메뉴 건너뛰기




Volumn 191, Issue 14, 2009, Pages 4667-4670

Uptake of glycerol-2-phosphate via the ugp-encoded transporter in Escherichia coli K-12

Author keywords

[No Author keywords available]

Indexed keywords

GLYCEROL 2 PHOSPHATE; PHOSPHORUS; CARRIER PROTEIN; ESCHERICHIA COLI PROTEIN; GLYCEROPHOSPHATE;

EID: 67650318512     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00235-09     Document Type: Article
Times cited : (20)

References (21)
  • 1
    • 0035810954 scopus 로고    scopus 로고
    • High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter
    • Auer, M., M. J. Kim, M. J. Lemieux, A. Villa, J. Song, X. D. Li, and D. N. Wang. 2001. High-yield expression and functional analysis of Escherichia coli glycerol-3-phosphate transporter. Biochemistry 40:6628-6635.
    • (2001) Biochemistry , vol.40 , pp. 6628-6635
    • Auer, M.1    Kim, M.J.2    Lemieux, M.J.3    Villa, A.4    Song, J.5    Li, X.D.6    Wang, D.N.7
  • 2
    • 0024076898 scopus 로고
    • Characteristics of a ugp-encoded and phoBdependent glycerophosphoryl diester phosphodiesterase which is physically dependent on the ugp transport system of Escherichia coli
    • Brzoska, P., and W. Boos. 1988. Characteristics of a ugp-encoded and phoBdependent glycerophosphoryl diester phosphodiesterase which is physically dependent on the ugp transport system of Escherichia coli. J. Bacteriol. 170:4125-4135.
    • (1988) J. Bacteriol , vol.170 , pp. 4125-4135
    • Brzoska, P.1    Boos, W.2
  • 4
    • 0026773209 scopus 로고
    • Structure and mechanism of alkaline phosphatase
    • Coleman, J. E. 1992. Structure and mechanism of alkaline phosphatase. Annu. Rev. Biophys. Biomol. Struct. 21:441-483.
    • (1992) Annu. Rev. Biophys. Biomol. Struct , vol.21 , pp. 441-483
    • Coleman, J.E.1
  • 5
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 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
  • 6
    • 0001385085 scopus 로고
    • Active transport of L-α-glycerophosphate in Escherichia coli
    • Hayashi, S., J. P. Koch, and E. C. Lin. 1964. Active transport of L-α-glycerophosphate in Escherichia coli. J. Biol. Chem. 239:3098-3105.
    • (1964) J. Biol. Chem , vol.239 , pp. 3098-3105
    • Hayashi, S.1    Koch, J.P.2    Lin, E.C.3
  • 7
    • 13244278165 scopus 로고    scopus 로고
    • Full NMR assignment and revised structure for the capsular polysaccharide from Streptococcus pneumoniae type 15B
    • Jones, C., and X. Lemercinier. 2005. Full NMR assignment and revised structure for the capsular polysaccharide from Streptococcus pneumoniae type 15B. Carbohydr. Res. 340:403-409.
    • (2005) Carbohydr. Res , vol.340 , pp. 403-409
    • Jones, C.1    Lemercinier, X.2
  • 8
    • 0026716412 scopus 로고
    • Evidence for two phosphonate degradative pathways in Enterobacter aerogenes
    • Lee, K. S., W. W. Metcalf, and B. L. Wanner. 1992. Evidence for two phosphonate degradative pathways in Enterobacter aerogenes. J. Bacteriol. 174:2501-2510.
    • (1992) J. Bacteriol , vol.174 , pp. 2501-2510
    • Lee, K.S.1    Metcalf, W.W.2    Wanner, B.L.3
  • 9
    • 67650751662 scopus 로고
    • Genetic and chemical studies with alkaline phosphatase of E
    • Levinthal, C. 1959. Genetic and chemical studies with alkaline phosphatase of E. coli. Brookhaven Symp. Biol. 12:76-85.
    • (1959) coli. Brookhaven Symp. Biol , vol.12 , pp. 76-85
    • Levinthal, C.1
  • 10
    • 0026067796 scopus 로고
    • Involvement of the Escherichia coli phn (psiD) gene cluster in assimilation of phosphorus in the form of phosphonates, phosphite, Pi esters, and Pi
    • Metcalf, W. W., and B. L. Wanner. 1991. Involvement of the Escherichia coli phn (psiD) gene cluster in assimilation of phosphorus in the form of phosphonates, phosphite, Pi esters, and Pi. J. Bacteriol. 173:587-600.
    • (1991) J. Bacteriol , vol.173 , pp. 587-600
    • Metcalf, W.W.1    Wanner, B.L.2
  • 11
    • 0019497196 scopus 로고
    • Deletion map of the Escherichia coli structural gene for alkaline phosphatase, phoA
    • Sarthy, A., S. Michaelis, and J. Beckwith. 1981. Deletion map of the Escherichia coli structural gene for alkaline phosphatase, phoA. J. Bacteriol. 145:288-292.
    • (1981) J. Bacteriol , vol.145 , pp. 288-292
    • Sarthy, A.1    Michaelis, S.2    Beckwith, J.3
  • 12
    • 0021059964 scopus 로고
    • Cloning of the ugp region containing the structural genes for the pho regulon-dependent sn-glycerol-3-phosphate transport system of Escherichia coli
    • Schweizer, H., and W. Boos. 1983. Cloning of the ugp region containing the structural genes for the pho regulon-dependent sn-glycerol-3-phosphate transport system of Escherichia coli. Mol. Gen. Genet. 192:177-186.
    • (1983) Mol. Gen. Genet , vol.192 , pp. 177-186
    • Schweizer, H.1    Boos, W.2
  • 13
    • 0023141781 scopus 로고
    • Cloning and characterization of the aerobic sn-glycerol-3-phosphate dehydrogenase structural gene glpD of Escherichia coli K-12
    • Schweizer, H., and T. J. Larson. 1987. Cloning and characterization of the aerobic sn-glycerol-3-phosphate dehydrogenase structural gene glpD of Escherichia coli K-12. J. Bacteriol. 169:507-513.
    • (1987) J. Bacteriol , vol.169 , pp. 507-513
    • Schweizer, H.1    Larson, T.J.2
  • 14
    • 73049145025 scopus 로고
    • Mutants of Escherichia coli constitutive for alkaline phosphatase
    • Torriani, A., and F. Rothman. 1961. Mutants of Escherichia coli constitutive for alkaline phosphatase. J. Bacteriol. 81:835-836.
    • (1961) J. Bacteriol , vol.81 , pp. 835-836
    • Torriani, A.1    Rothman, F.2
  • 15
    • 0027411096 scopus 로고
    • Gene regulation by phosphate in enteric bacteria
    • Wanner, B. L. 1993. Gene regulation by phosphate in enteric bacteria. J. Cell Biochem. 51:47-54.
    • (1993) J. Cell Biochem , vol.51 , pp. 47-54
    • Wanner, B.L.1
  • 16
    • 0020595079 scopus 로고
    • Overlapping and separate controls on the phosphate regulon in Escherichia coli K12
    • Wanner, B. L. 1983. Overlapping and separate controls on the phosphate regulon in Escherichia coli K12. J. Mol. Biol. 166:283-308.
    • (1983) J. Mol. Biol , vol.166 , pp. 283-308
    • Wanner, B.L.1
  • 17
    • 67650730338 scopus 로고    scopus 로고
    • Wanner, B. L. 1996. Phosphorus assimilation and control of the phosphate regulon, p. 1357-1381. In F. C. Neidhardt, R. Curtiss, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., I. ASM Press, Washington, DC.
    • Wanner, B. L. 1996. Phosphorus assimilation and control of the phosphate regulon, p. 1357-1381. In F. C. Neidhardt, R. Curtiss, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed., vol. I. ASM Press, Washington, DC.
  • 18
    • 0019970038 scopus 로고
    • Phosphate-controlled gene expression in Escherichia coli K12 using Mudl-directed lacZ fusions
    • Wanner, B. L., and R. McSharry. 1982. Phosphate-controlled gene expression in Escherichia coli K12 using Mudl-directed lacZ fusions. J. Mol. Biol. 158:347-363.
    • (1982) J. Mol. Biol , vol.158 , pp. 347-363
    • Wanner, B.L.1    McSharry, R.2
  • 19
    • 35848942616 scopus 로고    scopus 로고
    • Microbial metabolism of reduced phosphorus compounds
    • White, A. K., and W. W. Metcalf. 2007. Microbial metabolism of reduced phosphorus compounds. Annu. Rev. Microbiol. 61:379-400.
    • (2007) Annu. Rev. Microbiol , vol.61 , pp. 379-400
    • White, A.K.1    Metcalf, W.W.2
  • 20
    • 0031859636 scopus 로고    scopus 로고
    • Phosphate-independent expression of the carbon-phosphorus lyase activity of Escherichia coli
    • Yakovleva, G. M., S. K. Kim, and B. L. Wanner. 1998. Phosphate-independent expression of the carbon-phosphorus lyase activity of Escherichia coli. Appl. Microbiol. Biotechnol. 49:573-578.
    • (1998) Appl. Microbiol. Biotechnol , vol.49 , pp. 573-578
    • Yakovleva, G.M.1    Kim, S.K.2    Wanner, B.L.3
  • 21
    • 2542529286 scopus 로고    scopus 로고
    • A new activity for an old enzyme: Escherichia coli bacterial alkaline phosphatase is a phosphite-dependent hydrogenase
    • Yang, K. C., and W. W. Metcalf. 2004. A new activity for an old enzyme: Escherichia coli bacterial alkaline phosphatase is a phosphite-dependent hydrogenase. Proc. Natl. Acad. Sci. USA 101:7919- 7924.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7919-7924
    • Yang, K.C.1    Metcalf, W.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.