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Volumn 100, Issue 20, 2009, Pages 4848-4853

Effect of NH4+ and glycerol on cytidine 5′-diphosphocholine synthesis in Saccharomyces cerevisiae

Author keywords

Ammonium ion; Cytidine diphosphate choline; Glycerol; Saccharomyces cerevisiae; Utilization efficiency of energy

Indexed keywords

AMMONIUM ION; AMMONIUM IONS; CDP-CHOLINE; CENTRAL COMPOSITE DESIGNS; CHOLINE CHLORIDE; CYTIDINE; CYTIDINE DIPHOSPHATE CHOLINE; DIPHOSPHATE; GLYCOLYTIC FLUX; KEY ENZYMES; S.CEREVISIAE; SACCHAROMYCES CEREVISIAE; UTILIZATION EFFICIENCY; UTILIZATION EFFICIENCY OF ENERGY;

EID: 67649197376     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2009.04.045     Document Type: Article
Times cited : (15)

References (28)
  • 1
    • 34547925606 scopus 로고    scopus 로고
    • Role of lipids in brain injury and diseases
    • Adibhatla R.M., and Hatcher J.F. Role of lipids in brain injury and diseases. Future Lipidol. 2 (2007) 403-422
    • (2007) Future Lipidol. , vol.2 , pp. 403-422
    • Adibhatla, R.M.1    Hatcher, J.F.2
  • 2
    • 0030600132 scopus 로고    scopus 로고
    • The allosteric regulation of pyruvate kinase
    • Andrea M., Martino B., and Giovanna V. The allosteric regulation of pyruvate kinase. FEBS Lett. 389 (1996) 15-19
    • (1996) FEBS Lett. , vol.389 , pp. 15-19
    • Andrea, M.1    Martino, B.2    Giovanna, V.3
  • 3
    • 0025732448 scopus 로고
    • Protein-solvent interactions in pharmaceutical formulations
    • Arakawa T., Kita Y., and Carpenter J.F. Protein-solvent interactions in pharmaceutical formulations. Pharm. Res. 8 (1991) 285-291
    • (1991) Pharm. Res. , vol.8 , pp. 285-291
    • Arakawa, T.1    Kita, Y.2    Carpenter, J.F.3
  • 4
    • 0001321864 scopus 로고
    • The enzymatic synthesis of cytidine diphosphate choline
    • Borkenhagen L.F., and Kennedy E.P. The enzymatic synthesis of cytidine diphosphate choline. J. Biol. Chem. 227 (1957) 951-962
    • (1957) J. Biol. Chem. , vol.227 , pp. 951-962
    • Borkenhagen, L.F.1    Kennedy, E.P.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 47549099175 scopus 로고    scopus 로고
    • Choline, CDP-choline or phosphocholine increases plasma glucagon in rats: involvement of the peripheral autonomic nervous system
    • Cansev M., Ilcol Y.O., Yilmaz M.S., Hamurtekin E., and Ulus I.H. Choline, CDP-choline or phosphocholine increases plasma glucagon in rats: involvement of the peripheral autonomic nervous system. Eur. J. Pharmacol. 589 (2008) 315-322
    • (2008) Eur. J. Pharmacol. , vol.589 , pp. 315-322
    • Cansev, M.1    Ilcol, Y.O.2    Yilmaz, M.S.3    Hamurtekin, E.4    Ulus, I.H.5
  • 7
    • 51049108987 scopus 로고    scopus 로고
    • Influence of glycerol and sorbitol on thermally induced droplet aggregation in oil-in-water emulsions stabilized by β-lactoglobulin
    • Chanasattru W., Decker E.A., and McClements D.J. Influence of glycerol and sorbitol on thermally induced droplet aggregation in oil-in-water emulsions stabilized by β-lactoglobulin. Food Hydrocolloids 23 (2009) 253-261
    • (2009) Food Hydrocolloids , vol.23 , pp. 253-261
    • Chanasattru, W.1    Decker, E.A.2    McClements, D.J.3
  • 8
    • 36749043231 scopus 로고    scopus 로고
    • Water structure in vitro and within Saccharomyces cerevisiae yeast cells under conditions of heat shock
    • Dashnau J.L., Conlin L.K., Nelson H.C., and Vanderkooi J.M. Water structure in vitro and within Saccharomyces cerevisiae yeast cells under conditions of heat shock. Biochim. Biophys. Acta 1780 (2008) 41-50
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 41-50
    • Dashnau, J.L.1    Conlin, L.K.2    Nelson, H.C.3    Vanderkooi, J.M.4
  • 10
    • 0014027843 scopus 로고
    • The role of phospholipids in stimulating phosphorylcholine cytidyltransferase activity
    • Fiscus W.G., and Schneider W.C. The role of phospholipids in stimulating phosphorylcholine cytidyltransferase activity. J. Biol. Chem. 241 (1966) 3324-3330
    • (1966) J. Biol. Chem. , vol.241 , pp. 3324-3330
    • Fiscus, W.G.1    Schneider, W.C.2
  • 11
    • 55549110752 scopus 로고    scopus 로고
    • Optimization of culture conditions for hydrogen production by Ethanoligenens harbinense B49 using response surface methodology
    • Guo W.Q., Ren N.Q., Wang X.J., Xiang W.S., Ding J., You Y., et al. Optimization of culture conditions for hydrogen production by Ethanoligenens harbinense B49 using response surface methodology. Bioresource Technol. 100 (2009) 1192-1196
    • (2009) Bioresource Technol. , vol.100 , pp. 1192-1196
    • Guo, W.Q.1    Ren, N.Q.2    Wang, X.J.3    Xiang, W.S.4    Ding, J.5    You, Y.6
  • 12
    • 0011824269 scopus 로고
    • The synthesis of cytidine diphosphate choline, cytidine diphosphate ethanolamine, and related compounds
    • Kennedy E.P. The synthesis of cytidine diphosphate choline, cytidine diphosphate ethanolamine, and related compounds. J. Biol. Chem. 222 (1956) 185-191
    • (1956) J. Biol. Chem. , vol.222 , pp. 185-191
    • Kennedy, E.P.1
  • 13
    • 0000749205 scopus 로고
    • The function of cytidine coenzymes in the biosynthesis of phospholipids
    • Kennedy E.P., and Weiss S.B. The function of cytidine coenzymes in the biosynthesis of phospholipids. J. Biol. Chem. 222 (1956) 193-214
    • (1956) J. Biol. Chem. , vol.222 , pp. 193-214
    • Kennedy, E.P.1    Weiss, S.B.2
  • 14
    • 67649230753 scopus 로고
    • Fermentative production of CDP-choline by yeasts Part III some additional results on the production of CDP-choline by Brewer's yeast
    • Kimura A., Morita M., and Tochikura T. Fermentative production of CDP-choline by yeasts Part III some additional results on the production of CDP-choline by Brewer's yeast. Agric. Biol. Chem. 35 (1971) 1955-1960
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1955-1960
    • Kimura, A.1    Morita, M.2    Tochikura, T.3
  • 15
    • 0021810623 scopus 로고
    • AMP deaminase reaction as a control system of glycolysis in yeast: role of ammonium ion in the interaction of phosphofructokinase and pyruvate kinase activity with the adenylate energy charge
    • Masataka Y., and Keiko M. AMP deaminase reaction as a control system of glycolysis in yeast: role of ammonium ion in the interaction of phosphofructokinase and pyruvate kinase activity with the adenylate energy charge. J. Biol. Chem. 260 (1985) 4729-4732
    • (1985) J. Biol. Chem. , vol.260 , pp. 4729-4732
    • Masataka, Y.1    Keiko, M.2
  • 16
    • 33747863528 scopus 로고    scopus 로고
    • Control by osmolarity and electric field strength of electro-induced gene transfer and protein release in fission yeast cells
    • Minoru S., Atsumi G., and Toyomasa H. Control by osmolarity and electric field strength of electro-induced gene transfer and protein release in fission yeast cells. J. Electrostat. 64 (2006) 796-801
    • (2006) J. Electrostat. , vol.64 , pp. 796-801
    • Minoru, S.1    Atsumi, G.2    Toyomasa, H.3
  • 17
    • 32044436499 scopus 로고    scopus 로고
    • Fate and role of ammonium ions during fermentation of citric acid by Aspergillus niger
    • Papagianni M., Wayman F., and Mattey M. Fate and role of ammonium ions during fermentation of citric acid by Aspergillus niger. Appl. Environ. Microbiol. 71 (2005) 7178-7186
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 7178-7186
    • Papagianni, M.1    Wayman, F.2    Mattey, M.3
  • 18
    • 0037391699 scopus 로고    scopus 로고
    • Global metabolic regulation analysis for Escherichia coli K12 based on protein expression by 2-dimensional electrophoresis and enzyme activity measurement
    • Peng L., and Shimizu K. Global metabolic regulation analysis for Escherichia coli K12 based on protein expression by 2-dimensional electrophoresis and enzyme activity measurement. Appl. Microbiol. Biotechnol. 61 (2003) 163-178
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 163-178
    • Peng, L.1    Shimizu, K.2
  • 19
    • 0030887664 scopus 로고    scopus 로고
    • Overexpression of phosphofructokinase and pyruvate kinase in citric acid-producing Aspergillus niger
    • Ruijter G.J., Panneman H., and Visser J. Overexpression of phosphofructokinase and pyruvate kinase in citric acid-producing Aspergillus niger. Biochim. Biophys. Acta 1334 (1997) 317-326
    • (1997) Biochim. Biophys. Acta , vol.1334 , pp. 317-326
    • Ruijter, G.J.1    Panneman, H.2    Visser, J.3
  • 20
    • 0019127792 scopus 로고
    • Regulation of phosphatidylcholine biosynthesis in cultured chick embryonic muscle treated with phospholipase C
    • Sleight R., and Kent C. Regulation of phosphatidylcholine biosynthesis in cultured chick embryonic muscle treated with phospholipase C. J. Biol. Chem. 255 (1980) 10644-10650
    • (1980) J. Biol. Chem. , vol.255 , pp. 10644-10650
    • Sleight, R.1    Kent, C.2
  • 22
    • 67649221592 scopus 로고
    • The fermentative production of CDP-choline by yeasts: (I) identification of CDP-choline
    • Tochikura T., Kimura A., Kawai H., Tachiki T., and Gotan T. The fermentative production of CDP-choline by yeasts: (I) identification of CDP-choline. J. Ferment. Technol. 48 (1970) 763-768
    • (1970) J. Ferment. Technol. , vol.48 , pp. 763-768
    • Tochikura, T.1    Kimura, A.2    Kawai, H.3    Tachiki, T.4    Gotan, T.5
  • 23
    • 67649221152 scopus 로고
    • The fermentative production of CDP-choline by yeasts: (II) production and distribution of CDP-choline
    • Tochikura T., Kimura A., Kawai H., Tachiki T., and Gotan T. The fermentative production of CDP-choline by yeasts: (II) production and distribution of CDP-choline. J. Ferment. Technol. 48 (1970) 769-775
    • (1970) J. Ferment. Technol. , vol.48 , pp. 769-775
    • Tochikura, T.1    Kimura, A.2    Kawai, H.3    Tachiki, T.4    Gotan, T.5
  • 24
    • 0018830280 scopus 로고
    • Poliovirus increases phosphatidylcholine biosynthesis in HeLa cells by stimulation of the rate-limiting reaction catalyzed by CTP:phosphocholine cytidylyltransferase
    • Vance D.E., Trip E.M., and Paddon H.B. Poliovirus increases phosphatidylcholine biosynthesis in HeLa cells by stimulation of the rate-limiting reaction catalyzed by CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 255 (1980) 1064-1069
    • (1980) J. Biol. Chem. , vol.255 , pp. 1064-1069
    • Vance, D.E.1    Trip, E.M.2    Paddon, H.B.3
  • 25
    • 0034255393 scopus 로고    scopus 로고
    • Lyophilization and development of solid protein pharmaceuticals
    • Wang W. Lyophilization and development of solid protein pharmaceuticals. Int. J. Pharm. 203 (2000) 1-60
    • (2000) Int. J. Pharm. , vol.203 , pp. 1-60
    • Wang, W.1
  • 26
  • 27
    • 0001191635 scopus 로고
    • Intracellular distribution of some enzymes catalyzing reactions in the biosynthesis of complex lipids
    • Wilgram G.F., and Kennedy E.P. Intracellular distribution of some enzymes catalyzing reactions in the biosynthesis of complex lipids. J. Biol. Chem. 238 (1963) 2615-2619
    • (1963) J. Biol. Chem. , vol.238 , pp. 2615-2619
    • Wilgram, G.F.1    Kennedy, E.P.2
  • 28
    • 49749108901 scopus 로고    scopus 로고
    • CDP-choline prevents cardiac arrhythmias and lethality induced by short-term myocardial ischemia-reperfusion injury in the rat: involvement of central muscarinic cholinergic mechanisms
    • Yilmaz M.S., Coskun C., Yalcin M., and Savci V. CDP-choline prevents cardiac arrhythmias and lethality induced by short-term myocardial ischemia-reperfusion injury in the rat: involvement of central muscarinic cholinergic mechanisms. N-S. Arch. Pharmacol. 378 (2008) 293-301
    • (2008) N-S. Arch. Pharmacol. , vol.378 , pp. 293-301
    • Yilmaz, M.S.1    Coskun, C.2    Yalcin, M.3    Savci, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.