메뉴 건너뛰기




Volumn 1794, Issue 11, 2009, Pages 1709-1714

"Short-chain" α-1,4-glucan phosphorylase having a truncated N-terminal domain: Functional expression and characterization of the enzyme from Sulfolobus solfataricus

Author keywords

Dimer; Glycogen phosphorylase; Oligomerisation; Thermococcus kodakaraensis; Thermophilic enzyme

Indexed keywords

HOMODIMER; MONOMER; PHOSPHORYLASE; RECOMBINANT PROTEIN; TYROSINE DERIVATIVE;

EID: 70249146096     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.08.006     Document Type: Article
Times cited : (22)

References (42)
  • 3
    • 0038192506 scopus 로고    scopus 로고
    • Tracking interactions that stabilize the dimer structure of starch phosphorylase from Corynebacterium callunae. Roles of Arg234 and Arg242 revealed by sequence analysis and site-directed mutagenesis
    • Griessler R., Schwarz A., Mucha J., and Nidetzky B. Tracking interactions that stabilize the dimer structure of starch phosphorylase from Corynebacterium callunae. Roles of Arg234 and Arg242 revealed by sequence analysis and site-directed mutagenesis. Eur. J. Biochem. 270 (2003) 2126-2136
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2126-2136
    • Griessler, R.1    Schwarz, A.2    Mucha, J.3    Nidetzky, B.4
  • 4
    • 0031014875 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase
    • Watson K.A., Schinzel R., Palm D., and Johnson L.N. The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase. EMBO J. 16 (1997) 1-14
    • (1997) EMBO J. , vol.16 , pp. 1-14
    • Watson, K.A.1    Schinzel, R.2    Palm, D.3    Johnson, L.N.4
  • 5
    • 0025017865 scopus 로고
    • The role of pyridoxal 5′-phosphate in glycogen phosphorylase catalysis
    • Palm D., Klein H.W., Schinzel R., Buehner M., and Helmreich E.J. The role of pyridoxal 5′-phosphate in glycogen phosphorylase catalysis. Biochemistry 29 (1990) 1099-1107
    • (1990) Biochemistry , vol.29 , pp. 1099-1107
    • Palm, D.1    Klein, H.W.2    Schinzel, R.3    Buehner, M.4    Helmreich, E.J.5
  • 6
    • 0027145152 scopus 로고
    • Evolution of allosteric control in glycogen phosphorylase
    • Hudson J.W., Golding G.B., and Crerar M.M. Evolution of allosteric control in glycogen phosphorylase. J. Mol. Biol. 234 (1993) 700-721
    • (1993) J. Mol. Biol. , vol.234 , pp. 700-721
    • Hudson, J.W.1    Golding, G.B.2    Crerar, M.M.3
  • 8
    • 0026562948 scopus 로고
    • Glycogen phosphorylase: control by phosphorylation and allosteric effectors
    • Johnson L.N. Glycogen phosphorylase: control by phosphorylation and allosteric effectors. FASEB J. 6 (1992) 2274-2282
    • (1992) FASEB J. , vol.6 , pp. 2274-2282
    • Johnson, L.N.1
  • 9
    • 0026326962 scopus 로고
    • Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate
    • Sprang S.R., Withers S.G., Goldsmith E.J., Fletterick R.J., and Madsen N.B. Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate. Science 254 (1991) 1367-1371
    • (1991) Science , vol.254 , pp. 1367-1371
    • Sprang, S.R.1    Withers, S.G.2    Goldsmith, E.J.3    Fletterick, R.J.4    Madsen, N.B.5
  • 11
    • 0021964124 scopus 로고
    • Evolution of catalytic and regulatory sites in phosphorylases
    • Palm D., Goerl R., and Burger K.J. Evolution of catalytic and regulatory sites in phosphorylases. Nature 313 (1985) 500-502
    • (1985) Nature , vol.313 , pp. 500-502
    • Palm, D.1    Goerl, R.2    Burger, K.J.3
  • 12
    • 0037889501 scopus 로고
    • Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage
    • Newgard C.B., Nakano K., Hwang P.K., and Fletterick R.J. Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 8132-8136
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 8132-8136
    • Newgard, C.B.1    Nakano, K.2    Hwang, P.K.3    Fletterick, R.J.4
  • 13
    • 0030584682 scopus 로고    scopus 로고
    • The evolution of an allosteric site in phosphorylase
    • Rath V.L., Lin K., Hwang P.K., and Fletterick R.J. The evolution of an allosteric site in phosphorylase. Structure 4 (1996) 463-473
    • (1996) Structure , vol.4 , pp. 463-473
    • Rath, V.L.1    Lin, K.2    Hwang, P.K.3    Fletterick, R.J.4
  • 14
    • 0032438190 scopus 로고    scopus 로고
    • The stability of proteins in extreme environments
    • Jaenicke R., and Bohm G. The stability of proteins in extreme environments. Curr. Opin. Struct. Biol. 8 (1998) 738-748
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Bohm, G.2
  • 15
    • 0033003021 scopus 로고    scopus 로고
    • Maltose metabolism in the hyperthermophilic archaeon Thermococcus litoralis: purification and characterization of key enzymes
    • Xavier K.B., Peist R., Kossmann M., Boos W., and Santos H. Maltose metabolism in the hyperthermophilic archaeon Thermococcus litoralis: purification and characterization of key enzymes. J. Bacteriol. 181 (1999) 3358-3367
    • (1999) J. Bacteriol. , vol.181 , pp. 3358-3367
    • Xavier, K.B.1    Peist, R.2    Kossmann, M.3    Boos, W.4    Santos, H.5
  • 16
    • 57449098023 scopus 로고    scopus 로고
    • Recombinant production and biochemical characterization of a hyperthermostable α-glucan/maltodextrin phosphorylase from Pyrococcus furiosus
    • Mizanur R.M., Griffin A.K., and Pohl N.L. Recombinant production and biochemical characterization of a hyperthermostable α-glucan/maltodextrin phosphorylase from Pyrococcus furiosus. Archaea 2 (2008) 169-176
    • (2008) Archaea , vol.2 , pp. 169-176
    • Mizanur, R.M.1    Griffin, A.K.2    Pohl, N.L.3
  • 17
    • 37449008528 scopus 로고    scopus 로고
    • Unusual starch degradation pathway via cyclodextrins in the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324
    • Labes A., and Schonheit P. Unusual starch degradation pathway via cyclodextrins in the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus strain 7324. J. Bacteriol. 189 (2007) 8901-8913
    • (2007) J. Bacteriol. , vol.189 , pp. 8901-8913
    • Labes, A.1    Schonheit, P.2
  • 18
    • 0029995823 scopus 로고    scopus 로고
    • Purification and characterisation of an α-glucan phosphorylase from the thermophilic bacterium Thermus thermophilus
    • Boeck B., and Schinzel R. Purification and characterisation of an α-glucan phosphorylase from the thermophilic bacterium Thermus thermophilus. Eur. J. Biochem. 239 (1996) 150-155
    • (1996) Eur. J. Biochem. , vol.239 , pp. 150-155
    • Boeck, B.1    Schinzel, R.2
  • 19
    • 44649171718 scopus 로고    scopus 로고
    • Characterization of a glucan phosphorylase from the thermophilic archaeon Sulfolobus tokodaii strain 7
    • Hong Y., Wu L., Liu B., Peng C., Sheng D., JNi J., and Shen Y. Characterization of a glucan phosphorylase from the thermophilic archaeon Sulfolobus tokodaii strain 7. J. Mol. Cat. B:Enzymatic 54 (2008) 27-34
    • (2008) J. Mol. Cat. B:Enzymatic , vol.54 , pp. 27-34
    • Hong, Y.1    Wu, L.2    Liu, B.3    Peng, C.4    Sheng, D.5    JNi, J.6    Shen, Y.7
  • 20
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho P.M., Deleury E., Davies G.J., and Henrissat B. An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 328 (2003) 307-317
    • (2003) J. Mol. Biol. , vol.328 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 21
    • 8444239349 scopus 로고    scopus 로고
    • Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1
    • Atomi H., Fukui T., Kanai T., Morikawa M., and Imanaka T. Description of Thermococcus kodakaraensis sp. nov., a well studied hyperthermophilic archaeon previously reported as Pyrococcus sp. KOD1. Archaea 1 (2004) 263-267
    • (2004) Archaea , vol.1 , pp. 263-267
    • Atomi, H.1    Fukui, T.2    Kanai, T.3    Morikawa, M.4    Imanaka, T.5
  • 22
    • 0037071909 scopus 로고    scopus 로고
    • Integrated strategy for selective expanded bed ion-exchange adsorption and site-specific protein processing using gene fusion technology
    • Graslund T., Hedhammar M., Uhlen M., Nygren P.A., and Hober S. Integrated strategy for selective expanded bed ion-exchange adsorption and site-specific protein processing using gene fusion technology. J. Biotechnol. 96 (2002) 93-102
    • (2002) J. Biotechnol. , vol.96 , pp. 93-102
    • Graslund, T.1    Hedhammar, M.2    Uhlen, M.3    Nygren, P.A.4    Hober, S.5
  • 23
    • 34447617851 scopus 로고    scopus 로고
    • basic-a novel purification tag for efficient protein recovery
    • basic-a novel purification tag for efficient protein recovery. J. Chromatogr. A 1161 (2007) 22-28
    • (2007) J. Chromatogr. A , vol.1161 , pp. 22-28
    • Hedhammar, M.1    Hober, S.2
  • 24
    • 34250766201 scopus 로고    scopus 로고
    • The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins
    • Schmidt T.G., and Skerra A. The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat. Protoc. 2 (2007) 1528-1535
    • (2007) Nat. Protoc. , vol.2 , pp. 1528-1535
    • Schmidt, T.G.1    Skerra, A.2
  • 25
    • 0037215528 scopus 로고    scopus 로고
    • Targeted gene disruption by homologous recombination in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1
    • Sato T., Fukui T., Atomi H., and Imanaka T. Targeted gene disruption by homologous recombination in the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1. J. Bacteriol. 185 (2003) 210-220
    • (2003) J. Bacteriol. , vol.185 , pp. 210-220
    • Sato, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 26
    • 22144443201 scopus 로고    scopus 로고
    • Improved and versatile transformation system allowing multiple genetic manipulations of the hyperthermophilic archaeon Thermococcus kodakaraensis
    • Sato T., Fukui T., Atomi H., and Imanaka T. Improved and versatile transformation system allowing multiple genetic manipulations of the hyperthermophilic archaeon Thermococcus kodakaraensis. Appl. Environ. Microbiol. 71 (2005) 3889-3899
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 3889-3899
    • Sato, T.1    Fukui, T.2    Atomi, H.3    Imanaka, T.4
  • 27
    • 4344692495 scopus 로고    scopus 로고
    • Genetic evidence identifying the true gluconeogenic fructose-1, 6-bisphosphatase in Thermococcus kodakaraensis and other hyperthermophiles
    • Sato T., Imanaka H., Rashid N., Fukui T., Atomi H., and Imanaka T. Genetic evidence identifying the true gluconeogenic fructose-1, 6-bisphosphatase in Thermococcus kodakaraensis and other hyperthermophiles. J. Bacteriol. 186 (2004) 5799-5807
    • (2004) J. Bacteriol. , vol.186 , pp. 5799-5807
    • Sato, T.1    Imanaka, H.2    Rashid, N.3    Fukui, T.4    Atomi, H.5    Imanaka, T.6
  • 29
    • 0030867469 scopus 로고    scopus 로고
    • α-1,4-D-glucan phosphorylase of gram-positive Corynebacterium callunae: isolation, biochemical properties and molecular shape of the enzyme from solution X-ray scattering
    • Weinhausel A., Griessler R., Krebs A., Zipper P., Haltrich D., Kulbe K.D., and Nidetzky B. α-1,4-D-glucan phosphorylase of gram-positive Corynebacterium callunae: isolation, biochemical properties and molecular shape of the enzyme from solution X-ray scattering. Biochem. J. 326 (1997) 773-783
    • (1997) Biochem. J. , vol.326 , pp. 773-783
    • Weinhausel, A.1    Griessler, R.2    Krebs, A.3    Zipper, P.4    Haltrich, D.5    Kulbe, K.D.6    Nidetzky, B.7
  • 30
    • 0033565384 scopus 로고    scopus 로고
    • Characterization of trehalose phosphorylase from Schizophyllum commune
    • Eis C., and Nidetzky B. Characterization of trehalose phosphorylase from Schizophyllum commune. Biochem. J. 341 (1999) 385-393
    • (1999) Biochem. J. , vol.341 , pp. 385-393
    • Eis, C.1    Nidetzky, B.2
  • 32
    • 0034536389 scopus 로고    scopus 로고
    • Charge engineering of a protein domain to allow efficient ion-exchange recovery
    • Graslund T., Lundin G., Uhlen M., Nygren P.A., and Hober S. Charge engineering of a protein domain to allow efficient ion-exchange recovery. Protein Eng. 13 (2000) 703-709
    • (2000) Protein Eng. , vol.13 , pp. 703-709
    • Graslund, T.1    Lundin, G.2    Uhlen, M.3    Nygren, P.A.4    Hober, S.5
  • 33
    • 0028314030 scopus 로고
    • Enhanced in vitro refolding of insulin-like growth factor I using a solubilizing fusion partner
    • Samuelsson E., Moks T., Nilsson B., and Uhlen M. Enhanced in vitro refolding of insulin-like growth factor I using a solubilizing fusion partner. Biochemistry 33 (1994) 4207-4211
    • (1994) Biochemistry , vol.33 , pp. 4207-4211
    • Samuelsson, E.1    Moks, T.2    Nilsson, B.3    Uhlen, M.4
  • 34
    • 0014588495 scopus 로고
    • Fluorometric determination of pyridoxal phosphate in enzymes
    • Adams E. Fluorometric determination of pyridoxal phosphate in enzymes. Anal. Biochem. 31 (1969) 118-122
    • (1969) Anal. Biochem. , vol.31 , pp. 118-122
    • Adams, E.1
  • 35
    • 0015239160 scopus 로고
    • Fluorescence of glycogen phosphorylase b. Structural transitions and energy transfer
    • Cortijo M., Steinberg I.Z., and Shaltiel S. Fluorescence of glycogen phosphorylase b. Structural transitions and energy transfer. J. Biol. Chem. 246 (1971) 933-938
    • (1971) J. Biol. Chem. , vol.246 , pp. 933-938
    • Cortijo, M.1    Steinberg, I.Z.2    Shaltiel, S.3
  • 36
    • 0014938502 scopus 로고
    • The mode of binding of pyridoxal 5′-phosphate in glycogen phosphorylase
    • Shaltiel S., and Cortijo M. The mode of binding of pyridoxal 5′-phosphate in glycogen phosphorylase. Biochem. Biophys. Res. Commun. 41 (1970) 594-600
    • (1970) Biochem. Biophys. Res. Commun. , vol.41 , pp. 594-600
    • Shaltiel, S.1    Cortijo, M.2
  • 37
    • 0014133549 scopus 로고
    • Maltodextrin phosphorylase of Escherichia coli
    • Schwartz M., and Hofnung M. Maltodextrin phosphorylase of Escherichia coli. Eur. J. Biochem. 2 (1967) 132-145
    • (1967) Eur. J. Biochem. , vol.2 , pp. 132-145
    • Schwartz, M.1    Hofnung, M.2
  • 38
    • 0031978953 scopus 로고    scopus 로고
    • Purification and characterization of α-glucan phosphorylase from Bacillus stearothermophilus
    • Takata H., Takaha T., Okada S., Takagi M., and Imanaka T. Purification and characterization of α-glucan phosphorylase from Bacillus stearothermophilus. J. Ferment. Bioeng. 85 (1998) 156-161
    • (1998) J. Ferment. Bioeng. , vol.85 , pp. 156-161
    • Takata, H.1    Takaha, T.2    Okada, S.3    Takagi, M.4    Imanaka, T.5
  • 39
    • 0014500018 scopus 로고
    • Kinetic mechanism of maltodextrin phosphorylase
    • Chao J., Johnson G.F., and Graves D.J. Kinetic mechanism of maltodextrin phosphorylase. Biochemistry 8 (1969) 1459-1466
    • (1969) Biochemistry , vol.8 , pp. 1459-1466
    • Chao, J.1    Johnson, G.F.2    Graves, D.J.3
  • 40
    • 17644368570 scopus 로고    scopus 로고
    • Catalytic mechanism of α-retaining glucosyl transfer by Corynebacterium callunae starch phosphorylase: the role of histidine-334 examined through kinetic characterization of site-directed mutants
    • Schwarz A., Pierfederici F.M., and Nidetzky B. Catalytic mechanism of α-retaining glucosyl transfer by Corynebacterium callunae starch phosphorylase: the role of histidine-334 examined through kinetic characterization of site-directed mutants. Biochem. J. 387 (2005) 437-445
    • (2005) Biochem. J. , vol.387 , pp. 437-445
    • Schwarz, A.1    Pierfederici, F.M.2    Nidetzky, B.3
  • 41
    • 0036384359 scopus 로고    scopus 로고
    • Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase
    • Geremia S., Campagnolo M., Schinzel R., and Johnson L.N. Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase. J. Mol. Biol. 322 (2002) 413-423
    • (2002) J. Mol. Biol. , vol.322 , pp. 413-423
    • Geremia, S.1    Campagnolo, M.2    Schinzel, R.3    Johnson, L.N.4
  • 42
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones D.T. Protein secondary structure prediction based on position-specific scoring matrices. J. Mol. Biol. 292 (1999) 195-202
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.