메뉴 건너뛰기




Volumn 370, Issue 2, 2003, Pages 409-415

Cloning, expression and characterization of a mammalian nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose

Author keywords

Gluconeogenesis; Glycogen; Nucleotide sugar

Indexed keywords

BIOSYNTHESIS; CELLS; DNA; ENZYMES; ESCHERICHIA COLI; GLUCOSE; HYDROLYSIS;

EID: 0242501006     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021140     Document Type: Article
Times cited : (26)

References (48)
  • 1
    • 0029924167 scopus 로고    scopus 로고
    • UDP-glucose deficiency in a mutant cell line protects against glucosyltransferase toxins from Clostridium difficile and Clostridium sordellii
    • Chaves-Olarte, E., Florin, I., Boquet, P., Popoff, M., von Eichel-Streiber, C. and Thelestam, M. (1996) UDP-glucose deficiency in a mutant cell line protects against glucosyltransferase toxins from Clostridium difficile and Clostridium sordellii. J. Biol. Chem. 271, 6925-6932
    • (1996) J. Biol. Chem. , vol.271 , pp. 6925-6932
    • Chaves-Olarte, E.1    Florin, I.2    Boquet, P.3    Popoff, M.4    Von Eichel-Streiber, C.5    Thelestam, M.6
  • 4
    • 0030856736 scopus 로고    scopus 로고
    • Metabolic impact of adenovirus-mediated overexpression of the glucose-6-phosphate catalytic subunit in hepatocytes
    • Seoane, J., Trinh, K., O'Doherty, R. M., Gómez-Foix, A. M., Lange, A. J., Newgard, C. B. and Guinovart, J. J. (1997) Metabolic impact of adenovirus-mediated overexpression of the glucose-6-phosphate catalytic subunit in hepatocytes. J. Biol. Chem. 272, 26972-26977
    • (1997) J. Biol. Chem. , vol.272 , pp. 26972-26977
    • Seoane, J.1    Trinh, K.2    O'Doherty, R.M.3    Gómez-Foix, A.M.4    Lange, A.J.5    Newgard, C.B.6    Guinovart, J.J.7
  • 5
    • 0032533162 scopus 로고    scopus 로고
    • Specific features of glycogen metabolism in the liver
    • Bollen, M., Keppens, S. and Stalmans, W. (1998) Specific features of glycogen metabolism in the liver. Biochem. J. 336, 19-31
    • (1998) Biochem. J. , vol.336 , pp. 19-31
    • Bollen, M.1    Keppens, S.2    Stalmans, W.3
  • 9
    • 0032772985 scopus 로고    scopus 로고
    • Sucrose-starch conversion in heterotrophic tissues of plants
    • Pozueta-Romero, J., Perata, P. and Akazawa, T. (1999) Sucrose-starch conversion in heterotrophic tissues of plants. Crit. Rev. Plant Sci. 18, 489-525
    • (1999) Crit. Rev. Plant Sci. , vol.18 , pp. 489-525
    • Pozueta-Romero, J.1    Perata, P.2    Akazawa, T.3
  • 10
    • 0032724559 scopus 로고    scopus 로고
    • Exponential-phase glycogen recycling is essential for growth of Micobacterium smegmatis
    • Belanger, A. E. and Hatfull, G. F. (1999) Exponential-phase glycogen recycling is essential for growth of Micobacterium smegmatis. J. Bacteriol. 181, 6670-6678
    • (1999) J. Bacteriol. , vol.181 , pp. 6670-6678
    • Belanger, A.E.1    Hatfull, G.F.2
  • 11
    • 0034019605 scopus 로고    scopus 로고
    • Kinetic analysis of Clostridium cellulolyticum carbohydrate metabolism: Importance of glucose-1-phosphate and glucose-6-phosphate branch points for distribution of carbon fluxes inside and outside cells as revealed by steady-state continuous culture
    • Guedon, E., Desvaux, M. and Petitdemange, H. (2000) Kinetic analysis of Clostridium cellulolyticum carbohydrate metabolism: importance of glucose-1-phosphate and glucose-6-phosphate branch points for distribution of carbon fluxes inside and outside cells as revealed by steady-state continuous culture. J. Bacteriol. 182, 2010-2017
    • (2000) J. Bacteriol. , vol.182 , pp. 2010-2017
    • Guedon, E.1    Desvaux, M.2    Petitdemange, H.3
  • 12
    • 0017616868 scopus 로고
    • Glycosyltransferase and UDP-galactose pyrophosphatase activities in the endometrium during the oestrous cycle of the rat
    • Nelson, J. D., Jato-Rodriguez, J. J., Labrie, F. and Mookerjea, S. (1977) Glycosyltransferase and UDP-galactose pyrophosphatase activities in the endometrium during the oestrous cycle of the rat. J. Endocr. 73, 53-58
    • (1977) J. Endocr. , vol.73 , pp. 53-58
    • Nelson, J.D.1    Jato-Rodriguez, J.J.2    Labrie, F.3    Mookerjea, S.4
  • 13
    • 0020565299 scopus 로고
    • Increased glycosylation capacity in regenerating rat liver is paralleled by decreased activities of CMP-N-acetylneuraminate hydrolase and UDP galactose pyrophosphatase
    • Van Dijk, W., Lasthuis, A.-M., Trippelvitz, L. A. W. and Muilerman, H. G. (1983) Increased glycosylation capacity in regenerating rat liver is paralleled by decreased activities of CMP-N-acetylneuraminate hydrolase and UDP galactose pyrophosphatase. Biochem. J. 214, 1003-1006
    • (1983) Biochem. J. , vol.214 , pp. 1003-1006
    • Van Dijk, W.1    Lasthuis, A.-M.2    Trippelvitz, L.A.W.3    Muilerman, H.G.4
  • 14
    • 0021845192 scopus 로고
    • Formation of lipid-linked oligosaccharides by MOPC 315 plasmacytoma cells
    • Hickman, S., Wong-Yip, Y. P., Rebbe, N. F. and Greco, J. M. (1985) Formation of lipid-linked oligosaccharides by MOPC 315 plasmacytoma cells. J. Biol. Chem. 260, 6098-6106
    • (1985) J. Biol. Chem. , vol.260 , pp. 6098-6106
    • Hickman, S.1    Wong-Yip, Y.P.2    Rebbe, N.F.3    Greco, J.M.4
  • 17
    • 0242476654 scopus 로고
    • The purification and properties of a nucleotide pyrophosphatase of rat liver nuclei
    • Schliselfeld, L. H., van Eys, J. and Touster, O. (1965) The purification and properties of a nucleotide pyrophosphatase of rat liver nuclei. J. Biol. Chem. 240, 811-818
    • (1965) J. Biol. Chem. , vol.240 , pp. 811-818
    • Schliselfeld, L.H.1    Van Eys, J.2    Touster, O.3
  • 18
    • 0014717840 scopus 로고
    • Nucleotide pyrophosphatase activity of rat liver plasma membranes
    • Skidmore, J. and Trams, E. G. (1970) Nucleotide pyrophosphatase activity of rat liver plasma membranes. Biochim. Biophys. Acta 219, 93-103
    • (1970) Biochim. Biophys. Acta , vol.219 , pp. 93-103
    • Skidmore, J.1    Trams, E.G.2
  • 19
    • 0015523526 scopus 로고
    • The purification and properties of detergent-solubilized rat liver nucleotide pyrophosphatase
    • Bachorik, P. S. and Dietrich, L. S. (1972) The purification and properties of detergent-solubilized rat liver nucleotide pyrophosphatase. J. Biol. Chem. 247, 5071-5078
    • (1972) J. Biol. Chem. , vol.247 , pp. 5071-5078
    • Bachorik, P.S.1    Dietrich, L.S.2
  • 20
    • 0019774072 scopus 로고
    • Glycosaminoglycan synthesis by cultured skin fibroblasts from a patient with Lowe's syndrome
    • Fukui, S., Yoshida, H., Tanaka, T., Sakano, T., Usui, T. and Yamashina, I. (1981) Glycosaminoglycan synthesis by cultured skin fibroblasts from a patient with Lowe's syndrome. J. Biol. Chem. 256, 10313-10318
    • (1981) J. Biol. Chem. , vol.256 , pp. 10313-10318
    • Fukui, S.1    Yoshida, H.2    Tanaka, T.3    Sakano, T.4    Usui, T.5    Yamashina, I.6
  • 23
    • 0033863689 scopus 로고    scopus 로고
    • Association between the human glycoprotein PC-1 gene and elevated glucose and insulin levels in a paired-sibling analysis
    • Gu, H. F., Almgren, P., Lindholm, E., Frittitta, L., Pizzuti, A., Trischitta, V. and Groop, L. C. (2000) Association between the human glycoprotein PC-1 gene and elevated glucose and insulin levels in a paired-sibling analysis. Diabetes 49, 1601-1603
    • (2000) Diabetes , vol.49 , pp. 1601-1603
    • Gu, H.F.1    Almgren, P.2    Lindholm, E.3    Frittitta, L.4    Pizzuti, A.5    Trischitta, V.6    Groop, L.C.7
  • 24
    • 0033957339 scopus 로고    scopus 로고
    • Membrane glycoprotein PC-1 inhibiticn of insulin receptor function occurs via direct interaction with the receptor a-subunit
    • Maddux, B. A. and Goldfine, I. D. (2000) Membrane glycoprotein PC-1 inhibiticn of insulin receptor function occurs via direct interaction with the receptor a-subunit. Diabetes 49, 13-19
    • (2000) Diabetes , vol.49 , pp. 13-19
    • Maddux, B.A.1    Goldfine, I.D.2
  • 27
    • 0017158639 scopus 로고
    • Location of nucleotide pyrophosphatase and alkaline phosphodiesterase activities on the lymphocyte surface membrane
    • Abney, E. R., Evans, W. H. and Parkhouse, M. E. (1976) Location of nucleotide pyrophosphatase and alkaline phosphodiesterase activities on the lymphocyte surface membrane. Biochem. J. 159, 293-299
    • (1976) Biochem. J. , vol.159 , pp. 293-299
    • Abney, E.R.1    Evans, W.H.2    Parkhouse, M.E.3
  • 28
    • 0026009523 scopus 로고
    • Identification of nucleotide pyrophosphatase/alkaline phosphodiesterase I activity associated with the mouse plasma cell differentiation antigen PC-1
    • Rebbe, N. F., Tong, B. D., Finley, E. M. and Hickman, S. (1991) Identification of nucleotide pyrophosphatase/alkaline phosphodiesterase I activity associated with the mouse plasma cell differentiation antigen PC-1. Proc. Natl. Acad. Sci. U.S.A. 88, 5192-5196
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 5192-5196
    • Rebbe, N.F.1    Tong, B.D.2    Finley, E.M.3    Hickman, S.4
  • 30
    • 0006366015 scopus 로고    scopus 로고
    • Inhibition of phosphodiesterase/pyrophosphatase activity of PC-1 by its association with glycosaminoglycans
    • Hosoda, N., Hoshino, S.-I, Kanda, Y. and Katada, T. (1999) Inhibition of phosphodiesterase/pyrophosphatase activity of PC-1 by its association with glycosaminoglycans. Eur. J. Biochem. 265, 763-770
    • (1999) Eur. J. Biochem. , vol.265 , pp. 763-770
    • Hosoda, N.1    Hoshino, S.-I.2    Kanda, Y.3    Katada, T.4
  • 31
    • 0035847049 scopus 로고    scopus 로고
    • Structural and catalytic similarities between nucleotide pyrophosphatases/phosphodiesterases and alkaline phosphatases
    • Gisjbers, R., Ceulemans, H., Stalmans, W. and Bollen, M. (2000) Structural and catalytic similarities between nucleotide pyrophosphatases/phosphodiesterases and alkaline phosphatases. J. Biol. Chem. 276, 1361-1368
    • (2000) J. Biol. Chem. , vol.276 , pp. 1361-1368
    • Gisjbers, R.1    Ceulemans, H.2    Stalmans, W.3    Bollen, M.4
  • 32
    • 0035865662 scopus 로고    scopus 로고
    • Sucrose and light regulation of a cold-inducible UDP-glucose pyrophosphorylase gene via a hexokinase-independent and abscisic acid-insensitive pathway in Arabidopsis
    • Ciereszko, I., Johansson, H. and Kleczkowski, L. A. (2001) Sucrose and light regulation of a cold-inducible UDP-glucose pyrophosphorylase gene via a hexokinase-independent and abscisic acid-insensitive pathway in Arabidopsis. Biochem. J. 354, 67-72
    • (2001) Biochem. J. , vol.354 , pp. 67-72
    • Ciereszko, I.1    Johansson, H.2    Kleczkowski, L.A.3
  • 33
    • 0029877062 scopus 로고    scopus 로고
    • The importance of conserved residues in human liver UDPglucose pyrophosphorylase
    • Chang, H. Y., Peng, H. L., Chao, Y. C. and Duggleby, R. G. (1996) The importance of conserved residues in human liver UDPglucose pyrophosphorylase. Eur. J. Biochem. 236, 723-728
    • (1996) Eur. J. Biochem. , vol.236 , pp. 723-728
    • Chang, H.Y.1    Peng, H.L.2    Chao, Y.C.3    Duggleby, R.G.4
  • 36
    • 0033452851 scopus 로고    scopus 로고
    • Cloning, expression and characterization of YSA1H, a human adenosine 5′-diphosphosugar pyrophosphatase possessing a MutT motif
    • Gasmi, L., Cartwright, J. L. and McLennan, A. (1999) Cloning, expression and characterization of YSA1H, a human adenosine 5′-diphosphosugar pyrophosphatase possessing a MutT motif. Biochem. J. 344, 331-337
    • (1999) Biochem. J. , vol.344 , pp. 331-337
    • Gasmi, L.1    Cartwright, J.L.2    McLennan, A.3
  • 37
    • 0029835350 scopus 로고    scopus 로고
    • The MutT proteins or 'Nudix' hydrolases, a family of versatile, widely distributed, 'housecleaning' enzymes
    • Bessman, M. J., Frick, D. N. and O'Handley, S. F. (1996) The MutT proteins or 'Nudix' hydrolases, a family of versatile, widely distributed, 'housecleaning' enzymes. J. Biol. Chem. 271, 25059-25062
    • (1996) J. Biol. Chem. , vol.271 , pp. 25059-25062
    • Bessman, M.J.1    Frick, D.N.2    O'Handley, S.F.3
  • 39
    • 0035026968 scopus 로고    scopus 로고
    • The structure of ADP-ribose pyrophosphatase reveals the structural basis of the versatility of the Nudix family
    • Gabelli, S. B., Bianchet, M. A., Bessman, M. J. and Amzel, M. (2001) The structure of ADP-ribose pyrophosphatase reveals the structural basis of the versatility of the Nudix family. Nat. Struct. Biol. 8, 467-472
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 467-472
    • Gabelli, S.B.1    Bianchet, M.A.2    Bessman, M.J.3    Amzel, M.4
  • 40
    • 0032488819 scopus 로고    scopus 로고
    • Orf186 represents a new member of the nudix hydrolases, active on adenosine (5′) triphospho (5′) adenosine, ADP-ribose, and NADH
    • O'Handley, S., Frick, D. N., Dunn, C. A. and Bessman, M. J. (1998) Orf186 represents a new member of the nudix hydrolases, active on adenosine (5′) triphospho (5′) adenosine, ADP-ribose, and NADH. J. Biol. Chem. 273, 3192-3197
    • (1998) J. Biol. Chem. , vol.273 , pp. 3192-3197
    • O'Handley, S.1    Frick, D.N.2    Dunn, C.A.3    Bessman, M.J.4
  • 41
    • 0014216565 scopus 로고
    • Uridine diphosphate sugar hydrolase
    • Glaser, L., Melo, A. and Paul, R. (1967) Uridine diphosphate sugar hydrolase. J. Biol. Chem. 242, 1944-1954
    • (1967) J. Biol. Chem. , vol.242 , pp. 1944-1954
    • Glaser, L.1    Melo, A.2    Paul, R.3
  • 42
    • 0020424591 scopus 로고
    • Studies on the UDP-sugar hydrolases from Escherichia coli and Salmonella typhimurium
    • Beacham, I. R. and Wilson, M. S. (1982) Studies on the UDP-sugar hydrolases from Escherichia coli and Salmonella typhimurium. Arch. Biochem. Biophys. 218, 603-608
    • (1982) Arch. Biochem. Biophys. , vol.218 , pp. 603-608
    • Beacham, I.R.1    Wilson, M.S.2
  • 43
    • 0020974081 scopus 로고
    • Characterisation of the ush gene of Escherichia coli and its protein products
    • Burns, D. M., Abraham, L. J. and Beacham, I. R. (1983) Characterisation of the ush gene of Escherichia coli and its protein products. Gene 25, 343-353
    • (1983) Gene , vol.25 , pp. 343-353
    • Burns, D.M.1    Abraham, L.J.2    Beacham, I.R.3
  • 44
    • 0029840695 scopus 로고    scopus 로고
    • Identification of a bacterial inhibitor of protein kinases
    • Berger, S. A., Rowan, K., Morrison, H. D. and Ziltener, H. J. (1996) Identification of a bacterial inhibitor of protein kinases. J. Biol. Chem 271, 23431-23437
    • (1996) J. Biol. Chem. , vol.271 , pp. 23431-23437
    • Berger, S.A.1    Rowan, K.2    Morrison, H.D.3    Ziltener, H.J.4
  • 45
    • 0030931082 scopus 로고    scopus 로고
    • Toxins A and B from Clostridium difficile differ with respect to enzymatic potencies, cellular substrate specificities, and surface binding to cultured cells
    • Chaves-Olarte, E., Weidmann, M., von Eichel-Streiber, C. and Thelestam, M. (1997) Toxins A and B from Clostridium difficile differ with respect to enzymatic potencies, cellular substrate specificities, and surface binding to cultured cells. J. Clin. Invest. 100, 1734-1741
    • (1997) J. Clin. Invest. , vol.100 , pp. 1734-1741
    • Chaves-Olarte, E.1    Weidmann, M.2    Von Eichel-Streiber, C.3    Thelestam, M.4
  • 47
    • 0025933503 scopus 로고
    • Expert system for predicting protein localization sites in gram-negative bacteria
    • Nakai, K. and Kanehisa, M. (1991) Expert system for predicting protein localization sites in gram-negative bacteria. Proteins 11, 95-110
    • (1991) Proteins , vol.11 , pp. 95-110
    • Nakai, K.1    Kanehisa, M.2
  • 48
    • 0023765635 scopus 로고
    • Glycogenin is the priming glucosyltransferase required for the initiation of glycogen biogenesis in rabbit skeletal muscle
    • Pitcher, J., Smythe, C. and Cohen, P. (1988) Glycogenin is the priming glucosyltransferase required for the initiation of glycogen biogenesis in rabbit skeletal muscle. Eur. J. Biochem. 176, 391-395
    • (1988) Eur. J. Biochem. , vol.176 , pp. 391-395
    • Pitcher, J.1    Smythe, C.2    Cohen, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.