메뉴 건너뛰기




Volumn 416, Issue 2, 2011, Pages 152-158

A simple assay for 3-deoxy-D-manno-octulosonate cytidylyltransferase and its use as a pathway screen

Author keywords

3 Deoxy D manno octulosonate cytidylyltransferase (KdsB); 3 Deoxy D manno octulosonic acid (KDO); Inorganic phosphate determination; Pathway screen

Indexed keywords

BIOSYNTHESIS; ENZYMES;

EID: 80155147104     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2011.05.022     Document Type: Article
Times cited : (8)

References (23)
  • 1
    • 33845903833 scopus 로고    scopus 로고
    • Drugs for bad bugs: Confronting the challenges of antibacterial discovery
    • DOI 10.1038/nrd2201, PII NRD2201
    • D.J. Payne, M.N. Gwynn, D.J. Holmes, D.L. Pompliano, Drugs for bad bugs: confronting the challenges of antibacterial discovery, Nat. Rev. Drug Discov. 6 (2007) 29-40. (Pubitemid 46020284)
    • (2007) Nature Reviews Drug Discovery , vol.6 , Issue.1 , pp. 29-40
    • Payne, D.J.1    Gwynn, M.N.2    Holmes, D.J.3    Pompliano, D.L.4
  • 3
    • 33646037670 scopus 로고    scopus 로고
    • An in vitro screen of bacterial lipopolysaccharide biosynthetic enzymes identifies an inhibitor of ADP-heptose biosynthesis
    • G.P.D. Leon, N.H. Elowe, K.P. Koteva, M.A. Valvano, G.D. Wright,An in vitro screen of bacterial lipopolysaccharide biosynthetic enzymes identifies an inhibitor of ADP-heptose biosynthesis, Chem. Biol. Drug Des. 13 (2006) 437-441.
    • (2006) Chem. Biol. Drug Des. , vol.13 , pp. 437-441
    • Leon, G.P.D.1    Elowe, N.H.2    Koteva, K.P.3    Valvano, M.A.4    Wright, G.D.5
  • 4
    • 0035997382 scopus 로고    scopus 로고
    • Lipopolysaccharide endotoxins
    • DOI 10.1146/annurev.biochem.71.110601.135414
    • C.R.H. Raetz, C. Whitfield, Lipopolysaccharide endotoxins, Annu. Rev. Biochem. 71 (2002) 635-700. (Pubitemid 34800232)
    • (2002) Annual Review of Biochemistry , vol.71 , pp. 635-700
    • Raetz, C.R.H.1    Whitfield, C.2
  • 5
    • 0023273948 scopus 로고
    • Antibacterial agents specifically inhibiting lipopolysaccharide synthesis
    • DOI 10.1038/329162a0
    • R. Goldman, W. Kohlbrenner, P. Larty, A. Pernet, Antibacterial agents specifically inhibiting lipopolysaccharide biosynthesis, Nature 329 (1987) 162-164. (Pubitemid 17125253)
    • (1987) Nature , vol.329 , Issue.6135 , pp. 162-164
    • Goldman, R.1    Kohlbrenner, W.2    Lartey, P.3    Pernet, A.4
  • 6
    • 29244445498 scopus 로고    scopus 로고
    • A slow, tight-binding inhibitor of the zinc-dependent deacetylase LpxC of lipid a biosynthesis with antibiotic activity comparable to ciprofloxacin
    • DOI 10.1021/bi0518186
    • A.L. McClerren, S. Endsley, J.L. Bowman, N.H. Andersen, Z. Guan, J. Rudolph, C.R.H. Raetz, A slow, tight-binding inhibitor of the zinc-dependent deacetylase LpxC of lipid A biosynthesis with antibiotic activity comparable to ciprofloxacin, Biochemistry 44 (2005) 16574-16583. (Pubitemid 41832039)
    • (2005) Biochemistry , vol.44 , Issue.50 , pp. 16574-16583
    • McClerren, A.L.1    Endsley, S.2    Bowman, J.L.3    Andersen, N.H.4    Guan, Z.5    Rudolph, J.6    Raetz, C.R.H.7
  • 8
    • 27744480259 scopus 로고    scopus 로고
    • Moraxella catarrhalis bacterium without endotoxin, a potential vaccine candidate
    • DOI 10.1128/IAI.73.11.7569-7577.2005
    • D. Peng, W. Hong, B.P. Choudhury, R.W. Carlson, X.-X. Gu, Moraxella catarrhalis bacterium without endotoxin, a potential vaccine candidate, Infect. Immun. 73 (2005) 7569-7577. (Pubitemid 41587663)
    • (2005) Infection and Immunity , vol.73 , Issue.11 , pp. 7569-7577
    • Peng, D.1    Hong, W.2    Choudhury, B.P.3    Carlson, R.W.4    Gu, X.-X.5
  • 9
    • 0032473958 scopus 로고    scopus 로고
    • Meningitis bacterium is viable without endotoxin [7]
    • DOI 10.1038/33046
    • L. Steeghs, R. den Hartog, A. den Boer, B. Zomer, P. Roholl, P. van der Ley, Meningitis bacterium is viable without endotoxin, Nature 392 (1998) 449-450. (Pubitemid 28168969)
    • (1998) Nature , vol.392 , Issue.6675 , pp. 449-450
    • Steeghs, L.1    Den, H.R.2    Den, B.A.3    Zomer, B.4    Roholl, P.5    Van Der, L.P.6
  • 13
    • 0019510375 scopus 로고
    • Purification and characterization of cytidine 5'-triphosphate:cytidine 5'-monophosphate-3-deoxy-D-manno-octulosonate cytidylyltransferase
    • P.H. Ray, C.D. Benedict, H. Grasmuk, Purification and characterization of cytidine 50-triphosphate:cytidine 50-monophosphate-3-deoxy-D-mannooctulosonate cytidylyltransferase, J. Bacteriol. 145 (1981) 1273-1280. (Pubitemid 11097344)
    • (1981) Journal of Bacteriology , vol.145 , Issue.3 , pp. 1273-1280
    • Ray, P.H.1    Benedict, C.D.2    Grasmuk, H.3
  • 14
    • 77149152800 scopus 로고    scopus 로고
    • Implementation of anion-receptor macrocycles in supramolecular tandem assays for enzymes involving nucleotides as substrates, products, and cofactors
    • M. Florea, W.M. Nau, Implementation of anion-receptor macrocycles in supramolecular tandem assays for enzymes involving nucleotides as substrates, products, and cofactors, Org. Biomol. Chem. 8 (2010) 1033- 1039.
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 1033-1039
    • Florea, M.1    Nau, W.M.2
  • 15
    • 0041034107 scopus 로고
    • A colorimetric determination of inorganic pyrophosphate
    • R.M. Flynn, M.E. Jones, F. Lipmann, A colorimetric determination of inorganic pyrophosphate, J. Biol. Chem. 211 (1954) 791-796.
    • (1954) J. Biol. Chem. , vol.211 , pp. 791-796
    • Flynn, R.M.1    Jones, M.E.2    Lipmann, F.3
  • 16
    • 0016547933 scopus 로고
    • Colorimetric determination of inorganic pyrophosphate by a manual or automated method
    • R.F. Putnins, E.W. Yamada, Colorimetric determination of inorganic pyrophosphate by a manual or automated method, Anal. Biochem. 68 (1975) 185-195.
    • (1975) Anal. Biochem. , vol.68 , pp. 185-195
    • Putnins, R.F.1    Yamada, E.W.2
  • 17
    • 34247570886 scopus 로고    scopus 로고
    • A colorimetric assay method to measure acetyl-CoA synthetase activity: Application to woodchuck model of hepatitis virus-induced hepatocellular carcinoma
    • DOI 10.1016/j.jbbm.2007.02.008, PII S0165022X07000711
    • Y. Kuang, N. Salem, F. Wang, S.J. Schomisch, V. Chandramouli, Z. Lee, A colorimetric assay method to measure acetyl-CoA synthetase activity: Application to woodchuck model of hepatitis virus-induced hepatocellular carcinoma, J. Biochem. Biophys. Methods 70 (2007) 649-655. (Pubitemid 46669699)
    • (2007) Journal of Biochemical and Biophysical Methods , vol.70 , Issue.4 , pp. 649-655
    • Kuang, Y.1    Salem, N.2    Wang, F.3    Schomisch, S.J.4    Chandramouli, V.5    Lee, Z.6
  • 18
    • 0038719689 scopus 로고    scopus 로고
    • Escherichia coli YrbI is 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase
    • DOI 10.1074/jbc.M301983200
    • J. Wu, R.W. Woodard, Escherichia coli YrbI is 3-deoxy-D-manno- octulosonate 8-phosphate phosphatase, J. Biol. Chem. 278 (2003) 18117-18123. (Pubitemid 36799425)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.20 , pp. 18117-18123
    • Wu, J.1    Woodard, R.W.2
  • 19
    • 0037103781 scopus 로고    scopus 로고
    • Use of double-stranded RNA-mediated interference to determine the substrates of protein tyrosine kinases and phosphatases
    • M. Muda, C.A. Worby, N. Simonson-Leff, J.C. Clemens, J.E. Dixon, Use of double-stranded RNA-mediated interference to determine the substrates of protein tyrosine kinases and phosphatases, Biochem. J. 366 (2002) 73-78.
    • (2002) Biochem. J. , vol.366 , pp. 73-78
    • Muda, M.1    Worby, C.A.2    Simonson-Leff, N.3    Clemens, J.C.4    Dixon, J.E.5
  • 20
    • 0021803094 scopus 로고
    • Molecular cloning of the structural gene coding for CTP:CMP-3-deoxy- manno-octulosonate cytidylyltransferase from Escherichia coli K-12
    • R.C. Goldman, W.E. Kohlbrenner, Cloning of the structural gene coding for CTP:CMP-3-deoxy-manno-octulosonate cytidylyltransferase from Escherichia coli K-12, J. Bacteriol. 163 (1985) 256-261. (Pubitemid 15012745)
    • (1985) Journal of Bacteriology , vol.163 , Issue.1 , pp. 256-261
    • Goldman, R.C.1    Kohlbrenner, W.E.2
  • 21
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • DOI 10.1016/0003-2697(79)90115-5
    • P.A. Lanzetta, L.J. Alvarez, P.S. Reinach, O.A. Candia, An improved assay for nanomole amounts of inorganic phosphate, Anal. Biochem. 100 (1979) 95-97. (Pubitemid 10157636)
    • (1979) Analytical Biochemistry , vol.100 , Issue.1 , pp. 95-97
    • Lanzetta, P.A.1    Alvarez, L.J.2    Reinach, P.S.3    Candia, O.A.4
  • 22
    • 0030561461 scopus 로고    scopus 로고
    • A spectrophotometric method to measure enzymatic activity in reactions that generate inorganic pyrophosphate
    • DOI 10.1006/abio.1996.0479
    • R.H. Upson, R.P. Haugland, M.N. Malekzadeh, A spectrophotometric method to measure enzymic activity in reactions that generate inorganic pyrophosphate, Anal. Biochem. 243 (1996) 41-45. (Pubitemid 26418574)
    • (1996) Analytical Biochemistry , vol.243 , Issue.1 , pp. 41-45
    • Upson, R.H.1    Haugland, R.P.2    Malekzadeh, M.N.3    Haugland, R.P.4
  • 23
    • 0017171832 scopus 로고
    • A continuous spectrophotometric assay for argininosuccinate synthetase based on pyrophosphate formation
    • W.E. O'Brien, A continuous spectrophotometric assay for argininosuccinate synthetase based on pyrophosphate formation, Anal. Biochem. 76 (1976) 423-430.
    • (1976) Anal. Biochem. , vol.76 , pp. 423-430
    • O'Brien, W.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.