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Gene Review

guaA  -  GMP synthase

Escherichia coli O157:H7 str. Sakai

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Disease relevance of guaA


High impact information on guaA


Chemical compound and disease context of guaA


Biological context of guaA


Associations of guaA with chemical compounds


Other interactions of guaA


  1. Effects of xapA and guaA Disruption on Inosine Accumulation in Escherichia coli. Shimaoka, M., Takenaka, Y., Mihara, Y., Kurahashi, O., Kawasaki, H., Matsui, H. Biosci. Biotechnol. Biochem. (2006) [Pubmed]
  2. Characterization of LtsA from Rhodococcus erythropolis, an enzyme with glutamine amidotransferase activity. Mitani, Y., Meng, X., Kamagata, Y., Tamura, T. J. Bacteriol. (2005) [Pubmed]
  3. The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Tesmer, J.J., Klem, T.J., Deras, M.L., Davisson, V.J., Smith, J.L. Nat. Struct. Biol. (1996) [Pubmed]
  4. A new arrangement of (beta/alpha)8 barrels in the synthase subunit of PLP synthase. Zhu, J., Burgner, J.W., Harms, E., Belitsky, B.R., Smith, J.L. J. Biol. Chem. (2005) [Pubmed]
  5. Replacement by site-directed mutagenesis indicates a role for histidine 170 in the glutamine amide transfer function of anthranilate synthase. Amuro, N., Paluh, J.L., Zalkin, H. J. Biol. Chem. (1985) [Pubmed]
  6. Nucleotide sequence of the guaA gene encoding GMP synthetase of Escherichia coli K12. Tiedeman, A.A., Smith, J.M., Zalkin, H. J. Biol. Chem. (1985) [Pubmed]
  7. Crystal structure of Escherichia coli cytidine triphosphate synthetase, a nucleotide-regulated glutamine amidotransferase/ATP-dependent amidoligase fusion protein and homologue of anticancer and antiparasitic drug targets. Endrizzi, J.A., Kim, H., Anderson, P.M., Baldwin, E.P. Biochemistry (2004) [Pubmed]
  8. Expression of Escherichia coli pabA. Tran, P.V., Nichols, B.P. J. Bacteriol. (1991) [Pubmed]
  9. The C-terminal domain of HPII catalase is a member of the type I glutamine amidotransferase superfamily. Horvath, M.M., Grishin, N.V. Proteins (2001) [Pubmed]
  10. Combined, functional genomic-biochemical approach to intermediary metabolism: interaction of acivicin, a glutamine amidotransferase inhibitor, with Escherichia coli K-12. Smulski, D.R., Huang, L.L., McCluskey, M.P., Reeve, M.J., Vollmer, A.C., Van Dyk, T.K., LaRossa, R.A. J. Bacteriol. (2001) [Pubmed]
  11. Identification of a novel mycobacterial transcriptional regulator and its involvement in growth rate dependence and stringent control. Kamalakannan, V., Ramachandran, G., Narayanan, S., Vasan, S.K., Narayanan, P.R. FEMS Microbiol. Lett. (2002) [Pubmed]
  12. Characterization of the glutamine site of Escherichia coli guanosine 5'-monophosphate synthetase. Zalkin, H., Truitt, C.D. J. Biol. Chem. (1977) [Pubmed]
  13. Glutamine amidotransferase function. Replacement of the active-site cysteine in glutamine phosphoribosylpyrophosphate amidotransferase by site-directed mutagenesis. Mäntsälä, P., Zalkin, H. J. Biol. Chem. (1984) [Pubmed]
  14. Positional isotope exchange and kinetic experiments with Escherichia coli guanosine-5'-monophosphate synthetase. von der Saal, W., Crysler, C.S., Villafranca, J.J. Biochemistry (1985) [Pubmed]
  15. Guanosine monophosphate synthetase from Escherichia coli B-96. Inhibition by nucleosides. Spector, T., Beacham, L.M. J. Biol. Chem. (1975) [Pubmed]
  16. Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis. Klem, T.J., Davisson, V.J. Biochemistry (1993) [Pubmed]
  17. Structure of Escherichia coli aminodeoxychorismate synthase: architectural conservation and diversity in chorismate-utilizing enzymes. Parsons, J.F., Jensen, P.Y., Pachikara, A.S., Howard, A.J., Eisenstein, E., Ladner, J.E. Biochemistry (2002) [Pubmed]
  18. Enzymatic synthesis of guanine nucleotides labeled with 15N at the 2-amino group of the purine ring. Bouhss, A., Sakamoto, H., Palibroda, N., Chiriac, M., Sarfati, R., Smith, J.M., Craescu, C.T., Bârzu, O. Anal. Biochem. (1995) [Pubmed]
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