User:Takatsugu Miyazaki

Takatsugu Miyazaki is an Assistant Professor of Research Institute of Green Science and Technology (RIGST) and Department of Agriculture, Graduate School of Integrated Science and Technology (GSST), at Shizuoka University. He obtained his PhD under the supervision of Takashi Tonozuka at Tokyo University of Agriculture and Technology. He is interested in structures and functions of CAZymes, especially glycoside hydrolases and glycosyltransferases from microorganisms and insects. He has contributed to the crystal structure determination of

• GH6 Coprinopsis cinerea cellobiohydrolase CcCel6C
• GH6 Coprinopsis cinerea cellobiohydrolase CcCel6A
• GH13_17 Bombyx mori sucrose hydrolase BmSUH
• GH16 Microbulbifer thermotolerans β-agarase
• GH27 Arthrobacter globiformis isomalto-dextranase
• GH31 Pseudopedobacter saltans α-galactosidase
• GH31 Enterococcus faecalis exo-acting protein-α-N-acetylgalactosaminidase
• GH31 Lactococcus lactis subsp. cremoris α-1,3-glucosidase
• GH32 Bombyx mori β-fructofuranosidase BmSUC1
• GH49 Aspergillus brasiliensis isopullulanase (N-glycan-deficient variant)
• GH62 Coprinopsis cinerea α-L-arabinofuranosidase CcAbf62A
• GH63 Escherichia coli α-glycosidase YgjK (glycosynthase mutant)
• GH63 Thermus thermophillus mannosylglycerate hydrolase
• GH65 Flavobacterium johnsoniae kojibiose hydrolase
• GH68 Microbacterium saccharophilum β-fructofuranosidase and its thermostabilized mutants
• GH92 Enterococcus faecalis α-1,2-mannosidase (Michaelis complex)
• GH131 Coprinopsis cinerea CcGH131A

• CBM94 C-terminal domains of Homo sapiens GT54 N-acetylglucosaminyltransferase IVa (GnT-IVa, MGAT4A) and Bombyx mori ortholog

He also has contributed to identification and characterization of

• GH29 Bombyx mori α-L-fucosidase
• GH31 Pedobacter heparinus α-galactosidase
• GH31 Flavobacterium johnsoniae dextranase
• GH31 Paenibacillus sp. 598K 6-α-glucosyltransferase
• GH31 Bombyx mori exo-acting protein-α-N-acetylgalactosaminidase
• GH31 Cordyceps militaris α-1,3-glucosidase
• GH63 Aspergillus brasiliensis mannosyloligosaccharide glucosidase
• GH65 Microbacterium dextranolyticum dextran α-1,2-debranching enzyme
• GH66 Paenibacillus sp. 598K dextranase
• GH99 Shewanella amazonensis endo-α-1,2-mannosidase

• GT7 Bombyx mori β-1,4-N-acetylgalactosaminyltransferase
• GT16 Homo sapiens β-1,2-N-acetylglucosaminyltransferase II recombinantly expressed in Bombyx mori
• GT16 Bombyx mori β-1,2-N-acetylglucosaminyltransferase II

• PL21 Pedobacter heparinus heparin lyase II (mutants)

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1. Liu Y, Yoshida M, Kurakata Y, Miyazaki T, Igarashi K, Samejima M, Fukuda K, Nishikawa A, and Tonozuka T. (2010). Crystal structure of a glycoside hydrolase family 6 enzyme, CcCel6C, a cellulase constitutively produced by Coprinopsis cinerea. FEBS J. 2010;277(6):1532-42. DOI:10.1111/j.1742-4658.2010.07582.x |
2. Tamura M, Miyazaki T, Tanaka Y, Yoshida M, Nishikawa A, and Tonozuka T. (2012). Comparison of the structural changes in two cellobiohydrolases, CcCel6A and CcCel6C, from Coprinopsis cinerea--a tweezer-like motion in the structure of CcCel6C. FEBS J. 2012;279(10):1871-82. DOI:10.1111/j.1742-4658.2012.08568.x |
3. Miyazaki T and Park EY. (2020). Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17 exo-α-glucosidases. J Biol Chem. 2020;295(26):8784-8797. DOI:10.1074/jbc.RA120.013595 |
4. Takagi E, Hatada Y, Akita M, Ohta Y, Yokoi G, Miyazaki T, Nishikawa A, and Tonozuka T. (2015). Crystal structure of the catalytic domain of a GH16 β-agarase from a deep-sea bacterium, Microbulbifer thermotolerans JAMB-A94. Biosci Biotechnol Biochem. 2015;79(4):625-32. DOI:10.1080/09168451.2014.988680 |
5. Gilbert HJ, Stålbrand H, and Brumer H. (2008). How the walls come crumbling down: recent structural biochemistry of plant polysaccharide degradation. Curr Opin Plant Biol. 2008;11(3):338-48. DOI:10.1016/j.pbi.2008.03.004 |
5. Gilbert HJ, Stålbrand H, and Brumer H. (2008). How the walls come crumbling down: recent structural biochemistry of plant polysaccharide degradation. Curr Opin Plant Biol. 2008;11(3):338-48. DOI:10.1016/j.pbi.2008.03.004 |