https://scholars.lib.ntu.edu.tw/handle/123456789/501831
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.author | Sheng-Chia Chen | en_US |
dc.contributor.author | Szu-Pei Wu | en_US |
dc.contributor.author | Yu-Yung Chang | en_US |
dc.contributor.author | Tzann-Shun Hwang | en_US |
dc.contributor.author | TZONG-HUEI LEE | en_US |
dc.contributor.author | Chun-Hua Hsu | en_US |
dc.contributor.author | CHUN-HUA HSU | en_US |
dc.creator | Chun-Hua Hsu;TZONG-HUEI LEE;Tzann-Shun Hwang;Yu-Yung Chang;Szu-Pei Wu;Sheng-Chia Chen | - |
dc.date.accessioned | 2020-06-12T04:08:23Z | - |
dc.date.available | 2020-06-12T04:08:23Z | - |
dc.date.issued | 2020-05-10 | - |
dc.identifier.uri | https://scholars.lib.ntu.edu.tw/handle/123456789/501831 | - |
dc.description.abstract | α-Galactosidase catalyzes the hydrolysis of a terminal α-galactose residue in galacto-oligosaccharides and has potential in various industrial applications and food processing. We determined the crystal structures of α-galactosidase from the thermophilic microorganism Thermus thermophilus (TtGalA) and its complexes with pNPGal and stachyose. The monomer folds into an N-terminal domain, a catalytic (β/α)8 barrel domain, and a C-terminal domain. The domain organization is similar to that of the other family of 36 α-galactosidases, but TtGalA presents a cagelike hexamer. Structural analysis shows that oligomerization may be a key factor for the thermal adaption of TtGalA. The structure of TtGalA complexed with stachyose reveals only the existence of one −1 subsite and one +1 subsite in the active site. Structural comparison of the stachyose-bound complexes of TtGalA and GsAgaA, a tetrameric enzyme with four subsites, suggests evolutionary divergence of substrate specificity within the GH36 family of α-galactosidases. To the best of our knowledge, the crystal structure of TtGalA is the first report of a quaternary structure as a hexameric assembly in the α-galactosidase family. | en_US |
dc.language.iso | en | en_US |
dc.relation.ispartof | Journal of Agricultural and Food Chemistry | en_US |
dc.title | Crystal Structure of α-Galactosidase from Thermus thermophilus: Insight into Hexamer Assembly and Substrate Specificity | en_US |
dc.type | journal article | en |
dc.identifier.doi | 10.1021/acs.jafc.0c00871 | - |
dc.relation.pages | 6161 | en_US |
dc.relation.journalvolume | 68 | en_US |
dc.relation.journalissue | 22 | en_US |
item.fulltext | no fulltext | - |
item.openairetype | journal article | - |
item.languageiso639-1 | en | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
item.grantfulltext | none | - |
item.cerifentitytype | Publications | - |
crisitem.author.dept | Fisheries Science | - |
crisitem.author.dept | Life Science | - |
crisitem.author.dept | Agricultural Chemistry | - |
crisitem.author.dept | Biochemical Sciences | - |
crisitem.author.dept | Genome and Systems Biology Degree Program | - |
crisitem.author.dept | Master Program in Global Agriculture Technology and Genomic Science (Global ATGS) | - |
crisitem.author.orcid | 0000-0001-8036-7563 | - |
crisitem.author.orcid | 0000-0002-0008-7383 | - |
crisitem.author.parentorg | College of Life Science | - |
crisitem.author.parentorg | College of Life Science | - |
crisitem.author.parentorg | College of Bioresources and Agriculture | - |
crisitem.author.parentorg | College of Life Science | - |
crisitem.author.parentorg | College of Life Science | - |
crisitem.author.parentorg | International College | - |
顯示於: | 漁業科學研究所 |
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