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Volumn 590, Issue 1, 2016, Pages 118-128

Plant α-glucan phosphatases SEX4 and LSF2 display different affinity for amylopectin and amylose

Author keywords

affinity gel electrophoresis; carbohydrate binding domain; Like Sex Four2; Starch Excess 4; surface binding sites; surface plasmon resonance

Indexed keywords

ALPHA GLUCAN PHOSPHATASE; AMYLOPECTIN; AMYLOSE; BETA CYCLODEXTRIN; LIKE SEX FOUR2 PROTEIN; MUTANT PROTEIN; PHOSPHATASE; STARCH EXCESS 4 PROTEIN; UNCLASSIFIED DRUG; VEGETABLE PROTEIN; ARABIDOPSIS PROTEIN; BETA CYCLODEXTRIN DERIVATIVE; DUAL SPECIFICITY PHOSPHATASE; LSF2 PROTEIN, ARABIDOPSIS; RECOMBINANT PROTEIN; SEX4 PROTEIN, ARABIDOPSIS;

EID: 84955557966     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1002/1873-3468.12027     Document Type: Article
Times cited : (17)

References (52)
  • 1
    • 77956377452 scopus 로고    scopus 로고
    • The molecular structures of starch components and their contribution to the architecture of starch granules: A comprehensive review
    • Pérez S, and, Bertoft E, (2010) The molecular structures of starch components and their contribution to the architecture of starch granules: a comprehensive review. Starch - Stärke 62, 389-420.
    • (2010) Starch - Stärke , vol.62 , pp. 389-420
    • Pérez, S.1    Bertoft, E.2
  • 2
    • 84880570732 scopus 로고    scopus 로고
    • Starch metabolism in Arabidopsis
    • Streb S, and, Zeeman SC, (2012) Starch metabolism in Arabidopsis. Arabidopsis Book 10, e0160.
    • (2012) Arabidopsis Book , vol.10
    • Streb, S.1    Zeeman, S.C.2
  • 3
    • 0000329882 scopus 로고
    • Multi-branched nature of amylose and the action of debranching enzymes
    • Zuicuri H, (1981) Multi-branched nature of amylose and the action of debranching enzymes. Carbohydr Res 94, 205-213.
    • (1981) Carbohydr Res , vol.94 , pp. 205-213
    • Zuicuri, H.1
  • 5
    • 14744269983 scopus 로고    scopus 로고
    • Identification of a novel enzyme required for starch metabolism in Arabidopsis leaves. The phosphoglucan, water dikinase
    • Kötting O, Pusch K, Tiessen A, Geigenberger P, Steup M, and, Ritte G, (2005) Identification of a novel enzyme required for starch metabolism in Arabidopsis leaves. The phosphoglucan, water dikinase. Plant Physiol 137, 242-252.
    • (2005) Plant Physiol , vol.137 , pp. 242-252
    • Kötting, O.1    Pusch, K.2    Tiessen, A.3    Geigenberger, P.4    Steup, M.5    Ritte, G.6
  • 7
    • 17944366026 scopus 로고    scopus 로고
    • The Arabidopsis sex1 mutant is defective in the R1 protein, a general regulator of starch degradation in plants, and not in the chloroplast hexose transporter
    • Yu TS, Kofler H, Häusler RE, Hille D, Flügge UI, Zeeman SC, Smith AM, Kossmann J, Lloyd J, Ritte G, et al. (2001) The Arabidopsis sex1 mutant is defective in the R1 protein, a general regulator of starch degradation in plants, and not in the chloroplast hexose transporter. Plant Cell 13, 1907-1918.
    • (2001) Plant Cell , vol.13 , pp. 1907-1918
    • Yu, T.S.1    Kofler, H.2    Häusler, R.E.3    Hille, D.4    Flügge, U.I.5    Zeeman, S.C.6    Smith, A.M.7    Kossmann, J.8    Lloyd, J.9    Ritte, G.10
  • 8
    • 0032004183 scopus 로고    scopus 로고
    • The degree of starch phosphorylation is related to the chain length distribution of the neutral and the phosphorylated chains of amylopectin
    • Blennow A, Bay-Smidt AM, Wischmann B, Olsen CE, and, Møller BL, (1998) The degree of starch phosphorylation is related to the chain length distribution of the neutral and the phosphorylated chains of amylopectin. Carbohydr Res 307, 45-54.
    • (1998) Carbohydr Res , vol.307 , pp. 45-54
    • Blennow, A.1    Bay-Smidt, A.M.2    Wischmann, B.3    Olsen, C.E.4    Møller, B.L.5
  • 9
    • 77950519125 scopus 로고    scopus 로고
    • Helix-breaking news: Fighting crystalline starch energy deposits in the cell
    • Blennow A, and, Engelsen SB, (2010) Helix-breaking news: fighting crystalline starch energy deposits in the cell. Trends Plant Sci 15, 236-240.
    • (2010) Trends Plant Sci , vol.15 , pp. 236-240
    • Blennow, A.1    Engelsen, S.B.2
  • 10
    • 77951222409 scopus 로고    scopus 로고
    • First principles insight into the α-glucan structures of starch: Their synthesis, conformation, and hydration
    • Damager I, Engelsen SB, Blennow A, Møller BL, and, Motawia MS, (2010) First principles insight into the α-glucan structures of starch: their synthesis, conformation, and hydration. Chem Rev 110, 2049-2080.
    • (2010) Chem Rev , vol.110 , pp. 2049-2080
    • Damager, I.1    Engelsen, S.B.2    Blennow, A.3    Møller, B.L.4    Motawia, M.S.5
  • 13
    • 75949119507 scopus 로고    scopus 로고
    • The laforin-like dual-specificity phosphatase SEX4 from Arabidopsis hydrolyzes both C6 -and C3-phosphate esters introduced by starch-related dikinases and thereby affects phase transition of α-glucans
    • Hejazi M, Fettke J, Kötting O, Zeeman SC, and, Steup M, (2010) The laforin-like dual-specificity phosphatase SEX4 from Arabidopsis hydrolyzes both C6- and C3-phosphate esters introduced by starch-related dikinases and thereby affects phase transition of α-glucans. Plant Physiol 152, 711-722.
    • (2010) Plant Physiol , vol.152 , pp. 711-722
    • Hejazi, M.1    Fettke, J.2    Kötting, O.3    Zeeman, S.C.4    Steup, M.5
  • 16
    • 84887979987 scopus 로고    scopus 로고
    • Surface binding sites in carbohydrate active enzymes: An emerging picture of structural and functional diversity
    • (Rauter P and Lindhorst T, eds) The Royal Society of Chemistry, Cambrigde
    • Cockburn D, and, Svensson B, (2013) Surface binding sites in carbohydrate active enzymes: an emerging picture of structural and functional diversity. In Carbohydrate Chemistry, Vol. 39 (Rauter P and Lindhorst T, eds), pp. 204-221. The Royal Society of Chemistry, Cambrigde.
    • (2013) Carbohydrate Chemistry , vol.39 , pp. 204-221
    • Cockburn, D.1    Svensson, B.2
  • 17
    • 80054923047 scopus 로고    scopus 로고
    • Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases
    • Cuyvers S, Dornez E, Delcour JA, and, Courtin CM, (2011) Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases. Crit Rev Biotechnol 31, 93-107.
    • (2011) Crit Rev Biotechnol , vol.31 , pp. 93-107
    • Cuyvers, S.1    Dornez, E.2    Delcour, J.A.3    Courtin, C.M.4
  • 21
    • 33646236579 scopus 로고    scopus 로고
    • Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain
    • Sevcík J, Hostinová E, Solovicová A, Gasperík J, Dauter Z, and, Wilson KS, (2006) Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain. FEBS J 273, 2161-2171.
    • (2006) FEBS J , vol.273 , pp. 2161-2171
    • Sevcík, J.1    Hostinová, E.2    Solovicová, A.3    Gasperík, J.4    Dauter, Z.5    Wilson, K.S.6
  • 22
    • 84905991993 scopus 로고    scopus 로고
    • Crystal structure of the Chlamydomonas starch debranching enzyme isoamylase ISA1 reveals insights into the mechanism of branch trimming and complex assembly
    • Sim L, Beeren SR, Findinier J, Dauvillée D, Ball S, Henriksen A, and, Palcic MM, (2014) Crystal structure of the Chlamydomonas starch debranching enzyme isoamylase ISA1 reveals insights into the mechanism of branch trimming and complex assembly. J Biol Chem 289, 22991-23003.
    • (2014) J Biol Chem , vol.289 , pp. 22991-23003
    • Sim, L.1    Beeren, S.R.2    Findinier, J.3    Dauvillée, D.4    Ball, S.5    Henriksen, A.6    Palcic, M.M.7
  • 23
    • 84907510438 scopus 로고    scopus 로고
    • Selectivity of the surface binding site (SBS) on barley starch synthase I
    • Wilkens C, Cuesta-Seijo JA, Palcic M, and, Svensson B, (2014) Selectivity of the surface binding site (SBS) on barley starch synthase I. Biologia (Bratisl) 69, 1118-1121.
    • (2014) Biologia (Bratisl) , vol.69 , pp. 1118-1121
    • Wilkens, C.1    Cuesta-Seijo, J.A.2    Palcic, M.3    Svensson, B.4
  • 27
    • 0015423088 scopus 로고
    • Dissociation constants of glucan phosphorylases gel of rabbit tissue studied by polyacrylamide gel disc electrophoresis
    • Takeo K, and, Nakamura S, (1972) Dissociation constants of glucan phosphorylases gel of rabbit tissue studied by polyacrylamide gel disc electrophoresis. Arch Biochem Biophys 153, 1-7.
    • (1972) Arch Biochem Biophys , vol.153 , pp. 1-7
    • Takeo, K.1    Nakamura, S.2
  • 28
    • 84864473993 scopus 로고    scopus 로고
    • H++ 3.0: Automating pK prediction and the preparation of biomolecular structures for atomistic molecular modeling and simulations
    • Anandakrishnan R, Aguilar B, and, Onufriev AV, (2012) H++ 3.0: automating pK prediction and the preparation of biomolecular structures for atomistic molecular modeling and simulations. Nucleic Acids Res 40, 537-541.
    • (2012) Nucleic Acids Res , vol.40 , pp. 537-541
    • Anandakrishnan, R.1    Aguilar, B.2    Onufriev, A.V.3
  • 30
    • 84955609300 scopus 로고    scopus 로고
    • last accessed 15 December 2015
    • Web server Version 3.2. http://biophysics.cs.vt.edu/H++. (last accessed 15 December 2015)
    • Web Server Version 3.2
  • 31
    • 33646794930 scopus 로고    scopus 로고
    • Crystal structure and putative function of small toprim domain-containing protein from Bacillus stearothermophilus
    • Myers JB, Grothause G, Narayanan S, and, Onufriev A, (2006) Crystal structure and putative function of small toprim domain-containing protein from Bacillus stearothermophilus. Proteins 63, 928-938.
    • (2006) Proteins , vol.63 , pp. 928-938
    • Myers, J.B.1    Grothause, G.2    Narayanan, S.3    Onufriev, A.4
  • 35
    • 3142714765 scopus 로고    scopus 로고
    • Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulation
    • Mackerell AD, Feig M, and, Brooks CL, (2004) Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulation. J Comput Chem 25, 1400-1415.
    • (2004) J Comput Chem , vol.25 , pp. 1400-1415
    • Mackerell, A.D.1    Feig, M.2    Brooks, C.L.3
  • 38
    • 33751157933 scopus 로고
    • Solvent-induced forces between two hydrophilic groups
    • Durell SR, Brooks BR, and, Ben-Naim A, (1994) Solvent-induced forces between two hydrophilic groups. J Phys Chem 98, 2198-2202.
    • (1994) J Phys Chem , vol.98 , pp. 2198-2202
    • Durell, S.R.1    Brooks, B.R.2    Ben-Naim, A.3
  • 41
    • 74549127543 scopus 로고    scopus 로고
    • Dynamics of starch granule biogenesis - The role of redox-regulated enzymes and low-affinity carbohydrate-binding modules
    • Blennow A, and, Svensson B, (2010) Dynamics of starch granule biogenesis-the role of redox-regulated enzymes and low-affinity carbohydrate-binding modules. Biocatal Biotransform 28, 3-9.
    • (2010) Biocatal Biotransform , vol.28 , pp. 3-9
    • Blennow, A.1    Svensson, B.2
  • 42
    • 33645670615 scopus 로고    scopus 로고
    • A novel type carbohydrate-binding module identified in α-glucan, water dikinases is specific for regulated plastidial starch metabolism
    • Mikkelsen R, Suszkiewicz K, and, Blennow A, (2006) A novel type carbohydrate-binding module identified in α-glucan, water dikinases is specific for regulated plastidial starch metabolism. Biochemistry 45, 4674-4682.
    • (2006) Biochemistry , vol.45 , pp. 4674-4682
    • Mikkelsen, R.1    Suszkiewicz, K.2    Blennow, A.3
  • 45
    • 0035834494 scopus 로고    scopus 로고
    • Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose
    • Giardina T, Gunning AP, Juge N, Faulds CB, Furniss CS, Svensson B, Morris VJ, and, Williamson G, (2001) Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose. J Mol Biol 313, 1149-1159.
    • (2001) J Mol Biol , vol.313 , pp. 1149-1159
    • Giardina, T.1    Gunning, A.P.2    Juge, N.3    Faulds, C.B.4    Furniss, C.S.5    Svensson, B.6    Morris, V.J.7    Williamson, G.8
  • 47
    • 77951951973 scopus 로고    scopus 로고
    • Feature-incorporated alignment based ligand-binding residue prediction for carbohydrate-binding modules
    • Chou W-Y, Chou W-I, Pai T-W, Lin S-C, Jiang T-Y, Tang C-Y, and, Chang MD-T, (2010) Feature-incorporated alignment based ligand-binding residue prediction for carbohydrate-binding modules. Bioinformatics 26, 1022-1028.
    • (2010) Bioinformatics , vol.26 , pp. 1022-1028
    • Chou, W.-Y.1    Chou, W.-I.2    Pai, T.-W.3    Lin, S.-C.4    Jiang, T.-Y.5    Tang, C.-Y.6    Chang, M.D.-T.7
  • 48
  • 49
    • 1942424149 scopus 로고    scopus 로고
    • Two additional carbohydrate-binding sites of β-amylase from Bacillus cereus var. mycoides are involved in hydrolysis and raw starch-binding
    • Ye Z, Miyake H, Tatsumi M, Nishimura S, and, Nitta Y, (2004) Two additional carbohydrate-binding sites of β-amylase from Bacillus cereus var. mycoides are involved in hydrolysis and raw starch-binding. J Biochem 135, 355-363.
    • (2004) J Biochem , vol.135 , pp. 355-363
    • Ye, Z.1    Miyake, H.2    Tatsumi, M.3    Nishimura, S.4    Nitta, Y.5
  • 50
    • 0038629280 scopus 로고    scopus 로고
    • Crystal structure of a catalytic site mutant of β-amylase from Bacillus cereus var. mycoides cocrystallized with maltopentaose
    • Miyake H, Kurisu G, Kusunoki M, Nishimura S, Kitamura S, and, Nitta Y, (2003) Crystal structure of a catalytic site mutant of β-amylase from Bacillus cereus var. mycoides cocrystallized with maltopentaose. Biochemistry 42, 5574-5581.
    • (2003) Biochemistry , vol.42 , pp. 5574-5581
    • Miyake, H.1    Kurisu, G.2    Kusunoki, M.3    Nishimura, S.4    Kitamura, S.5    Nitta, Y.6
  • 52
    • 0029931070 scopus 로고    scopus 로고
    • Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 Å resolution. Implications for product specificity
    • Strokopytov B, Knegtel RM, Penninga D, Rozeboom HJ, Kalk KH, Dijkhuizen L, and, Dijkstra BW, (1996) Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 Å resolution. Implications for product specificity. Biochemistry 35, 4241-4249.
    • (1996) Biochemistry , vol.35 , pp. 4241-4249
    • Strokopytov, B.1    Knegtel, R.M.2    Penninga, D.3    Rozeboom, H.J.4    Kalk, K.H.5    Dijkhuizen, L.6    Dijkstra, B.W.7


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