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Gene Review

nagB  -  glucosamine-6-phosphate deaminase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK0666, JW0664, glmD
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Disease relevance of nagB

  • The products of these nag genes were identified by complementation of E. coli strains with mutations in nagA, nagB, and nagE [1].

High impact information on nagB


Chemical compound and disease context of nagB


Biological context of nagB


Associations of nagB with chemical compounds


Analytical, diagnostic and therapeutic context of nagB


  1. Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli. Peri, K.G., Goldie, H., Waygood, E.B. Biochem. Cell Biol. (1990) [Pubmed]
  2. DNA bending and expression of the divergent nagE-B operons. Plumbridge, J., Kolb, A. Nucleic Acids Res. (1998) [Pubmed]
  3. On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase. Bustos-Jaimes, I., Sosa-Peinado, A., Rudiño-Piñera, E., Horjales, E., Calcagno, M.L. J. Mol. Biol. (2002) [Pubmed]
  4. Site-directed fluorescence labeling reveals differences on the R-conformer of glucosamine 6-phosphate deaminase of Escherichia coli induced by active or allosteric site ligands at steady state. Sosa-Peinado, A., González-Andrade, M. Biochemistry (2005) [Pubmed]
  5. On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase. Montero-Morán, G.M., Lara-González, S., Alvarez-Añorve, L.I., Plumbridge, J.A., Calcagno, M.L. Biochemistry (2001) [Pubmed]
  6. Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase. Rogers, M.J., Ohgi, T., Plumbridge, J., Söll, D. Gene (1988) [Pubmed]
  7. Identification of two cysteine residues forming a pair of vicinal thiols in glucosamine-6-phosphate deaminase from Escherichia coli and a study of their functional role by site-directed mutagenesis. Altamirano, M.M., Plumbridge, J.A., Calcagno, M.L. Biochemistry (1992) [Pubmed]
  8. Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution. Oliva, G., Fontes, M.R., Garratt, R.C., Altamirano, M.M., Calcagno, M.L., Horjales, E. Structure (1995) [Pubmed]
  9. Alternative route for biosynthesis of amino sugars in Escherichia coli K-12 mutants by means of a catabolic isomerase. Vogler, A.P., Trentmann, S., Lengeler, J.W. J. Bacteriol. (1989) [Pubmed]
  10. Why does Escherichia coli grow more slowly on glucosamine than on N-acetylglucosamine? Effects of enzyme levels and allosteric activation of GlcN6P deaminase (NagB) on growth rates. Alvarez-Añorve, L.I., Calcagno, M.L., Plumbridge, J. J. Bacteriol. (2005) [Pubmed]
  11. Cloning and sequencing of the genes for N-acetylglucosamine use that construct divergent operons (nagE-nagAC) from Vibrio cholerae non-O1. Yamano, N., Oura, N., Wang, J., Fujishima, S. Biosci. Biotechnol. Biochem. (1997) [Pubmed]
  12. CAP and Nag repressor binding to the regulatory regions of the nagE-B and manX genes of Escherichia coli. Plumbridge, J., Kolb, A. J. Mol. Biol. (1991) [Pubmed]
  13. Induction of the nag regulon of Escherichia coli by N-acetylglucosamine and glucosamine: role of the cyclic AMP-catabolite activator protein complex in expression of the regulon. Plumbridge, J.A. J. Bacteriol. (1990) [Pubmed]
  14. Crystallization and preliminary crystallographic studies of glucosamine-6-phosphate deaminase from Escherichia coli K12. Horjales, E., Altamirano, M.M., Calcagno, M.L., Dauter, Z., Wilson, K., Garratt, R.C., Oliva, G. J. Mol. Biol. (1992) [Pubmed]
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