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]

---

Error fetching PMID 10884353:
Error fetching PMID 9514750:
Error fetching PMID 11226887:
Error fetching PMID 12657636:
Error fetching PMID 19809163:
Error fetching PMID 19608743:
Error fetching PMID 22337884:
Error fetching PMID 22367201:
Error fetching PMID 22878205:
Error fetching PMID 24482228:
Error fetching PMID 28385816:

7. Fujimoto Z, Suzuki N, Kishine N, Ichinose H, Momma M, Kimura A, and Funane K. (2017). Carbohydrate-binding architecture of the multi-modular α-1,6-glucosyltransferase from Paenibacillus sp. 598K, which produces α-1,6-glucosyl-α-glucosaccharides from starch. Biochem J. 2017;474(16):2763-2778. DOI:10.1042/BCJ20170152 |
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 |
11. Suzuki N, Fujimoto Z, Kim YM, Momma M, Kishine N, Suzuki R, Suzuki S, Kitamura S, Kobayashi M, Kimura A, and Funane K. (2014). Structural elucidation of the cyclization mechanism of α-1,6-glucan by Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase. J Biol Chem. 2014;289(17):12040-12051. DOI:10.1074/jbc.M114.547992 |
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 |