User:Zui Fujimoto

Zui FUJIMOTO is a research scientist in National Agriculture and Food Research Organization(NARO), Japan. He received his Ph.D. from the Graduate School of Agricultural and Life Sciences, The University of Tokyo. His research interests are the structural insights into protein functions of agricultural and food chemical use. He acts as a Responsible Curator for the Glycoside Hydrolase Family 66 (GH66) page. He has determined the crystal structures of

• GH10 endo-1,4-β-xylanase [1]
• GH13 α-amylase [2, 3]
• GH27 α-galactosidase [4, 5] and β-L-arabinopyranosidase [6]
• GH31 α-1,6-glucosyltransferase [7]

• GH43 exo-1,5-α-L-arabinofuranosidase [8]
• GH62 α-L-arabinofuranosidase [9]
• GH66 dextranase [10] and cycloisomaltooligosaccharide glucanotransferase[11],[12]
• GH78 α-L-rhamnosidase [13]
• GH79 β-glucuronidase [14]
• GT5 starch synthase [15]

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1. Fujimoto Z, Kuno A, Kaneko S, Yoshida S, Kobayashi H, Kusakabe I, and Mizuno H. (2000). Crystal structure of Streptomyces olivaceoviridis E-86 beta-xylanase containing xylan-binding domain. J Mol Biol. 2000;300(3):575-85. DOI:10.1006/jmbi.2000.3877 |
2. Fujimoto Z, Takase K, Doui N, Momma M, Matsumoto T, and Mizuno H. (1998). Crystal structure of a catalytic-site mutant alpha-amylase from Bacillus subtilis complexed with maltopentaose. J Mol Biol. 1998;277(2):393-407. DOI:10.1006/jmbi.1997.1599 |
3. Suvd D, Fujimoto Z, Takase K, Matsumura M, and Mizuno H. (2001). Crystal structure of Bacillus stearothermophilus alpha-amylase: possible factors determining the thermostability. J Biochem. 2001;129(3):461-8. DOI:10.1093/oxfordjournals.jbchem.a002878 |
4. Fujimoto Z, Kaneko S, Momma M, Kobayashi H, and Mizuno H. (2003). Crystal structure of rice alpha-galactosidase complexed with D-galactose. J Biol Chem. 2003;278(22):20313-8. DOI:10.1074/jbc.M302292200 |
5. Fujimoto Z, Kaneko S, Kim WD, Park GG, Momma M, and Kobayashi H. (2009). The tetramer structure of the glycoside hydrolase family 27 alpha-galactosidase I from Umbelopsis vinacea. Biosci Biotechnol Biochem. 2009;73(10):2360-4. DOI:10.1271/bbb.90604 |
6. Ichinose H, Fujimoto Z, Honda M, Harazono K, Nishimoto Y, Uzura A, and Kaneko S. (2009). A beta-l-Arabinopyranosidase from Streptomyces avermitilis is a novel member of glycoside hydrolase family 27. J Biol Chem. 2009;284(37):25097-106. DOI:10.1074/jbc.M109.022723 |
8. Fujimoto Z, Ichinose H, Maehara T, Honda M, Kitaoka M, and Kaneko S. (2010). Crystal structure of an Exo-1,5-{alpha}-L-arabinofuranosidase from Streptomyces avermitilis provides insights into the mechanism of substrate discrimination between exo- and endo-type enzymes in glycoside hydrolase family 43. J Biol Chem. 2010;285(44):34134-43. DOI:10.1074/jbc.M110.164251 |
9. Maehara T, Fujimoto Z, Ichinose H, Michikawa M, Harazono K, and Kaneko S. (2014). Crystal structure and characterization of the glycoside hydrolase family 62 α-L-arabinofuranosidase from Streptomyces coelicolor. J Biol Chem. 2014;289(11):7962-72. DOI:10.1074/jbc.M113.540542 |
10. Suzuki N, Kim YM, Fujimoto Z, Momma M, Okuyama M, Mori H, Funane K, and Kimura A. (2012). Structural elucidation of dextran degradation mechanism by streptococcus mutans dextranase belonging to glycoside hydrolase family 66. J Biol Chem. 2012;287(24):19916-26. DOI:10.1074/jbc.M112.342444 |
13. Fujimoto Z, Jackson A, Michikawa M, Maehara T, Momma M, Henrissat B, Gilbert HJ, and Kaneko S. (2013). The structure of a Streptomyces avermitilis α-L-rhamnosidase reveals a novel carbohydrate-binding module CBM67 within the six-domain arrangement. J Biol Chem. 2013;288(17):12376-85. DOI:10.1074/jbc.M113.460097 |
14. Michikawa M, Ichinose H, Momma M, Biely P, Jongkees S, Yoshida M, Kotake T, Tsumuraya Y, Withers SG, Fujimoto Z, and Kaneko S. (2012). Structural and biochemical characterization of glycoside hydrolase family 79 β-glucuronidase from Acidobacterium capsulatum. J Biol Chem. 2012;287(17):14069-77. DOI:10.1074/jbc.M112.346288 |
15. Momma M and Fujimoto Z. (2012). Interdomain disulfide bridge in the rice granule bound starch synthase I catalytic domain as elucidated by X-ray structure analysis. Biosci Biotechnol Biochem. 2012;76(8):1591-5. DOI:10.1271/bbb.120305 |