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Volumn 2, Issue C, 1996, Pages 259-279

ADPglucose Pyrophosphorylase: Basic Science and Applications in Biotechnology

Author keywords

ADPglucose pyrophosphorylase; bacterial glycogen synthesis; branching enzyme; control coefficient analysis of starch synthesis; starch synthase; starch synthesis

Indexed keywords

1,4 GLUCAN; 1,4-GLUCAN; GLUCAN; GLUCOSE 1 PHOSPHATE ADENYLYLTRANSFERASE; NUCLEOTIDYLTRANSFERASE;

EID: 0030309983     PISSN: 13872656     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1387-2656(08)70013-9     Document Type: Article
Times cited : (30)

References (72)
  • 1
    • 0001261938 scopus 로고
    • Enzymic synthesis of adenosine diphosphate glucose from glucose 1-phosphate and adenosine triphosphate
    • Espada J. Enzymic synthesis of adenosine diphosphate glucose from glucose 1-phosphate and adenosine triphosphate. J Biol Chem 237 (1962) 3577-3581
    • (1962) J Biol Chem , vol.237 , pp. 3577-3581
    • Espada, J.1
  • 2
    • 0000271302 scopus 로고
    • Regulation of the biosynthesis and degradation of starch
    • Preiss J. Regulation of the biosynthesis and degradation of starch. Ann Rev Plant Physiol 54 (1982) 431-454
    • (1982) Ann Rev Plant Physiol , vol.54 , pp. 431-454
    • Preiss, J.1
  • 3
    • 0021144092 scopus 로고
    • Bacterial glycogen synthesis and its regulation
    • Preiss J. Bacterial glycogen synthesis and its regulation. Ann Rev Microbiol 38 (1984) 419-458
    • (1984) Ann Rev Microbiol , vol.38 , pp. 419-458
    • Preiss, J.1
  • 4
    • 84940969074 scopus 로고
    • Biosynthesis of starch and its regulation
    • Preiss J. (Ed), Academic Press, New York
    • Preiss J. Biosynthesis of starch and its regulation. In: Preiss J. (Ed). The Biochemistry of Plants, 14 (1988), Academic Press, New York 181-254
    • (1988) The Biochemistry of Plants, 14 , pp. 181-254
    • Preiss, J.1
  • 5
    • 0002998420 scopus 로고
    • Starch biosynthesis and its regulation
    • Miflin J. (Ed), Oxford University Press, Oxford
    • Preiss J. Starch biosynthesis and its regulation. In: Miflin J. (Ed). Surveys of Plant Molecular and Cell Biology 7 (1991), Oxford University Press, Oxford 59-114
    • (1991) Surveys of Plant Molecular and Cell Biology , vol.7 , pp. 59-114
    • Preiss, J.1
  • 6
    • 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 Microbiol Physiol 30 (1989) 83-238
    • (1989) Adv Microbiol Physiol , vol.30 , pp. 83-238
    • Preiss, J.1    Romeo, T.2
  • 7
    • 0028189275 scopus 로고
    • Molecular biology and regulatory aspects of glycogen biosynthesis in bacteria
    • Preiss J., and Romeo T. Molecular biology and regulatory aspects of glycogen biosynthesis in bacteria. Prog Nucl Acid Res Molec Biol 47 (1994) 299-329
    • (1994) Prog Nucl Acid Res Molec Biol , vol.47 , pp. 299-329
    • Preiss, J.1    Romeo, T.2
  • 8
    • 85051574469 scopus 로고
    • Starch synthesis in seeds
    • Kigel J., and Galili G. (Eds), Marcel Dekker, Inc., New York
    • Sivak M.N., and Preiss J. Starch synthesis in seeds. In: Kigel J., and Galili G. (Eds). Seed Development and Germination (1994), Marcel Dekker, Inc., New York 139-168
    • (1994) Seed Development and Germination , pp. 139-168
    • Sivak, M.N.1    Preiss, J.2
  • 10
    • 0026767213 scopus 로고
    • Comparison of proteins of ADP-glucose pyrophosphorylase from diverse sources
    • Smith-White B.J., and Preiss J. Comparison of proteins of ADP-glucose pyrophosphorylase from diverse sources. J Molec Evol 34 (1992) 449-464
    • (1992) J Molec Evol , vol.34 , pp. 449-464
    • Smith-White, B.J.1    Preiss, J.2
  • 12
    • 0022993290 scopus 로고
    • Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADPglucose: α-1,4-glucan, 4-glucosyltransferase deduced from the nucleotide sequence of the glg A gene
    • Kumar A., Larsen C.E., and Preiss J. Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADPglucose: α-1,4-glucan, 4-glucosyltransferase deduced from the nucleotide sequence of the glg A gene. J Biol Chem 261 (1986) 14634-14639
    • (1986) J Biol Chem , vol.261 , pp. 14634-14639
    • Kumar, A.1    Larsen, C.E.2    Preiss, J.3
  • 14
    • 0027630893 scopus 로고
    • Soluble isoforms of starch synthase and starch branching enzyme also occur within starch granules in developing pea embryos
    • Denyer K., Sidebottom C., Hylton C.M., and Smith A.M. Soluble isoforms of starch synthase and starch branching enzyme also occur within starch granules in developing pea embryos. Plant J 4 (1993) 191-196
    • (1993) Plant J , vol.4 , pp. 191-196
    • Denyer, K.1    Sidebottom, C.2    Hylton, C.M.3    Smith, A.M.4
  • 15
    • 0026652567 scopus 로고
    • Waxy Chlamydomonas reinhardtii: monocellular algal mutants defective in amylose synthesis and granule-bound starch synthase activity accumulate a structurally modified amylopectin
    • Delrue B., Fontaine T., Routier F., Decq A., Wieruszeski J.-M., Van Den Koornhuyse N., Maddelein M.-L., Fournet B., and Ball S. Waxy Chlamydomonas reinhardtii: monocellular algal mutants defective in amylose synthesis and granule-bound starch synthase activity accumulate a structurally modified amylopectin. J Bacteriol 174 (1992) 3612-3620
    • (1992) J Bacteriol , vol.174 , pp. 3612-3620
    • Delrue, B.1    Fontaine, T.2    Routier, F.3    Decq, A.4    Wieruszeski, J.-M.5    Van Den Koornhuyse, N.6    Maddelein, M.-L.7    Fournet, B.8    Ball, S.9
  • 18
    • 0040687034 scopus 로고
    • Polymodal distribution of the chain lengths of amylopectins, and its significance
    • Hizukuri S. Polymodal distribution of the chain lengths of amylopectins, and its significance. CarbohydrRes 147 (1986) 342-347
    • (1986) CarbohydrRes , vol.147 , pp. 342-347
    • Hizukuri, S.1
  • 20
    • 0027524850 scopus 로고
    • Role of the conserved Lys-X-Gly-Gly sequence at the ADP-glucose-binding site in Escherichia coli glycogen synthase
    • Furukawa K., Tagaya M., Tanizawa K., and Fukui T. Role of the conserved Lys-X-Gly-Gly sequence at the ADP-glucose-binding site in Escherichia coli glycogen synthase. J Biol Chem 268 (1993) 23837-23842
    • (1993) J Biol Chem , vol.268 , pp. 23837-23842
    • Furukawa, K.1    Tagaya, M.2    Tanizawa, K.3    Fukui, T.4
  • 23
    • 0028409018 scopus 로고
    • Expression of branching enzyme I of maize endosperm in Escherichia coli
    • Guan H.P., Baba T., and Preiss J. Expression of branching enzyme I of maize endosperm in Escherichia coli. Plant Physiol 104 (1994) 1449-1453
    • (1994) Plant Physiol , vol.104 , pp. 1449-1453
    • Guan, H.P.1    Baba, T.2    Preiss, J.3
  • 24
    • 0011215373 scopus 로고
    • Expression of branching enzyme II of maize endosperm in Escherichia coli
    • Guan H.P., Baba T., and Preiss J. Expression of branching enzyme II of maize endosperm in Escherichia coli. Cell Molec Biol 40 (1994) 981-987
    • (1994) Cell Molec Biol , vol.40 , pp. 981-987
    • Guan, H.P.1    Baba, T.2    Preiss, J.3
  • 25
    • 0027623412 scopus 로고
    • Starch branching enzyme II from maize endosperm
    • Fisher D.K., Boyer C.D., and Hannah L.C. Starch branching enzyme II from maize endosperm. Plant Physiol 102 (1993) 1053-1054
    • (1993) Plant Physiol , vol.102 , pp. 1053-1054
    • Fisher, D.K.1    Boyer, C.D.2    Hannah, L.C.3
  • 27
    • 0000300787 scopus 로고
    • Nucleotide sequence of a cDNA encoding starch branching enzyme or Q-enzyme I from rice endosperm
    • Nakamura Y., and Yamanouchi H. Nucleotide sequence of a cDNA encoding starch branching enzyme or Q-enzyme I from rice endosperm. Plant Physiol 99 (1992) 1265-1266
    • (1992) Plant Physiol , vol.99 , pp. 1265-1266
    • Nakamura, Y.1    Yamanouchi, H.2
  • 28
    • 0027247801 scopus 로고
    • Alteration of the structural properties of starch components by the lack of an isoform of starch branching enzyme in rice seeds
    • Mizuno K., Kawasaki T., Shimada H., Satoh H., Kobayashi E., Okamura S., Arai Y., and Baba T. Alteration of the structural properties of starch components by the lack of an isoform of starch branching enzyme in rice seeds. J Biol Chem 268 (1993) 19084-19091
    • (1993) J Biol Chem , vol.268 , pp. 19084-19091
    • Mizuno, K.1    Kawasaki, T.2    Shimada, H.3    Satoh, H.4    Kobayashi, E.5    Okamura, S.6    Arai, Y.7    Baba, T.8
  • 29
    • 0027551838 scopus 로고
    • Branching of amylose by the branching isoenzymes of maize endosperm
    • Takeda Y., Guan H.P., and Preiss J. Branching of amylose by the branching isoenzymes of maize endosperm. Carbohydr Res 240 (1993) 253-263
    • (1993) Carbohydr Res , vol.240 , pp. 253-263
    • Takeda, Y.1    Guan, H.P.2    Preiss, J.3
  • 30
    • 0000361233 scopus 로고
    • Differentiation of the properties of the branching isozymes from maize endosperm
    • Guan H.-P., and Preiss J. Differentiation of the properties of the branching isozymes from maize endosperm. Plant Physiol 102 (1993) 1269-1273
    • (1993) Plant Physiol , vol.102 , pp. 1269-1273
    • Guan, H.-P.1    Preiss, J.2
  • 31
    • 0000586974 scopus 로고
    • Evidence for independent genetic control of the multiple forms of maize endosperm branching enzymes and starch synthases
    • Boyer C.D., and Preiss J. Evidence for independent genetic control of the multiple forms of maize endosperm branching enzymes and starch synthases. Plant Physiol 67 (1981) 1141-1145
    • (1981) Plant Physiol , vol.67 , pp. 1141-1145
    • Boyer, C.D.1    Preiss, J.2
  • 32
    • 0028889109 scopus 로고
    • Maize branching enzyme catalyzes the synthesis of glycogen-like polysaccharide in glgB deficient Escherichia coli
    • Guan H.P., Kuriki T., Sivak M.N., and Preiss J. Maize branching enzyme catalyzes the synthesis of glycogen-like polysaccharide in glgB deficient Escherichia coli. Proc Natl Acad Sci USA 92 (1995) 964-967
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 964-967
    • Guan, H.P.1    Kuriki, T.2    Sivak, M.N.3    Preiss, J.4
  • 33
    • 0028429952 scopus 로고
    • Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity and stability
    • Svensson B. Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity and stability. Plant Molec Biol 25 (1994) 141-157
    • (1994) Plant Molec Biol , vol.25 , pp. 141-157
    • Svensson, B.1
  • 34
    • 85012586970 scopus 로고
    • The regulation of the biosynthesis of α-1,4 glucans in bacteria and plants
    • Stadtmen E.R., and Horecker B.L. (Eds), Academic Press, New York
    • Preiss J. The regulation of the biosynthesis of α-1,4 glucans in bacteria and plants. In: Stadtmen E.R., and Horecker B.L. (Eds). Current Topics of Cellular Regulation, vol 1 (1969), Academic Press, New York 125-161
    • (1969) Current Topics of Cellular Regulation, vol 1 , pp. 125-161
    • Preiss, J.1
  • 35
    • 0014690480 scopus 로고
    • Biosynthesis of bacterial glycogen synthesis VII. Purification and properties of adenosine diphosphoglucose pyrophosphorylase of Rhodospirillum rubrum
    • Furlong C.E., and Preiss J. Biosynthesis of bacterial glycogen synthesis VII. Purification and properties of adenosine diphosphoglucose pyrophosphorylase of Rhodospirillum rubrum. J Biol Chem 244 (1969) 2539-2548
    • (1969) J Biol Chem , vol.244 , pp. 2539-2548
    • Furlong, C.E.1    Preiss, J.2
  • 36
    • 0020354745 scopus 로고
    • Biosynthesis of bacterial glycogen: purification and structural and immunological properties of Rhodopseudomonas sphaeroides ADPglucose synthetase
    • Yung S.-G., and Preiss J. Biosynthesis of bacterial glycogen: purification and structural and immunological properties of Rhodopseudomonas sphaeroides ADPglucose synthetase. J Bacteriol 151 (1982) 742-749
    • (1982) J Bacteriol , vol.151 , pp. 742-749
    • Yung, S.-G.1    Preiss, J.2
  • 37
    • 0014667235 scopus 로고
    • TPNH and pyridoxal-5′-phosphate: Activators of ADP-glucose pyrophosphorylase of Escherichia coli B
    • Gentner N., Greenberg E., and Preiss J. TPNH and pyridoxal-5′-phosphate: Activators of ADP-glucose pyrophosphorylase of Escherichia coli B. Biochem Biophys Res Commun 36 (1969) 373-380
    • (1969) Biochem Biophys Res Commun , vol.36 , pp. 373-380
    • Gentner, N.1    Greenberg, E.2    Preiss, J.3
  • 38
    • 0017106677 scopus 로고
    • ADP-glucose pyrophosphorylase: evidence for a lysine residue at the activator site of the Escherichia coli B enzyme
    • Haugen T., Ishaque A., and Preiss J. ADP-glucose pyrophosphorylase: evidence for a lysine residue at the activator site of the Escherichia coli B enzyme. Biochem Biophys Res Commun 69 (1976) 346-353
    • (1976) Biochem Biophys Res Commun , vol.69 , pp. 346-353
    • Haugen, T.1    Ishaque, A.2    Preiss, J.3
  • 39
    • 0018160620 scopus 로고
    • Biosynthesis of bacterial glycogen. Incorporation of pyridoxal phosphate into the allosteric activator site and an ADP-glucose-protected pyridoxal phosphate binding site of Escherichia coli B ADP-glucose synthase
    • Parsons T.F., and Preiss J. Biosynthesis of bacterial glycogen. Incorporation of pyridoxal phosphate into the allosteric activator site and an ADP-glucose-protected pyridoxal phosphate binding site of Escherichia coli B ADP-glucose synthase. J Biol Chem 253 (1978) 6197-6202
    • (1978) J Biol Chem , vol.253 , pp. 6197-6202
    • Parsons, T.F.1    Preiss, J.2
  • 40
    • 0018265510 scopus 로고
    • Biosynthesis of bacterial glycogen. Isolation and characterization of the pyridoxal-P allosteric activator site and the ADP-glucose protected pyridoxal-P binding site of Escherichia coli B ADP-glucose synthase
    • Parsons T.F., and Preiss J. Biosynthesis of bacterial glycogen. Isolation and characterization of the pyridoxal-P allosteric activator site and the ADP-glucose protected pyridoxal-P binding site of Escherichia coli B ADP-glucose synthase. J Biol Chem 253 (1978) 7638-7645
    • (1978) J Biol Chem , vol.253 , pp. 7638-7645
    • Parsons, T.F.1    Preiss, J.2
  • 41
    • 0024286506 scopus 로고
    • Affinity labeling of the allosteric activator site(s) of spinach leaf ADPglucose pyrophosphorylase
    • Morell M., Bloom M., and Preiss J. Affinity labeling of the allosteric activator site(s) of spinach leaf ADPglucose pyrophosphorylase. J Biol Chem 263 (1988) 633-637
    • (1988) J Biol Chem , vol.263 , pp. 633-637
    • Morell, M.1    Bloom, M.2    Preiss, J.3
  • 42
    • 0027971163 scopus 로고
    • Structure-function relationships of cyanobacterial ADP-glucose pyrophosphorylase: site-directed mutagenesis and chemical modification of the activator-binding sites of ADP-glucose pyrophosphorylase from Anabaena PCC 7120
    • Charng Y.-Y., Iglesias A.A., and Preiss J. Structure-function relationships of cyanobacterial ADP-glucose pyrophosphorylase: site-directed mutagenesis and chemical modification of the activator-binding sites of ADP-glucose pyrophosphorylase from Anabaena PCC 7120. J Biol Chem 269 (1994) 24107-24113
    • (1994) J Biol Chem , vol.269 , pp. 24107-24113
    • Charng, Y.-Y.1    Iglesias, A.A.2    Preiss, J.3
  • 43
    • 0025326951 scopus 로고
    • Escherichia coli E-39 ADPglucose synthetase has different activation kinetics from the wild-type allosteric enzyme
    • Gardiol A., and Preiss J. Escherichia coli E-39 ADPglucose synthetase has different activation kinetics from the wild-type allosteric enzyme. Arch Biochem Biophys 280 (1990) 175-180
    • (1990) Arch Biochem Biophys , vol.280 , pp. 175-180
    • Gardiol, A.1    Preiss, J.2
  • 44
    • 0028138290 scopus 로고
    • Allosteric sites of the large subunit of the spinach leaf adenosine diphosphate glucose pyrophosphorylase
    • Ball K.L., and Preiss J. Allosteric sites of the large subunit of the spinach leaf adenosine diphosphate glucose pyrophosphorylase. J Biol Chem 269 (1994) 24706-24711
    • (1994) J Biol Chem , vol.269 , pp. 24706-24711
    • Ball, K.L.1    Preiss, J.2
  • 45
    • 0023404070 scopus 로고
    • Biosynthesis of bacterial glycogen. Primary structure of Salmonella typhimurium ADPglucose synthetase as deduced from the nucleotide sequence of the glg C gene
    • Leung P., and Preiss J. Biosynthesis of bacterial glycogen. Primary structure of Salmonella typhimurium ADPglucose synthetase as deduced from the nucleotide sequence of the glg C gene. J Bacteriol 169 (1987) 4355-4360
    • (1987) J Bacteriol , vol.169 , pp. 4355-4360
    • Leung, P.1    Preiss, J.2
  • 46
    • 0022501240 scopus 로고
    • Cloning and expression of the Escherichia coli glg C gene from a mutant containing an ADPglucose pyrophosphorylase with altered allosteric properties
    • Leung P., Lee Y.M., Greenberg E., Esch K., Boylan S., and Preiss J. Cloning and expression of the Escherichia coli glg C gene from a mutant containing an ADPglucose pyrophosphorylase with altered allosteric properties. J Bacteriol 167 (1986) 82-88
    • (1986) J Bacteriol , vol.167 , pp. 82-88
    • Leung, P.1    Lee, Y.M.2    Greenberg, E.3    Esch, K.4    Boylan, S.5    Preiss, J.6
  • 47
    • 0024403428 scopus 로고
    • Biosynthesis of bacterial glycogen: determination of the amino acid changes that alter the regulatory properties of a mutant Escherichia coli ADPglucose synthetase
    • Kumar A., Ghosh P., Lee Y.M., Hill M.A., and Preiss J. Biosynthesis of bacterial glycogen: determination of the amino acid changes that alter the regulatory properties of a mutant Escherichia coli ADPglucose synthetase. J Biol Chem 264 (1989) 10464-10471
    • (1989) J Biol Chem , vol.264 , pp. 10464-10471
    • Kumar, A.1    Ghosh, P.2    Lee, Y.M.3    Hill, M.A.4    Preiss, J.5
  • 48
    • 0026703397 scopus 로고
    • Biosynthesis of bacterial glycogen: cloning, expression and nucleotide sequence of glg C gene from an allosteric mutant of Escherichia coli B
    • Ghosh P., Meyer C., Remy E., Peterson D., and Preiss J. Biosynthesis of bacterial glycogen: cloning, expression and nucleotide sequence of glg C gene from an allosteric mutant of Escherichia coli B. Arch Biochem Biophys 296 (1992) 122-128
    • (1992) Arch Biochem Biophys , vol.296 , pp. 122-128
    • Ghosh, P.1    Meyer, C.2    Remy, E.3    Peterson, D.4    Preiss, J.5
  • 49
    • 0026656459 scopus 로고
    • Cloning, expression and nucleotide sequence of a mutant glg C gene from Escherichia coli B; substitution of a proline to serine at position 295 results in altered allosteric properties of ADPGlc synthetase
    • Meyer C.R., Ghosh P., Remy E., and Preiss J. Cloning, expression and nucleotide sequence of a mutant glg C gene from Escherichia coli B; substitution of a proline to serine at position 295 results in altered allosteric properties of ADPGlc synthetase. J Bacteriol 174 (1992) 4509-4512
    • (1992) J Bacteriol , vol.174 , pp. 4509-4512
    • Meyer, C.R.1    Ghosh, P.2    Remy, E.3    Preiss, J.4
  • 50
    • 0027202593 scopus 로고
    • Cloning, expression and sequence of an allosteric mutant ADPglucose pyrophosphorylase from E. coli B
    • Meyer C.R., Ghosh P., Nadler S., and Preiss J. Cloning, expression and sequence of an allosteric mutant ADPglucose pyrophosphorylase from E. coli B. Arch Biochem Biophys 302 (1993) 64-71
    • (1993) Arch Biochem Biophys , vol.302 , pp. 64-71
    • Meyer, C.R.1    Ghosh, P.2    Nadler, S.3    Preiss, J.4
  • 51
    • 0017610784 scopus 로고
    • Biosynthesis of bacterial glycogen genetic and allosteric regulation of glycogen biosynthesis in Salmonella typhimurium LT.2
    • Steiner K.E., and Preiss J. Biosynthesis of bacterial glycogen genetic and allosteric regulation of glycogen biosynthesis in Salmonella typhimurium LT.2. J Bacteriol 129 (1977) 246-253
    • (1977) J Bacteriol , vol.129 , pp. 246-253
    • Steiner, K.E.1    Preiss, J.2
  • 52
    • 0003006270 scopus 로고
    • A Chlamydomonas reinhardtii low-starch mutant is defective for 3-phosphoglycerate activation and orthophosphate inhibition of ADPglucose pyrophosphorylase
    • Ball S., Marianne T., Dirick L., Fresnoy M., Delrue B., and Decq A. A Chlamydomonas reinhardtii low-starch mutant is defective for 3-phosphoglycerate activation and orthophosphate inhibition of ADPglucose pyrophosphorylase. Planta 185 (1991) 17-26
    • (1991) Planta , vol.185 , pp. 17-26
    • Ball, S.1    Marianne, T.2    Dirick, L.3    Fresnoy, M.4    Delrue, B.5    Decq, A.6
  • 53
    • 0000117374 scopus 로고
    • Control analysis of photosynthate partitioning: impact of reduced activity of ADPglucose pyrophosphorylase activity or plastid phosphoglucomutase on the fluxes to starch and sucrose in Arabidopsis
    • Neuhaus H.E., and Stitt M. Control analysis of photosynthate partitioning: impact of reduced activity of ADPglucose pyrophosphorylase activity or plastid phosphoglucomutase on the fluxes to starch and sucrose in Arabidopsis. Planta 182 (1990) 445-454
    • (1990) Planta , vol.182 , pp. 445-454
    • Neuhaus, H.E.1    Stitt, M.2
  • 55
    • 0002319467 scopus 로고
    • Control of metabolism
    • Davies D.D. (Ed), Academic Press, Inc., New York
    • Kacser H. Control of metabolism. In: Davies D.D. (Ed). The Biochemistry of Plants, vol 11 (1987), Academic Press, Inc., New York 39-67
    • (1987) The Biochemistry of Plants, vol 11 , pp. 39-67
    • Kacser, H.1
  • 57
    • 0000984370 scopus 로고
    • A starch deficient mutant of Arabidopsis thaliana with low ADPglucose activity lacks one of the two sununits of the enzyme
    • Lin T.P., Caspar T., Somerville C., and Preiss J. A starch deficient mutant of Arabidopsis thaliana with low ADPglucose activity lacks one of the two sununits of the enzyme. Plant Physiol 88 (1988) 1175-1181
    • (1988) Plant Physiol , vol.88 , pp. 1175-1181
    • Lin, T.P.1    Caspar, T.2    Somerville, C.3    Preiss, J.4
  • 58
    • 0012477911 scopus 로고
    • Alterations in growth, photosynthesis and respiration in a starch mutant of Arabidopsis thaliana (L.) Heynh deficient in chloroplast phosphoglucomutase activity
    • Caspar C., Huber S.C., and Somerville C. Alterations in growth, photosynthesis and respiration in a starch mutant of Arabidopsis thaliana (L.) Heynh deficient in chloroplast phosphoglucomutase activity. Plant Physiol 79 (1986) 1-7
    • (1986) Plant Physiol , vol.79 , pp. 1-7
    • Caspar, C.1    Huber, S.C.2    Somerville, C.3
  • 59
    • 0001481929 scopus 로고
    • Major differences in isoforms of starch branching enzyme between developing embryos of round and wrinkled-seeded peas (Pisum sativum L.)
    • Smith A.M. Major differences in isoforms of starch branching enzyme between developing embryos of round and wrinkled-seeded peas (Pisum sativum L.). Planta 175 (1988) 270-279
    • (1988) Planta , vol.175 , pp. 270-279
    • Smith, A.M.1
  • 60
    • 0000060178 scopus 로고
    • The impact of decreased activity of starch branching enzyme on photosynthetic starch synthesis in leaves of wrinkled-seeded peas
    • Smith A.M., Neuhaus H.E., and Stitt M. The impact of decreased activity of starch branching enzyme on photosynthetic starch synthesis in leaves of wrinkled-seeded peas. Planta 181 (1990) 310-315
    • (1990) Planta , vol.181 , pp. 310-315
    • Smith, A.M.1    Neuhaus, H.E.2    Stitt, M.3
  • 61
    • 0024970864 scopus 로고
    • Decreased-activity mutants of phosphoglucose isomerase in the cytosol and chloroplast of Clarkia xantiana. Impact on mass-action ratios and fluxes to sucrose and starch and estimation of flux control coefficients and elasticity coefficients
    • Kruckeberg A.L., Neuhaus H.E., Feil R., Gottlieb L.D., and Stitt M. Decreased-activity mutants of phosphoglucose isomerase in the cytosol and chloroplast of Clarkia xantiana. Impact on mass-action ratios and fluxes to sucrose and starch and estimation of flux control coefficients and elasticity coefficients. Biochem J 261 (1989) 457-467
    • (1989) Biochem J , vol.261 , pp. 457-467
    • Kruckeberg, A.L.1    Neuhaus, H.E.2    Feil, R.3    Gottlieb, L.D.4    Stitt, M.5
  • 63
    • 38249032437 scopus 로고
    • Activity of branching enzyme as a cardinal feature of the Ra locus in Pisum sativum
    • Edwards J., Green J.H., and Ap Rees T. Activity of branching enzyme as a cardinal feature of the Ra locus in Pisum sativum. Phytochem 27 (1988) 1615-1620
    • (1988) Phytochem , vol.27 , pp. 1615-1620
    • Edwards, J.1    Green, J.H.2    Ap Rees, T.3
  • 64
    • 0017946942 scopus 로고
    • Actions of glycogen synthase and phosphorylase of rabbit-skeletal muscle on modified glycogens
    • Carter J., and Smith E.E. Actions of glycogen synthase and phosphorylase of rabbit-skeletal muscle on modified glycogens. Carbohyd Res 61 (1978) 395-406
    • (1978) Carbohyd Res , vol.61 , pp. 395-406
    • Carter, J.1    Smith, E.E.2
  • 65
    • 34250076038 scopus 로고
    • Elevated temperature reduces starch deposition in wheat endosperm by reducing the activity of soluble starch synthase
    • Keeling P.L., Bacon P.J., and Holt D.C. Elevated temperature reduces starch deposition in wheat endosperm by reducing the activity of soluble starch synthase. Planta 191 (1993) 342-348
    • (1993) Planta , vol.191 , pp. 342-348
    • Keeling, P.L.1    Bacon, P.J.2    Holt, D.C.3
  • 67
    • 0002792852 scopus 로고
    • High temperature affects the activity of enzymes in the committed pathway of starch synthesis in developing wheat endosperm
    • Hawker J.S., and Jenner C.F. High temperature affects the activity of enzymes in the committed pathway of starch synthesis in developing wheat endosperm. Aust J Plant Physiol 20 (1993) 197-209
    • (1993) Aust J Plant Physiol , vol.20 , pp. 197-209
    • Hawker, J.S.1    Jenner, C.F.2
  • 68
    • 0003263599 scopus 로고
    • Starch synthesis in the kernel of wheat under high temperature conditions
    • Jenner C.F. Starch synthesis in the kernel of wheat under high temperature conditions. Aust J Plant Physiol 21 (1994) 791-806
    • (1994) Aust J Plant Physiol , vol.21 , pp. 791-806
    • Jenner, C.F.1
  • 69
    • 0000511670 scopus 로고
    • Heat stress during grain filling in maize: Effects on carbohydrate storage and metabolism
    • Singletary G.W., Banisadr R., and Keeling P.L. Heat stress during grain filling in maize: Effects on carbohydrate storage and metabolism. Aust J Plant Physiol 21 (1994) 829-841
    • (1994) Aust J Plant Physiol , vol.21 , pp. 829-841
    • Singletary, G.W.1    Banisadr, R.2    Keeling, P.L.3
  • 70
    • 0026458333 scopus 로고
    • Role of ADPglucose pyrophosphorylase in regulating starch levels in plant tissues
    • Stark D.M., Timmerman K.P., Barry G.F., and Preiss J Kishore G.M. Role of ADPglucose pyrophosphorylase in regulating starch levels in plant tissues. Science 258 (1992) 287-292
    • (1992) Science , vol.258 , pp. 287-292
    • Stark, D.M.1    Timmerman, K.P.2    Barry, G.F.3    Preiss J Kishore, G.M.4
  • 71
    • 0026533580 scopus 로고
    • Inhibition of ADPglucose pyrophosphorylase in transgenic potatoes leads to sugar-storing tubers and influences tuber formation and expression of tuber storage protein genes
    • Müller-Röber B.T., Sonnewald U., and Willmitzer L. Inhibition of ADPglucose pyrophosphorylase in transgenic potatoes leads to sugar-storing tubers and influences tuber formation and expression of tuber storage protein genes. EMBO J 11 (1992) 1229-1238
    • (1992) EMBO J , vol.11 , pp. 1229-1238
    • Müller-Röber, B.T.1    Sonnewald, U.2    Willmitzer, L.3
  • 72
    • 0007302858 scopus 로고
    • Goldberg I., and Williams R. (Eds), Van Nostrand Reinhold, New York
    • Katz F.R. In: Goldberg I., and Williams R. (Eds). Biotechnology and Food Ingredients (1991), Van Nostrand Reinhold, New York 315-326
    • (1991) Biotechnology and Food Ingredients , pp. 315-326
    • Katz, F.R.1


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