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Volumn 65, Issue 1, 2006, Pages 27-31

Starch-synthase III family encodes a tandem of three starch-binding domains

Author keywords

Carbohydrate binding module family (CBM); Starch binding domain; Starch synthase III

Indexed keywords

STARCH; STARCH SYNTHASE; STARCH SYNTHASE III; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 33748273525     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21007     Document Type: Article
Times cited : (31)

References (44)
  • 1
    • 0142040430 scopus 로고    scopus 로고
    • From bacterial glycogen to starch: Understanding the biogenesis of the plant starch granule
    • Ball SG, Morell MK. From bacterial glycogen to starch: understanding the biogenesis of the plant starch granule. Annu Rev Plant Biol 2003;54:207-233.
    • (2003) Annu Rev Plant Biol , vol.54 , pp. 207-233
    • Ball, S.G.1    Morell, M.K.2
  • 2
    • 26944490008 scopus 로고    scopus 로고
    • Mutations affecting starch synthase III in Arabidopsis alter leaf starch structure and increase the rate of starch synthesis
    • Zhang X, Myers AM, James MG. Mutations affecting starch synthase III in Arabidopsis alter leaf starch structure and increase the rate of starch synthesis. Plant Physiol 2005;138:663-674.
    • (2005) Plant Physiol , vol.138 , pp. 663-674
    • Zhang, X.1    Myers, A.M.2    James, M.G.3
  • 4
    • 4444373841 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase: Homologous enzymes catalyze glycogen synthesis and degradation
    • Buschiazzo A, Ugalde JE, Guerin ME, Shepard W, Ugalde RA, Alzari PM. Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation. EMBO J 2004;23:3196-3205.
    • (2004) EMBO J , vol.23 , pp. 3196-3205
    • Buschiazzo, A.1    Ugalde, J.E.2    Guerin, M.E.3    Shepard, W.4    Ugalde, R.A.5    Alzari, P.M.6
  • 5
    • 0034089676 scopus 로고    scopus 로고
    • The structure and expression of the wheat starch synthase III gene. Motifs in the expressed gene define the lineage of the starch synthase III gene family
    • Li Z, Mouille G, Kosar-Hashemi B, Rahman S, Clarke B, Gale KR, Appels R, Morell MK. The structure and expression of the wheat starch synthase III gene. Motifs in the expressed gene define the lineage of the starch synthase III gene family. Plant Physiol 2000;123:613-624.
    • (2000) Plant Physiol , vol.123 , pp. 613-624
    • Li, Z.1    Mouille, G.2    Kosar-Hashemi, B.3    Rahman, S.4    Clarke, B.5    Gale, K.R.6    Appels, R.7    Morell, M.K.8
  • 6
    • 0344223437 scopus 로고    scopus 로고
    • The evolution of starch-binding domain
    • Janecek S, Sevcik J. The evolution of starch-binding domain. FEES Lett 1999;456:119-125.
    • (1999) FEES Lett , vol.456 , pp. 119-125
    • Janecek, S.1    Sevcik, J.2
  • 7
    • 0001849438 scopus 로고    scopus 로고
    • The modular structure of cellulases and other carbohydrate-active enzymes: An integrated database approach
    • Coutinho PM, Henrissat B. The modular structure of cellulases and other carbohydrate-active enzymes: an integrated database approach. Genet Biochem Ecol Cellulose Degradation 1999:15-23.
    • (1999) Genet Biochem Ecol Cellulose Degradation , pp. 15-23
    • Coutinho, P.M.1    Henrissat, B.2
  • 9
    • 0031570348 scopus 로고    scopus 로고
    • Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin
    • Sorimachi K, Le Gal-Coeffet MF, Williamson G, Archer DB, Williamson MP. Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin. Structure 1997;5:647-661.
    • (1997) Structure , vol.5 , pp. 647-661
    • Sorimachi, K.1    Le Gal-Coeffet, M.F.2    Williamson, G.3    Archer, D.B.4    Williamson, M.P.5
  • 11
    • 1542495429 scopus 로고    scopus 로고
    • Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 with maltooligosaccharides demonstrate the role of domain N acting as a starch-binding domain
    • Abe A, Tonozuka T, Sakano Y, Kamitori S. Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 1 with maltooligosaccharides demonstrate the role of domain N acting as a starch-binding domain. J Mol Biol 2004;335:811-822.
    • (2004) J Mol Biol , vol.335 , pp. 811-822
    • Abe, A.1    Tonozuka, T.2    Sakano, Y.3    Kamitori, S.4
  • 12
    • 0031934403 scopus 로고    scopus 로고
    • Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermotoga maritima
    • Bibel M, Brettl C, Gosslar U, Kriegshauser G, Liebl W. Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermotoga maritima. FEMS Microbiol Lett 1998;158:9-15.
    • (1998) FEMS Microbiol Lett , vol.158 , pp. 9-15
    • Bibel, M.1    Brettl, C.2    Gosslar, U.3    Kriegshauser, G.4    Liebl, W.5
  • 13
    • 0030729996 scopus 로고    scopus 로고
    • Glucoamylase structural, functional, and evolutionary relationships
    • Coutinho PM, Reilly PJ. Glucoamylase structural, functional, and evolutionary relationships. Proteins 97;29:334-347.
    • Proteins , vol.97 , Issue.29 , pp. 334-347
    • Coutinho, P.M.1    Reilly, P.J.2
  • 14
    • 0034283404 scopus 로고    scopus 로고
    • New type of starch-binding domain: The direct repeat motif in the C-terminal region of Bacillus sp. no. 195 alpha-amylase contributes to starch binding and raw starch degrading
    • Sumitani J, Tottori T, Kawaguchi T, Arai M. New type of starch-binding domain: the direct repeat motif in the C-terminal region of Bacillus sp. no. 195 alpha-amylase contributes to starch binding and raw starch degrading. Biochem J 2000;350:477-484.
    • (2000) Biochem J , vol.350 , pp. 477-484
    • Sumitani, J.1    Tottori, T.2    Kawaguchi, T.3    Arai, M.4
  • 16
    • 0036855905 scopus 로고    scopus 로고
    • A motif of a microbial starch-binding domain found in human genethonin
    • Janecek, S. A motif of a microbial starch-binding domain found in human genethonin. Bioinformatics 2002;18:1534-1537.
    • (2002) Bioinformatics , vol.18 , pp. 1534-1537
    • Janecek, S.1
  • 18
    • 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, Williamson G. Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose. J Mol Biol 2001;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
  • 22
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 24
    • 0029595442 scopus 로고
    • SOPMA: Significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • Geourjon C, Deleage G. SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments. Comput Appl Biosci 1995;11:681-684.
    • (1995) Comput Appl Biosci , vol.11 , pp. 681-684
    • Geourjon, C.1    Deleage, G.2
  • 25
    • 0028501914 scopus 로고
    • Non-globular domains in protein sequences: Automated segmentation using complexity measures
    • Wooton J. Non-globular domains in protein sequences: automated segmentation using complexity measures. Comput Chem 1994;18:269-285.
    • (1994) Comput Chem , vol.18 , pp. 269-285
    • Wooton, J.1
  • 27
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM. The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci 1992;8:275-282.
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 28
    • 15844406550 scopus 로고    scopus 로고
    • HyPhy: Hypothesis testing using phytogenies
    • Pond SL, Frost SD, Muse SV. HyPhy: hypothesis testing using phytogenies. Bioinformatics 2005;21:676-679.
    • (2005) Bioinformatics , vol.21 , pp. 676-679
    • Pond, S.L.1    Frost, S.D.2    Muse, S.V.3
  • 30
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley LA, MacCallum RM, Sternberg MJ. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J Mol Biol 2000;299:499-520.
    • (2000) J Mol Biol , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 31
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J, Blundell TL, Mizuguchi K. FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 2001;310:243-257.
    • (2001) J Mol Biol , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 33
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993;234:779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 34
    • 0034843745 scopus 로고    scopus 로고
    • Easier threading through web-based comparisons and cross-validations
    • Douguet D, Labesse G. Easier threading through web-based comparisons and cross-validations. Bioinformatics 2001;17:752-753.
    • (2001) Bioinformatics , vol.17 , pp. 752-753
    • Douguet, D.1    Labesse, G.2
  • 35
    • 0031680752 scopus 로고    scopus 로고
    • Incremental threading optimization (TITO) to help alignment and modelling of remote homologues
    • Labesse G, Mornon J. Incremental threading optimization (TITO) to help alignment and modelling of remote homologues. Bioinformatics 1998;14:206-211.
    • (1998) Bioinformatics , vol.14 , pp. 206-211
    • Labesse, G.1    Mornon, J.2
  • 36
    • 0032506030 scopus 로고    scopus 로고
    • Large-scale protein structure modeling of the Saccharomyces cerevisiae genome
    • Sanchez R, Sali A. Large-scale protein structure modeling of the Saccharomyces cerevisiae genome. Proc Natl Acad Sci U S A 1998;95:13597-13602.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 13597-13602
    • Sanchez, R.1    Sali, A.2
  • 37
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl MJ. Recognition of errors in three-dimensional structures of proteins. Proteins 1993;17:355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 38
    • 0029775624 scopus 로고    scopus 로고
    • Clusters of charged residues in protein three-dimensional structures
    • Zhu ZY, Karlin S. Clusters of charged residues in protein three-dimensional structures. Proc Natl Acad Sci U S A 1996;93:8350-8355.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 8350-8355
    • Zhu, Z.Y.1    Karlin, S.2
  • 39
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin AG, Brenner SE, Hubbard T, Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 1995;247:536-540.
    • (1995) J Mol Biol , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 44
    • 0024430052 scopus 로고
    • Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes
    • Svensson B, Jespersen H, Sierks MR, MacGregor EA. Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes. Biochem J 1989;264:309-311.
    • (1989) Biochem J , vol.264 , pp. 309-311
    • Svensson, B.1    Jespersen, H.2    Sierks, M.R.3    MacGregor, E.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.