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Volumn 191, Issue 20, 2009, Pages 6401-6407

Allosteric regulation of glucosamine-6-phosphate deaminase (NagB) and growth of Escherichia coli on glucosamine

Author keywords

[No Author keywords available]

Indexed keywords

AMINOSUGAR; DEAMINASE; ESCHERICHIA COLI PROTEIN; GLUCOSAMINE; GLUCOSAMINE 6 PHOSPHATE DEAMINASE; PEPTIDOGLYCAN; UNCLASSIFIED DRUG;

EID: 70350445578     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00633-09     Document Type: Article
Times cited : (26)

References (33)
  • 1
    • 17644396319 scopus 로고    scopus 로고
    • 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
    • Álvarez-Añorve, L. I., M. Calcagno, and J. Plumbridge. 2005. 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. J. Bacteriol. 187:2974-2982.
    • (2005) J. Bacteriol. , vol.187 , pp. 2974-2982
    • Álvarez-Añorve, L.I.1    Calcagno, M.2    Plumbridge, J.3
  • 2
    • 0142070957 scopus 로고    scopus 로고
    • Two mammalian glucosamine-6-phosphate deaminases: A structural and genetic study
    • DOI 10.1016/S0014-5793(03)00896-2
    • Arreola, R., B. Valderrama, M. L. Morante, and E. Horjales. 2003. Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study. FEBS Lett. 551:63-70. (Pubitemid 37281329)
    • (2003) FEBS Letters , vol.551 , Issue.1-3 , pp. 63-70
    • Arreola, R.1    Valderrama, B.2    Morante, M.L.3    Horjales, E.4
  • 3
    • 0035887342 scopus 로고    scopus 로고
    • Allosteric transition and substrate binding are entropy driven in glucosamine-6-phosphate deaminase from Escherichia coli
    • Bustos-Jaimes, I., and M. Calcagno. 2001. Allosteric transition and substrate binding are entropy driven in glucosamine-6-phosphate deaminase from Escherichia coli. Arch. Biochem. Biophys. 394:156-160.
    • (2001) Arch. Biochem. Biophys. , vol.394 , pp. 156-160
    • Bustos-Jaimes, I.1    Calcagno, M.2
  • 4
    • 13444267354 scopus 로고    scopus 로고
    • Evidence for two different mechanisms triggering the change in quaternary structure of the allosteric enzyme, glucosamine-6-phosphate deaminase
    • DOI 10.1021/bi048514o
    • Bustos-Jaimes, I., M. Ramírez-Costa, L. D. Anda-Aguilar, P. Hinjosa-Ocaña, and M. Calcagno. 2005. Evidence for two different mechanisms triggering the change in quaternary structure of the allosteric enzyme, glucosamine-6-phosphate deaminase. Biochemistry 44:1127-1135. (Pubitemid 40208992)
    • (2005) Biochemistry , vol.44 , Issue.4 , pp. 1127-1135
    • Bustos-Jaimes, I.1    Ramirez-Costa, M.2    De Anda-Aguilar, L.3    Hinojosa-Ocana, P.4    Calcagno, M.L.5
  • 5
    • 0036301014 scopus 로고    scopus 로고
    • On the role of the conformational flexibility of the active site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase
    • Bustos-Jaimes, I., A. Sosa-Peinado, E. Rudiño-Piñera, E. Horjales, and M. L. Calcagno. 2002. On the role of the conformational flexibility of the active site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase. J. Mol. Biol. 319:183-189.
    • (2002) J. Mol. Biol. , vol.319 , pp. 183-189
    • Bustos-Jaimes, I.1    Sosa-Peinado, A.2    Rudiño-Piñera, E.3    Horjales, E.4    Calcagno, M.L.5
  • 6
    • 0021762288 scopus 로고
    • Purification, molecular and kinetic properties of glucosamine-6-phosphate isomerase (deaminase) from E. coli
    • Calcagno, M., P. J. Campos, G. Mulliert, and J. Suastegui. 1984. Purification, molecular and kinetic properties of glucosamine-6-phosphate isomerase (deaminase) from E. coli. Biochim. Biophys. Acta 787:165-173.
    • (1984) Biochim. Biophys. Acta , vol.787 , pp. 165-173
    • Calcagno, M.1    Campos, P.J.2    Mulliert, G.3    Suastegui, J.4
  • 7
    • 0034612342 scopus 로고    scopus 로고
    • One step inactivation of chromosomal genes in Escherichia coli K12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One step inactivation of chromosomal genes in Escherichia coli K12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 8
    • 0031983641 scopus 로고    scopus 로고
    • Negative transcriptional regulation of a positive regulator: The expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc
    • Decker, K., J. Plumbridge, and W. Boos. 1998. Negative transcriptional regulation of a positive regulator: the expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc. Mol. Microbiol. 27:381-390.
    • (1998) Mol. Microbiol. , vol.27 , pp. 381-390
    • Decker, K.1    Plumbridge, J.2    Boos, W.3
  • 9
    • 0014247957 scopus 로고
    • Effect of amino sugars on catabolite repression in Escherichia coli
    • Dobrogosz, W. J. 1968. Effect of amino sugars on catabolite repression in Escherichia coli. J. Bacteriol. 95:578-584.
    • (1968) J. Bacteriol. , vol.95 , pp. 578-584
    • Dobrogosz, W.J.1
  • 10
    • 34548317154 scopus 로고    scopus 로고
    • Feedback control of glucosamine-6-phosphate synthase GlmS expression depends on the small RNA GlmZ and involves the novel protein YhbJ in Escherichia coli
    • DOI 10.1111/j.1365-2958.2007.05888.x
    • Kalamorz, F., B. Reichenbach, W. Marz, B. Rak, and B. Görke. 2007. Feedback control of glucosamine-6-phosphate synthase GlmS expression depends on the small RNA and involves the novel protein YhbJ in Escherichia coli. Mol. Microbiol. 65:1518-1533. (Pubitemid 47347835)
    • (2007) Molecular Microbiology , vol.65 , Issue.6 , pp. 1518-1533
    • Kalamorz, F.1    Reichenbach, B.2    Marz, W.3    Rak, B.4    Gorke, B.5
  • 12
    • 78651189765 scopus 로고
    • On the nature of the allosteric transitions a plausible model
    • Monod, J., J. Wyman, and J. Changeux. 1965. On the nature of the allosteric transitions a plausible model. J. Mol. Biol. 12:88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.3
  • 13
    • 0035964293 scopus 로고    scopus 로고
    • 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., S. Lara-González, L. I. Álvarez-Añorve, J. A. Plumbridge, and M. L. Calcagno. 2001. On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase. Biochemistry 40:10187-10196.
    • (2001) Biochemistry , vol.40 , pp. 10187-10196
    • Montero-Morán, G.M.1    Lara-González, S.2    Álvarez- Añorve, L.I.3    Plumbridge, J.A.4    Calcagno, M.L.5
  • 14
    • 0027205157 scopus 로고
    • Molecular cloning and analysis of the NAG1 cDNA coding for glucosamine-6- Phosphate deaminase from Candida albicans
    • Natarajan, K., and A. Datta. 1993. Molecular cloning and analysis of the NAG1 cDNA coding for glucosamine-6-phosphate deaminase from Candida albicans. J. Biol. Chem. 268:9206-9214. (Pubitemid 23145962)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.13 , pp. 9206-9214
    • Natarajan, K.1    Datta, A.2
  • 15
    • 44949258242 scopus 로고    scopus 로고
    • How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)
    • Park, J. T., and T. Uehara. 2008. How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan). Microbiol. Mol. Biol. Rev. 72:211-227.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 211-227
    • Park, J.T.1    Uehara, T.2
  • 16
    • 37349036156 scopus 로고    scopus 로고
    • Different regions of Mlc and NagC, homologous transcriptional repressors controlling expression of the glucose and N-acetylglucosamine phosphotransferase systems in Escherichia coli, are required for inducer signal recognition
    • Pennetier, C., L. Domínguez-Ramírez, and J. Plumbridge. 2008. Different regions of Mlc and NagC, homologous transcriptional repressors controlling expression of the glucose and N-acetylglucosamine phosphotransferase systems in Escherichia coli, are required for inducer signal recognition. Mol. Microbiol. 67:364-377.
    • (2008) Mol. Microbiol. , vol.67 , pp. 364-377
    • Pennetier, C.1    Domínguez-Ramírez, L.2    Plumbridge, J.3
  • 17
    • 69949107818 scopus 로고    scopus 로고
    • An alternate route for recycling of N-acetylglucosamine from peptidoglycan involves the N-acetylglucosamine phosphotransferase system in E. coli
    • Plumbridge, J. 2009. An alternate route for recycling of N-acetylglucosamine from peptidoglycan involves the N-acetylglucosamine phosphotransferase system in E. coli. J. Bacteriol. 191:5641-5647.
    • (2009) J. Bacteriol. , vol.191 , pp. 5641-5647
    • Plumbridge, J.1
  • 18
    • 0029145921 scopus 로고
    • Co-ordinated regulation of aminosugar biosynthesis and degradation: The NagC repressor acts as an activator for the transcription of the glmUS operon and requires two separated NagC binding sites
    • Plumbridge, J. 1995. Co-ordinated regulation of aminosugar biosynthesis and degradation: the NagC repressor acts as an activator for the transcription of the glmUS operon and requires two separated NagC binding sites. EMBO J. 14:3958-3965.
    • (1995) EMBO J. , vol.14 , pp. 3958-3965
    • Plumbridge, J.1
  • 19
    • 0031973888 scopus 로고    scopus 로고
    • Control of the expression of the manXYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS
    • Plumbridge, J. 1998. Control of the expression of the manXYZ operon in Escherichia coli: Mlc is a negative regulator of the mannose PTS. Mol. Microbiol. 27:369-381.
    • (1998) Mol. Microbiol. , vol.27 , pp. 369-381
    • Plumbridge, J.1
  • 20
    • 0036217950 scopus 로고    scopus 로고
    • Regulation of gene expression in the PTS in Escherichia coli: The role and interactions of Mlc
    • Plumbridge, J. 2002. Regulation of gene expression in the PTS in Escherichia coli: the role and interactions of Mlc. Curr. Opin. Microbiol. 5:187-193.
    • (2002) Curr. Opin. Microbiol. , vol.5 , pp. 187-193
    • Plumbridge, J.1
  • 21
    • 0029913483 scopus 로고    scopus 로고
    • How to achieve constitutive expression of a gene within an inducible operon: The example of the nagC gene of Escherichia coli
    • Plumbridge, J. 1996. How to achieve constitutive expression of a gene within an inducible operon: the example of the nagC gene of Escherichia coli. J. Bacteriol. 178:2629-2636. (Pubitemid 26134488)
    • (1996) Journal of Bacteriology , vol.178 , Issue.9 , pp. 2629-2636
    • Plumbridge, J.1
  • 22
    • 0032929297 scopus 로고    scopus 로고
    • Convergent pathways for utilization of the amino sugars N- Acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by Escherichia coli
    • Plumbridge, J., and E. Vimr. 1999. Convergent pathways for utilization of the amino sugars N-acetylglucosamine, N-acetylmannosamine and N-acetylneuraminic acid by Escherichia coli. J. Bacteriol. 181:47-54. (Pubitemid 29013652)
    • (1999) Journal of Bacteriology , vol.181 , Issue.1 , pp. 47-54
    • Plumbridge, J.1    Vimr, E.2
  • 23
    • 0026563016 scopus 로고
    • A dominant mutation in the gene for the Nag repressor of Escherichia coli that renders the nag regulon uninducible
    • Plumbridge, J. A. 1992. A dominant mutation in the gene for the Nag repressor of Escherichia coli that renders the nag regulon uninducible. J. Gen. Microbiol. 138:1011-1017.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1011-1017
    • Plumbridge, J.A.1
  • 24
    • 0025278370 scopus 로고
    • 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. 1990. 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. J. Bacteriol. 172:2728-2735.
    • (1990) J. Bacteriol. , vol.172 , pp. 2728-2735
    • Plumbridge, J.A.1
  • 25
    • 0025816596 scopus 로고
    • Repression and induction of the nag regulon of Escherichia coli K12: The roles of nagC and nagA in maintenance of the uninduced state
    • Plumbridge, J. A. 1991. Repression and induction of the nag regulon of Escherichia coli K12: the roles of nagC and nagA in maintenance of the uninduced state. Mol. Microbiol. 5:2053-2062.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2053-2062
    • Plumbridge, J.A.1
  • 26
    • 0024469348 scopus 로고
    • Sequence of the nagBACD operon in Escherichia coli K12 and pattern of transcription within the nag regulon
    • Plumbridge, J. A. 1989. Sequence of the nagBACD operon in Escherichia coli K12 and pattern of transcription within the nag regulon. Mol. Microbiol. 3:506-515.
    • (1989) Mol. Microbiol. , vol.3 , pp. 506-515
    • Plumbridge, J.A.1
  • 27
    • 43349096395 scopus 로고    scopus 로고
    • The small RNA GlmY acts upstream of the sRNA GlmZ in the activation of glmS expression and is subject to regulation by polyadenylation in Escherichia coli
    • Reichenbach, B., A. Maes, F. Kalamorz, E. Hajnsdorf, and B. Görke. 2008. The small RNA GlmY acts upstream of the sRNA GlmZ in the activation of glmS expression and is subject to regulation by polyadenylation in Escherichia coli. Nucleic Acids Res. 36:2570-2580.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2570-2580
    • Reichenbach, B.1    Maes, A.2    Kalamorz, F.3    Hajnsdorf, E.4    Görke, B.5
  • 29
    • 0031569854 scopus 로고    scopus 로고
    • N-Acetyl-D-glucosamine-6-phosphate deacetylase from Escherichia coli: Purification and molecular and kinetic characterization
    • Souza, J.-M., J. A. Plumbridge, and M. L. Calcagno. 1997. N-Acetyl-D-glucosamine-6-phosphate deacetylase from Escherichia coli: purification and molecular and kinetic characterization. Arch. Biochem. Biophys. 340:338-346.
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 338-346
    • Souza, J.-M.1    Plumbridge, J.A.2    Calcagno, M.L.3
  • 30
    • 31544471658 scopus 로고    scopus 로고
    • Structure and activity analyses of Escherichia coli K-12 NagD provide insight into the evolution of biochemical function in the haloalkanoic acid dehalogenase superfamily
    • Tremblay, L., D. Dunaway-Mariano, and K. Allen. 2006. Structure and activity analyses of Escherichia coli K-12 NagD provide insight into the evolution of biochemical function in the haloalkanoic acid dehalogenase superfamily. Biochemistry 45:1183-1193.
    • (2006) Biochemistry , vol.45 , pp. 1183-1193
    • Tremblay, L.1    Dunaway-Mariano, D.2    Allen, K.3
  • 31
    • 41749124288 scopus 로고    scopus 로고
    • Two seemingly homologous noncoding RNAs act hierarchically to activate glmS mRNA translation
    • Urban, J., and J. Vogel. 2008. Two seemingly homologous noncoding RNAs act hierarchically to activate glmS mRNA translation. PLoS Biol. 6:e64.
    • (2008) PLoS Biol. , vol.6
    • Urban, J.1    Vogel, J.2
  • 32
    • 21244505806 scopus 로고    scopus 로고
    • Structure and kinetics of a monomeric glucosamine-6 phosphate deaminase. Missing link of the NagB superfamily?
    • Vincent, F., G. Davies, and J. Brannigan. 2005. Structure and kinetics of a monomeric glucosamine-6 phosphate deaminase. Missing link of the NagB superfamily? J. Biol. Chem. 280:19649-19655.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19649-19655
    • Vincent, F.1    Davies, G.2    Brannigan, J.3
  • 33
    • 0014251825 scopus 로고
    • Control of aminosugar metabolism in Escherichia coli and isolation of mutants unable to degrade amino sugars
    • White, R. J. 1968. Control of aminosugar metabolism in Escherichia coli and isolation of mutants unable to degrade amino sugars. Biochem. J. 106:847-858.
    • (1968) Biochem. J. , vol.106 , pp. 847-858
    • White, R.J.1


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