참고문헌
- Moon YH, Kim G, Lee JH, Jin XJ, Kim DW, Kim D. 2006. Enzymatic synthesis and characterization of novel epigallocatechin gallate glucosides. J. Mol. Catalysis B: Enzymatic. 40: 1-7. https://doi.org/10.1016/j.molcatb.2006.01.030
- Li D, Park JH, Park JT, Park CS, Park KH. 2004. Biotechnological production of highly soluble daidzein glycosides using Thermotoga maritima maltosyltransferase. J. Agric. Food Chem. 52: 2561-2567. https://doi.org/10.1021/jf035109f
- Bae HK, Lee SB, Park CS, Shim JH, Lee HY, Kim MJ, et al. 2002. Modification of ascorbic acid using transglycosylation activity of Bacillus stearothermophilus maltogenic amylase to enhance its oxidative stability. J. Agric.Food Chem. 50: 3309-3316. https://doi.org/10.1021/jf011550z
- Liang C, Zhang Y, Jia Y, Wenzhao W, Li Y, Lu S, et al. 2016. Engineering a carbohydrate-processing transglycosidase into glycosyltransferase for natural product glycodiversification. Sci. Rep. 6: 21051. https://doi.org/10.1038/srep21051
- Seo D-H, Yoo S-H, Choi S-J, Kim Y-R, Park C-S. 2020. Versatile biotechnological applications of amylosucrase, a novel glucosyltransferase. Food Sci. Biotechnol. 29: 1-16. https://doi.org/10.1007/s10068-019-00686-6
- Cho HK, Kim HH, Seo DH, Jung JH, Park JH, Baek NI, et al. 2011. Biosynthesis of (+)-catechin glycosides using recombinant amylosucrase from Deinococcus geothermalis DSM 11300. Enzyme Microb. Technol. 49: 246-253. https://doi.org/10.1016/j.enzmictec.2011.05.007
-
Seo DH, Jung JH, Ha SJ, Cho HK, Jung DH, Kim TJ, et al. 2012. High-yield enzymatic bioconversion of hydroquinone to
$\alpha$ -arbutin, a powerful skin lightening agent, by amylosucrase. Appl. Microbiol. Biotechnol. 94: 1189-1197. https://doi.org/10.1007/s00253-012-3905-7 -
Seo DH, Jung JH, Ha SJ, Song MC, Cha J, Yoo SH, et al. 2009. Highly selective biotransformation of arbutin to arbutin-
$\alpha$ -glucoside using amylosucrase from Deinococcus geothermalis DSM 11300. J. Mol. Catalysis B: Enzymatic. 60: 113-118. https://doi.org/10.1016/j.molcatb.2009.04.006 - Seo DH, Jung JH, Ha SJ, Yoo SH, Kim TJ, Cha J, et al. 2008. Molecular cloning of the amylosucrase gene from a moderate thermophilic bacterium Deinococcus geothermalis and analysis of its dual enzyme activity, pp. 125-140. In Park KH (ed.), Carbohydrate-active enzyme structure, function and application, Ed. CRC press, Boca Raton
- Jung JH, Seo DH, Ha SJ, Song MC, Cha J, Yoo SH, et al. 2009. Enzymatic synthesis of salicin glycosides through transglycosylation catalyzed by amylosucrases from Deinococcus geothermalis and Neisseria polysaccharea. Carbohydr. Res. 344: 1612-1619. https://doi.org/10.1016/j.carres.2009.04.019
- Kim KH, Park Y-D, Park H, Moon K-O, Ha K-T, Baek N-I, et al. 2014. Synthesis and biological evaluation of a novel baicalein glycoside as an anti-inflammatory agent. Eur. J. Pharmacol. 744: 147-156. https://doi.org/10.1016/j.ejphar.2014.10.013
-
Skov LK, Mirza O, Henriksen A, De Montalk GP, Remaud-Simeon M, Sarcabal P, et al. 2001. Amylosucrase, a glucan-synthesizing enzyme from the
$\alpha$ -amylase family. J. Biol. Chem. 276: 25273-25278. https://doi.org/10.1074/jbc.M010998200 - Guerin F, Barbe S, Pizzut-Serin S, Potocki-Veronese G, Guieysse D, Guillet V, et al. 2012. Structural Investigation of the thermostability and product specificity of amylosucrase from the bacterium Deinococcus geothermalis. J. Biol. Chem. 287: 6642-6654. https://doi.org/10.1074/jbc.M111.322917
- Seo DH, Jung JH, Jung DH, Park S, Yoo SH, Kim YR, et al. 2016. An unusual chimeric amylosucrase generated by domain-swapping mutagenesis. Enzyme Microb. Technol. 86: 7-16. https://doi.org/10.1016/j.enzmictec.2016.01.004
- Seo DH, Jung JH, Park CS. 2019. Improved polymerization activity of Deinococcus geothermalis amylosucrase by semi-rational design: Effect of loop flexibility on the polymerization reaction. Int. J. Biol. Macromol. 130: 177-185. https://doi.org/10.1016/j.ijbiomac.2019.02.139
- Hanwell MD, Curtis DE, Lonie DC, Vandermeersch T, Zurek E, Hutchison GR. 2012. Avogadro: an advanced semantic chemical editor, visualization, and analysis platform. J. Cheminform. 4: 17. https://doi.org/10.1186/1758-2946-4-17
- Salomon-Ferrer R, Case DA, Walker RC. 2013. An overview of the Amber biomolecular simulation package. Comput. Mol. Sci. 3: 198-210. https://doi.org/10.1002/wcms.1121
- Leaver-Fay A, Tyka M, Lewis SM, Lange OF, Thompson J, Jacak R, et al. 2011. Chapter nineteen - Rosetta3: An object-oriented software suite for the simulation and design of macromolecules, pp. 545-574. In Johnson ML, Brand L (eds.), Methods in Enzymology, Ed. Academic Press
- Abraham MJ, Murtola T, Schulz R, Páll S, Smith JC, Hess B, et al. 2015. GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers. SoftwareX 1-2: 19-25. https://doi.org/10.1016/j.softx.2015.06.001
- Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE, Belew RK, et al. 1998. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Computat. Chem. 19: 1639-1662. https://doi.org/10.1002/(SICI)1096-987X(19981115)19:14<1639::AID-JCC10>3.0.CO;2-B
- Trott O, Olson AJ. 2010. AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31: 455-461. https://doi.org/10.1002/jcc.21334
- Hunter JD. 2007. Matplotlib: A 2D Graphics Environment. Comput. Sci. Eng. 9: 90-95. https://doi.org/10.1109/MCSE.2007.55
-
Rha C-S, Jung YS, Seo D-H, Kim D-O, Park C-S. 2019. Site-specific
$\alpha$ -glycosylation of hydroxyflavones and hydroxyflavanones by amylosucrase from Deinococcus geothermalis. Enzyme Microb. Technol. 129: 109361. https://doi.org/10.1016/j.enzmictec.2019.109361 - Williams GJ, Zhang C, Thorson JS. 2007. Expanding the promiscuity of a natural-product glycosyltransferase by directed evolution. Nat. Chem. Biol. 3: 657-662. https://doi.org/10.1038/nchembio.2007.28
- Kim Y-W, Lee SS, Warren RAJ, Withers SG. 2004. Directed evolution of a glycosynthase from Agrobacterium sp. increases its catalytic activity dramatically and expands its substrate repertoire. J. Biol. Chem. 279: 42787-42793. https://doi.org/10.1074/jbc.M406890200
-
Seo D-H, Jung J-H, Ha S-J, Cho H-K, Jung D-H, Kim T-J, et al. 2012. High-yield enzymatic bioconversion of hydroquinone to
$\alpha$ -arbutin, a powerful skin lightening agent, by amylosucrase. Appl. Microbiol. Biotechnol. 94: 1189-1197. https://doi.org/10.1007/s00253-012-3905-7
피인용 문헌
- Biosynthesis of glyceride glycoside (nonionic surfactant) by amylosucrase, a powerful glycosyltransferase vol.30, pp.2, 2020, https://doi.org/10.1007/s10068-020-00861-0