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Volumn 192, Issue 20, 2010, Pages 5506-5514

Characterization of the CDP-2-glycerol biosynthetic pathway in Streptococcus pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

1,3 DIHYDROXYACETONE; BACTERIAL ENZYME; GLYCERALDEHYDE REDUCTASE; GLYCEROL 2 PHOSPHATE; GLYCEROL 2 PHOSPHATE CYTIDYLYLTRANSFERASE; GLYCEROL 2 PHOSPHOTRANSFERASE; GUANOSINE TRIPHOSPHATE; GUANOSINE TRIPHOSPHATE 1; GUANOSINE TRIPHOSPHATE 3; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; CYTIDINE DIPHOSPHATE GLYCEROL; NUCLEOSIDE DIPHOSPHATE SUGAR;

EID: 77957836518     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00561-10     Document Type: Article
Times cited : (8)

References (24)
  • 1
    • 35648988999 scopus 로고    scopus 로고
    • Predicted functions and linkage specificities of the products of the Streptococcus pneumoniae capsular biosynthetic loci
    • Aanensen, D. M., A. Mavroidi, S. D. Bentley, P. R. Reeves, and B. G. Spratt. 2007. Predicted functions and linkage specificities of the products of the Streptococcus pneumoniae capsular biosynthetic loci. J. Bacteriol. 189:7856-7876.
    • (2007) J. Bacteriol. , vol.189 , pp. 7856-7876
    • Aanensen, D.M.1    Mavroidi, A.2    Bentley, S.D.3    Reeves, P.R.4    Spratt, B.G.5
  • 2
    • 0028863854 scopus 로고
    • Streptococcus pneumoniae: Virulence factors, pathogenesis, and vaccines
    • Alonso De Velasco, E., A. Verheul, J. Verhoef, and H. Snippe. 1995. Streptococcus pneumoniae: virulence factors, pathogenesis, and vaccines. Microbiol. Rev. 59:591-603.
    • (1995) Microbiol. Rev. , vol.59 , pp. 591-603
    • Alonso De Velasco, E.1    Verheul, A.2    Verhoef, J.3    Snippe, H.4
  • 3
    • 0344699119 scopus 로고
    • A glycerol dehydrogenase from Escherichia coli
    • Asnis, R. E., and A. F. Brodie. 1953. A glycerol dehydrogenase from Escherichia coli. J. Biol. Chem. 203:153-159.
    • (1953) J. Biol. Chem. , vol.203 , pp. 153-159
    • Asnis, R.E.1    Brodie, A.F.2
  • 5
    • 33746922036 scopus 로고    scopus 로고
    • Evolutionary genomics of the HAD superfamily: Understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes
    • Burroughs, A. M., K. N. Allen, D. Dunaway-Mariano, and L. Aravind. 2006. Evolutionary genomics of the HAD superfamily: understanding the structural adaptations and catalytic diversity in a superfamily of phosphoesterases and allied enzymes. J. Mol. Biol. 361:1003-1034.
    • (2006) J. Mol. Biol. , vol.361 , pp. 1003-1034
    • Burroughs, A.M.1    Allen, K.N.2    Dunaway-Mariano, D.3    Aravind, L.4
  • 6
    • 36348973023 scopus 로고    scopus 로고
    • Calmodulin binds and stabilizes the regulatory enzyme, CTP: Phosphocholine cytidylyltransferase
    • Chen, B. B., and R. K. Mallampalli. 2007. Calmodulin binds and stabilizes the regulatory enzyme, CTP: phosphocholine cytidylyltransferase. J. Biol. Chem. 282:33494-33506.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33494-33506
    • Chen, B.B.1    Mallampalli, R.K.2
  • 7
    • 0036942348 scopus 로고    scopus 로고
    • Analysis of membrane stereochemistry with homology modeling of sn-glycerol-1-phosphate dehydrogenase
    • Daiyasu, H., T. Hiroike, Y. Koga, and H. Toh. 2002. Analysis of membrane stereochemistry with homology modeling of sn-glycerol-1-phosphate dehydrogenase. Protein Eng. 15:987-995.
    • (2002) Protein Eng. , vol.15 , pp. 987-995
    • Daiyasu, H.1    Hiroike, T.2    Koga, Y.3    Toh, H.4
  • 9
    • 0029150941 scopus 로고
    • Six newly recognized types of Streptococcus pneumoniae
    • Henrichsen, J. 1995. Six newly recognized types of Streptococcus pneumoniae. J. Clin. Microbiol. 33:2759-2762.
    • (1995) J. Clin. Microbiol. , vol.33 , pp. 2759-2762
    • Henrichsen, J.1
  • 10
    • 0029786674 scopus 로고    scopus 로고
    • Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold
    • Hisano, T., Y. Hata, T. Fujii, J. Q. Liu, T. Kurihara, N. Esaki, and K. Soda. 1996. Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold. J. Biol. Chem. 271:20322-20330.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20322-20330
    • Hisano, T.1    Hata, Y.2    Fujii, T.3    Liu, J.Q.4    Kurihara, T.5    Esaki, N.6    Soda, K.7
  • 11
    • 0037008092 scopus 로고    scopus 로고
    • Caught in the act: The structure of phosphorylated beta- phosphoglucomutase from Lactococcus lactis
    • Lahiri, S. D., G. Zhang, D. Dunaway-Mariano, and K. N. Allen. 2002. Caught in the act: the structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis. Biochemistry 41:8351-8359.
    • (2002) Biochemistry , vol.41 , pp. 8351-8359
    • Lahiri, S.D.1    Zhang, G.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 12
    • 0028049079 scopus 로고
    • Purification, characterization, and high performance liquid chromatography assay of Salmonella glucose-1-phosphate cytidylyltransferase from the cloned rfbF gene
    • Lindqvist, L., R. Kaiser, P. R. Reeves, and A. A. Lindberg. 1994. Purification, characterization, and high performance liquid chromatography assay of Salmonella glucose-1-phosphate cytidylyltransferase from the cloned rfbF gene. J. Biol. Chem. 269:122-126.
    • (1994) J. Biol. Chem. , vol.269 , pp. 122-126
    • Lindqvist, L.1    Kaiser, R.2    Reeves, P.R.3    Lindberg, A.A.4
  • 13
    • 0034730072 scopus 로고    scopus 로고
    • The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: Insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily
    • Morais, M. C., W. Zhang, A. S. Baker, G. Zhang, D. Dunaway-Mariano, and K. N. Allen. 2000. The crystal structure of bacillus cereus phosphonoacetaldehyde hydrolase: insight into catalysis of phosphorus bond cleavage and catalytic diversification within the HAD enzyme superfamily. Biochemistry 39:10385-10396.
    • (2000) Biochemistry , vol.39 , pp. 10385-10396
    • Morais, M.C.1    Zhang, W.2    Baker, A.S.3    Zhang, G.4    Dunaway-Mariano, D.5    Allen, K.N.6
  • 14
    • 0032901263 scopus 로고    scopus 로고
    • Molecular and genetic characterization of the capsule biosynthesis locus of Streptococcus pneumoniae type 23F
    • Morona, J. K., D. C. Miller, T. J. Coffey, C. J. Vindurampulle, B. G. Spratt, R. Morona, and J. C. Paton. 1999. Molecular and genetic characterization of the capsule biosynthesis locus of Streptococcus pneumoniae type 23F. Microbiology 145:781-789.
    • (1999) Microbiology , vol.145 , pp. 781-789
    • Morona, J.K.1    Miller, D.C.2    Coffey, T.J.3    Vindurampulle, C.J.4    Spratt, B.G.5    Morona, R.6    Paton, J.C.7
  • 15
    • 0027185240 scopus 로고
    • Expression, purification, and characterization of CTP: Glycerol-3-phosphate cytidylytransferase from Bacillus subtilis
    • Park, Y. S., T. D. Sweitzer, J. E. Dixon, and C. Kent. 1993. Expression, purification, and characterization of CTP: glycerol-3-phosphate cytidylytransferase from Bacillus subtilis. J. Biol. Chem. 268:16648-16654.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16648-16654
    • Park, Y.S.1    Sweitzer, T.D.2    Dixon, J.E.3    Kent, C.4
  • 16
    • 0346434164 scopus 로고    scopus 로고
    • Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis
    • Pattridge, K. A., C. H. Weber, J. A. Friesen, S. Sanker, C. Kent, and M. L. Ludwig. 2003. Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis. J. Biol. Chem. 278:51863-51871.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51863-51871
    • Pattridge, K.A.1    Weber, C.H.2    Friesen, J.A.3    Sanker, S.4    Kent, C.5    Ludwig, M.L.6
  • 17
    • 4944254297 scopus 로고    scopus 로고
    • X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily
    • Peisach, E., J. D. Selengut, D. Dunaway-Mariano, and K. N. Allen. 2004. X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily. Biochemistry 43:12770-12779.
    • (2004) Biochemistry , vol.43 , pp. 12770-12779
    • Peisach, E.1    Selengut, J.D.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 20
    • 34547629796 scopus 로고    scopus 로고
    • Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol: Inositol-1-phosphate transferase, the key enzyme for di-myo-inositolphosphate synthesis in several (hyper)thermophiles
    • Rodrigues, M. V., N. Borges, M. Henriques, P. Lamosa, R. Ventura, C. Fernandes, N. Empadinhas, C. Maycock, M. S. da Costa, and H. Santos. 2007. Bifunctional CTP:inositol-1-phosphate cytidylyltransferase/CDP-inositol: inositol-1-phosphate transferase, the key enzyme for di-myo-inositolphosphate synthesis in several (hyper)thermophiles. J. Bacteriol. 189:5405-5412.
    • (2007) J. Bacteriol. , vol.189 , pp. 5405-5412
    • Rodrigues, M.V.1    Borges, N.2    Henriques, M.3    Lamosa, P.4    Ventura, R.5    Fernandes, C.6    Empadinhas, N.7    Maycock, C.8    Da Costa, M.S.9    Santos, H.10
  • 21
    • 26644470345 scopus 로고    scopus 로고
    • Mutagenesis of glycine 179 modulates both catalytic efficiency and reduced pyridine nucleotide specificity in cytochrome b5 reductase
    • Roma, G. W., L. J. Crowley, C. A. Davis, and M. J. Barber. 2005. Mutagenesis of glycine 179 modulates both catalytic efficiency and reduced pyridine nucleotide specificity in cytochrome b5 reductase. Biochemistry 44:13467-13476.
    • (2005) Biochemistry , vol.44 , pp. 13467-13476
    • Roma, G.W.1    Crowley, L.J.2    Davis, C.A.3    Barber, M.J.4
  • 22
    • 0028293665 scopus 로고
    • Cloning, sequencing, and overexpression in Escherichia coli of the alpha-D-glucose-1-phosphate cytidylyltransferase gene isolated from Yersinia pseudotuberculosis
    • Thorson, J. S., T. M. Kelly, and H. W. Liu. 1994. Cloning, sequencing, and overexpression in Escherichia coli of the alpha-D-glucose-1-phosphate cytidylyltransferase gene isolated from Yersinia pseudotuberculosis. J. Bacteriol. 176:1840-1849.
    • (1994) J. Bacteriol. , vol.176 , pp. 1840-1849
    • Thorson, J.S.1    Kelly, T.M.2    Liu, H.W.3
  • 23
    • 56749151152 scopus 로고    scopus 로고
    • Characterization of the dTDP-D-fucofuranose biosynthetic pathway in Escherichia coli O52
    • Wang, Q., P. Ding, A. V. Perepelov, Y. Xu, Y. Wang, Y. A. Knirel, L. Wang, and L. Feng. 2008. Characterization of the dTDP-D-fucofuranose biosynthetic pathway in Escherichia coli O52. Mol. Microbiol. 70:1358-1367.
    • (2008) Mol. Microbiol. , vol.70 , pp. 1358-1367
    • Wang, Q.1    Ding, P.2    Perepelov, A.V.3    Xu, Y.4    Wang, Y.5    Knirel, Y.A.6    Wang, L.7    Feng, L.8
  • 24
    • 0033546181 scopus 로고    scopus 로고
    • A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucose
    • Yoshida, Y., Y. Nakano, T. Nezu, Y. Yamashita, and T. Koga. 1999. A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucose. J. Biol. Chem. 274:16933-16939.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16933-16939
    • Yoshida, Y.1    Nakano, Y.2    Nezu, T.3    Yamashita, Y.4    Koga, T.5


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