bacterium; computer-assisted method for screening, identifying, and designing inhibitors of MurI; inhibitors of MurI; and uses thereof. US patent number US2005/0037478 A1 (2005).