최소 단어 이상 선택하여야 합니다.
최대 10 단어까지만 선택 가능합니다.
다음과 같은 기능을 한번의 로그인으로 사용 할 수 있습니다.
NTIS 바로가기Applied and environmental microbiology, v.73 no.12, 2007년, pp.3833 - 3837
Guillén, D. (Departamento de Biologí) , Santiago, M. (a Molecular y Biotecnologí) , Linares, L. (a, Instituto de Investigaciones Biomé) , Pérez, R. (dicas, Universidad Nacional Autó) , Morlon, J. (noma de Mé) , Ruiz, B. (xico, A.P. 70228, Ciudad Universitaria, Coyoacá) , Sánchez, S. (n 04510, Mé) , Rodríguez-Sanoja, R. (xico D.F., Mé)
ABSTRACT The Lactobacillus amylovorus alpha-amylase starch binding domain (SBD) is a functional domain responsible for binding to insoluble starch. Structurally, this domain is dissimilar from other reported SBDs because it is composed of five identical tandem modules of 91 amino acids each. To unde...
Belshaw, N.J., Williamson, G.. Production and purification of a granular-starch-binding domain of glucoamylase 1 from Aspergillus niger. FEBS letters, vol.269, no.2, 350-353.
Anal. Biochem. 580 82 1977 10.1016/0003-2697(77)90197-X Blakesley, R. W., and J. A. Boezi. 1977. A new staining technique for protein in polyacrylamide gels using Coomassie Brilliant Blue G-250. Anal. Biochem.82:580-582.
BOLAM, David N., CIRUELA, Antonio, McQUEEN-MASON, Simon, SIMPSON, Peter, WILLIAMSON, Michael P., RIXON, Jane E., BORASTON, Alisdair, HAZLEWOOD, Geoffrey P., GILBERT, Harry J.. Pseudomonas cellulose-binding domains mediate their effects by increasing enzyme substrate proximity. The Biochemical journal, vol.331, no.3, 775-781.
Biochemistry 2468 40 2001 10.1021/bi002564l Bolam, D. N., H. Xie, P. White, P. J. Simpson, S. M. Hancock, M. P. Williamson, and H. J. Gilbert. 2001. Evidence for synergy between family 2b carbohydrate binding modules in Cellulomonas fimi xylanase 11A. Biochemistry40:2468-2477.
J. Biol. Chem. 587 281 2006 10.1074/jbc.M509958200 Boraston, A. B., M. Healey, J. Klassen, E. Ficko-Blean, A. Lammerts van Bueren, and V. Law. 2006. A structural and functional analysis of α-glucan recognition by family 25 and 26 carbohydrate-binding modules reveals a conserved mode of starch recognition. J. Biol. Chem.281:587-598.
Mol. Microbiol. 187 43 2002 10.1046/j.1365-2958.2002.02730.x Boraston, A. B., B. W. McLean, G. Chen, A. Li, R. A. Warren, and D. G. Kilburn. 2002. Co-operative binding of triplicate carbohydrate binding modules from a thermophilic xylanase. Mol. Microbiol.43:187-194.
Bothwell, M.K., Daughhetee, S.D., Chaua, G.Y., Wilson, D.B., Walker, L.P.. Binding capacities for Thermomonospora fusca E3, E4 and E5, the E3 binding domain, and Trichoderma reesei CBHI on Avicel and bacterial microcrystalline cellulose. Bioresource technology : biomass, bioenergy, biowastes, conversion technologies, biotransformations, production technologies, vol.60, no.2, 169-178.
Combet, C., Blanchet, C., Geourjon, C., Deleage, G.. NPS@: Network Protein Sequence Analysis. Trends in biochemical sciences, vol.25, no.3, 147-150.
De MAN, J. C., ROGOSA, M., SHARPE, M. ELISABETH. A MEDIUM FOR THE CULTIVATION OF LACTOBACILLI. The Journal of applied bacteriology, vol.23, no.1, 130-135.
Appl. Biochem. Biotechnol. 721 84 2000 Florencio, J., D. Eiras-Stofella, C. Soccol, M. Raimbault, J. P. Guyot, and J. Fontana. 2000. Lactobacillus plantarum amylase acting on crude starch granules. Appl. Biochem. Biotechnol.84:721-730.
Gene 149 198 1997 10.1016/S0378-1119(97)00309-0 Giraud, E., and G. Cuny. 1997. Molecular characterization of the α-amylase genes of Lactobacillus plantarum A6 and Lactobacillus amylovorus reveals an unusual 3′ end structure with direct tandem repeats and suggests a common evolutionary origin. Gene198:149-157.
Eur. J. Biochem. 635 270 2003 10.1046/j.1432-1033.2003.03404.x Janeek, S., B. Svensson, and E. A. MacGregor. 2003. Relation between domain evolution, specificity, and taxonomy of the α-amylase family members containing a C-terminal starch binding-domain. Eur. J. Biochem.270:635-645.
Janeček, Štefan, Ševčı́k, Jozef. The evolution of starch-binding domain. FEBS letters, vol.456, no.1, 119-125.
Enzyme Microb. Technol. 675 10 1988 10.1016/0141-0229(88)90059-2 Kyriacou, A., R. Neufeld, and C. R. MacKenzie. 1988. Effect of physical parameters on the adsorption characteristics of fractionated Trichoderma reesei cellulase components. Enzyme Microb. Technol.10:675-681.
LAEMMLI, U. K.. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature, vol.227, no.5259, 680-685.
Biotechnol. Bioeng. 127 38 1991 10.1002/bit.260380204 Leloup, V. M., P. Colonna, and S. G. Ring. 1991. α-Amylase adsorption on starch crystallites. Biotechnol. Bioeng.38:127-134.
Linder, Markus, Salovuori, Irma, Ruohonen, Laura, Teeri, Tuula T.. Characterization of a Double Cellulose-binding Domain. The Journal of biological chemistry, vol.271, no.35, 21268-21272.
FEBS J. 5497 272 2005 10.1111/j.1742-4658.2005.04942.x Machovi, M., B. Svensson, E. A. MacGregor, and S. Janeek. 2005. A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21. FEBS J.272:5497-5513.
J. Chromatogr. A 148 1113 2006 10.1016/j.chroma.2006.02.001 Mihlbachler, K., M. A. De Jesus, K. Kaczmarski, M. J. Sepaniak, A. Seidel-Morgenstern, and G. Guiochon. 2006. Adsorption behavior of the (+/?)-Troger's base enantiomers in the phase system of a silica-based packing coated with amylose tri(3,5-dimethyl carbamate) and 2-propanol and molecular modeling interpretation. J. Chromatogr. A1113:148-161.
DNA Seq. 27 12 2001 10.3109/10425170109042048 Morlon-Guyot, J., F. Mucciolo-Roux, R. Rodriguez-Sanoja, and J. P. Guyot. 2001. Characterization of the L. manihotivorans α-amylase gene. DNA Seq.12:27-37.
Nölling, Jörk, Breton, Gary, Omelchenko, Marina V., Makarova, Kira S., Zeng, Qiandong, Gibson, Rene, Lee, Hong Mei, Dubois, JoAnn, Qiu, Dayong, Hitti, Joseph, Wolf, Yuri I., Tatusov, Roman L., Sabathe, Fabrice, Doucette-Stamm, Lynn, Soucaille, Philippe, Daly, Michael J., Bennett, George N., Koonin, Eugene V., Smith, Douglas R.. Genome Sequence and Comparative Analysis of the Solvent-Producing BacteriumClostridium acetobutylicum. Journal of bacteriology, vol.183, no.16, 4823-4838.
Rodriguez Sanoja, R., Morlon-Guyot, J., Jore, J., Pintado, J., Juge, N., Guyot, J. P.. Comparative Characterization of Complete and Truncated Forms of Lactobacillus amylovorus α-Amylase and Role of the C-Terminal Direct Repeats in Raw-Starch Binding. Applied and environmental microbiology, vol.66, no.8, 3350-3356.
Rodríguez-Sanoja, Romina, Oviedo, Norma, Sánchez, Sergio. Microbial starch-binding domain. Current opinion in microbiology, vol.8, no.3, 260-267.
Rodríguez-Sanoja, R., Ruiz, B., Guyot, J. P., Sanchez, S.. Starch-Binding Domain Affects Catalysis in Two Lactobacillus α-Amylases. Applied and environmental microbiology, vol.71, no.1, 297-302.
Molecular cloning: a laboratory manual 1989
Biologia (Bratisl.) 111 60 2005 Santiago, M., L. Linares, S. Sanchez, and R. Rodriguez-Sanoja. 2005. Functional characteristics of the starch binding domain of Lactobacillus amylovorus α-amylase. Biologia (Bratisl.)60:111-114.
SUMITANI, Jun-ichi, TOTTORI, Tadashi, KAWAGUCHI, Takashi, ARAI, Motoo. New type of starch-binding domain: the direct repeat motif in the C-terminal region of Bacillus sp. no. 195 α-amylase contributes to starch binding and raw starch degrading. The Biochemical journal, vol.350, no.2, 477-484.
Williamson, G, Belshaw, N J, Williamson, M P. O-glycosylation in Aspergillus glucoamylase. Conformation and role in binding. The Biochemical journal, vol.282, no.2, 423-428.
*원문 PDF 파일 및 링크정보가 존재하지 않을 경우 KISTI DDS 시스템에서 제공하는 원문복사서비스를 사용할 수 있습니다.
출판사/학술단체 등이 한시적으로 특별한 프로모션 또는 일정기간 경과 후 접근을 허용하여, 출판사/학술단체 등의 사이트에서 이용 가능한 논문
※ AI-Helper는 부적절한 답변을 할 수 있습니다.