메뉴 건너뛰기




Volumn 390, Issue 4, 2009, Pages 1414-1418

Characterization of mouse UDP-glucose pyrophosphatase, a Nudix hydrolase encoded by the Nudt14 gene

Author keywords

ADP ribose; Glycogen; Nudix hydrolase; Nudt14; Pyrophosphatase; UDP glucose

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; MAGNESIUM ION; MONOMER; NUCLEOSIDE DIPHOSPHATE SUGAR; RECOMBINANT PROTEIN; URIDINE TRIPHOSPHATE GLUCOSE 1 PHOSPHATE URIDYLYLTRANSFERASE;

EID: 70450246990     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.11.007     Document Type: Article
Times cited : (20)

References (22)
  • 1
    • 0242476654 scopus 로고
    • The purification and properties of a nucleotide pyrophosphatase of rat liver nuclei
    • Schliselfeld L.H., Vaneys J., and Touster O. The purification and properties of a nucleotide pyrophosphatase of rat liver nuclei. J. Biol. Chem. 240 (1965) 811-818
    • (1965) J. Biol. Chem. , vol.240 , pp. 811-818
    • Schliselfeld, L.H.1    Vaneys, J.2    Touster, O.3
  • 2
    • 0014717840 scopus 로고
    • Nucleotide pyrophosphatase activity of rat liver plasma membranes
    • Skidmore J., and Trams E.G. Nucleotide pyrophosphatase activity of rat liver plasma membranes. Biochim. Biophys. Acta 219 (1970) 93-103
    • (1970) Biochim. Biophys. Acta , vol.219 , pp. 93-103
    • Skidmore, J.1    Trams, E.G.2
  • 3
    • 0015523526 scopus 로고
    • The purification and properties of detergent-solubilized rat liver nucleotide pyrophosphatase
    • Bachorik P.S., and Dietrich L.S. The purification and properties of detergent-solubilized rat liver nucleotide pyrophosphatase. J. Biol. Chem. 247 (1972) 5071-5078
    • (1972) J. Biol. Chem. , vol.247 , pp. 5071-5078
    • Bachorik, P.S.1    Dietrich, L.S.2
  • 4
    • 0242501006 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose
    • Yagi T., Baroja-Fernandez E., Yamamoto R., Munoz F.J., Akazawa T., Hong K.S., and Pozueta-Romero J. Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose. Biochem. J. 370 (2003) 409-415
    • (2003) Biochem. J. , vol.370 , pp. 409-415
    • Yagi, T.1    Baroja-Fernandez, E.2    Yamamoto, R.3    Munoz, F.J.4    Akazawa, T.5    Hong, K.S.6    Pozueta-Romero, J.7
  • 5
    • 30744470374 scopus 로고    scopus 로고
    • The Nudix hydrolase superfamily
    • McLennan A.G. The Nudix hydrolase superfamily. Cell. Mol. Life Sci. 63 (2006) 123-143
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 123-143
    • McLennan, A.G.1
  • 8
    • 0030856736 scopus 로고    scopus 로고
    • Metabolic impact of adenovirus-mediated overexpression of the glucose-6-phosphatase catalytic subunit in hepatocytes
    • Seoane J., Trinh K., O'Doherty R.M., Gomez-Foix A.M., Lange A.J., Newgard C.B., and Guinovart J.J. Metabolic impact of adenovirus-mediated overexpression of the glucose-6-phosphatase catalytic subunit in hepatocytes. J. Biol. Chem. 272 (1997) 26972-26977
    • (1997) J. Biol. Chem. , vol.272 , pp. 26972-26977
    • Seoane, J.1    Trinh, K.2    O'Doherty, R.M.3    Gomez-Foix, A.M.4    Lange, A.J.5    Newgard, C.B.6    Guinovart, J.J.7
  • 9
    • 0029744440 scopus 로고    scopus 로고
    • Increased glycogen accumulation in transgenic mice overexpressing glycogen synthase in skeletal muscle
    • Manchester J., Skurat A.V., Roach P., Hauschka S.D., and Lawrence Jr. J.C. Increased glycogen accumulation in transgenic mice overexpressing glycogen synthase in skeletal muscle. Proc. Natl. Acad. Sci. USA 93 (1996) 10707-10711
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10707-10711
    • Manchester, J.1    Skurat, A.V.2    Roach, P.3    Hauschka, S.D.4    Lawrence Jr., J.C.5
  • 11
    • 0002915347 scopus 로고    scopus 로고
    • Regulation of glycogen biosynthesis
    • LeRoith D., Olefsky J.E., and Taylor S. (Eds), J.B. Lippincott Company, Philadelphia
    • Skurat A.V., and Roach P.J. Regulation of glycogen biosynthesis. In: LeRoith D., Olefsky J.E., and Taylor S. (Eds). Diabetes Mellitus: A Fundamental and Clinical Text (2003), J.B. Lippincott Company, Philadelphia 317-333
    • (2003) Diabetes Mellitus: A Fundamental and Clinical Text , pp. 317-333
    • Skurat, A.V.1    Roach, P.J.2
  • 12
    • 0036079974 scopus 로고    scopus 로고
    • Glycogen and its metabolism
    • Roach P.J. Glycogen and its metabolism. Curr. Mol. Med. 2 (2002) 101-120
    • (2002) Curr. Mol. Med. , vol.2 , pp. 101-120
    • Roach, P.J.1
  • 14
    • 0024834054 scopus 로고
    • Physiology, biochemistry and genetics of bacterial glycogen synthesis
    • Preiss J., and Romeo T. Physiology, biochemistry and genetics of bacterial glycogen synthesis. Adv. Microb. Physiol. 30 (1989) 183-238
    • (1989) Adv. Microb. Physiol. , vol.30 , pp. 183-238
    • Preiss, J.1    Romeo, T.2
  • 15
    • 33846277297 scopus 로고    scopus 로고
    • The diurnal metabolism of leaf starch
    • Zeeman S.C., Smith S.M., and Smith A.M. The diurnal metabolism of leaf starch. Biochem. J. 401 (2007) 13-28
    • (2007) Biochem. J. , vol.401 , pp. 13-28
    • Zeeman, S.C.1    Smith, S.M.2    Smith, A.M.3
  • 17
    • 33747818834 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a Nudix hydrolase that catalyzes the hydrolytic breakdown of ADP-glucose linked to starch biosynthesis in Arabidopsis thaliana
    • Munoz F.J., Baroja-Fernandez E., Moran-Zorzano M.T., Alonso-Casajus N., and Pozueta-Romero J. Cloning, expression and characterization of a Nudix hydrolase that catalyzes the hydrolytic breakdown of ADP-glucose linked to starch biosynthesis in Arabidopsis thaliana. Plant Cell Physiol. 47 (2006) 926-934
    • (2006) Plant Cell Physiol. , vol.47 , pp. 926-934
    • Munoz, F.J.1    Baroja-Fernandez, E.2    Moran-Zorzano, M.T.3    Alonso-Casajus, N.4    Pozueta-Romero, J.5
  • 18
    • 0035682737 scopus 로고    scopus 로고
    • Reappraisal of the currently prevailing model of starch biosynthesis in photosynthetic tissues: a proposal involving the cytosolic production of ADP-glucose by sucrose synthase and occurrence of cyclic turnover of starch in the chloroplast
    • Baroja-Fernandez E., Munoz F.J., Akazawa T., and Pozueta-Romero J. Reappraisal of the currently prevailing model of starch biosynthesis in photosynthetic tissues: a proposal involving the cytosolic production of ADP-glucose by sucrose synthase and occurrence of cyclic turnover of starch in the chloroplast. Plant Cell Physiol. 42 (2001) 1311-1320
    • (2001) Plant Cell Physiol. , vol.42 , pp. 1311-1320
    • Baroja-Fernandez, E.1    Munoz, F.J.2    Akazawa, T.3    Pozueta-Romero, J.4
  • 21
    • 0031407133 scopus 로고    scopus 로고
    • Topography and function of golgi uridine-5[prime]-diphosphatase from pea stems
    • Orellana A., Neckelmann G., and Norambuena L. Topography and function of golgi uridine-5[prime]-diphosphatase from pea stems. Plant Physiol. 114 (1997) 99-107
    • (1997) Plant Physiol. , vol.114 , pp. 99-107
    • Orellana, A.1    Neckelmann, G.2    Norambuena, L.3
  • 22
    • 0028181369 scopus 로고
    • Purification of 1,3-beta-d-glucan synthase activity from pea tissue. Two polypeptides of 55 kDa and 70 kDa copurify with enzyme activity
    • Dhugga K.S., and Ray P.M. Purification of 1,3-beta-d-glucan synthase activity from pea tissue. Two polypeptides of 55 kDa and 70 kDa copurify with enzyme activity. Eur. J. Biochem. 220 (1994) 943-953
    • (1994) Eur. J. Biochem. , vol.220 , pp. 943-953
    • Dhugga, K.S.1    Ray, P.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.