Key aromatic residues at subsites +2 and +3 of glycoside hydrolase family 31 α-glucosidase contribute to recognition of long-chain substrates

2013 ◽  
Vol 1834 (1) ◽  
pp. 329-335 ◽  
Author(s):  
Takayoshi Tagami ◽  
Masayuki Okuyama ◽  
Hiroyuki Nakai ◽  
Young-Min Kim ◽  
Haruhide Mori ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Aromatic Residues ◽  
Glycoside Hydrolase Family 31 ◽  
Hydrolase Family ◽  
Long Chain

Production of 1,5-anhydro-d-fructose by an α-glucosidase belonging to glycoside hydrolase family 31

2014 ◽  
Vol 78 (12) ◽  
pp. 2064-2068 ◽  
Author(s):  
Janjira Maneesan ◽  
Hideyuki Matsuura ◽  
Takayoshi Tagami ◽  
Haruhide Mori ◽  
Atsuo Kimura
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 31 ◽  
Hydrolase Family

scholarly journals A glycoside hydrolase family 31 dextranase with high transglucosylation activity from Flavobacterium johnsoniae

2016 ◽  
Vol 80 (8) ◽  
pp. 1562-1567 ◽  
Author(s):  
Yoshifumi Gozu ◽  
Yuichi Ishizaki ◽  
Yuhei Hosoyama ◽  
Takatsugu Miyazaki ◽  
Atsushi Nishikawa ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Flavobacterium Johnsoniae ◽  
Glycoside Hydrolase Family 31 ◽  
Hydrolase Family

Characterization of a Glycoside Hydrolase Family 31 α-Glucosidase Involved in Starch Utilization inPodospora anserina

2013 ◽  
Vol 77 (10) ◽  
pp. 2117-2124 ◽  
Author(s):  
Kyung-Mo SONG ◽  
Masayuki OKUYAMA ◽  
Kazuyuki KOBAYASHI ◽  
Haruhide MORI ◽  
Atsuo KIMURA
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Starch Utilization ◽  
Glycoside Hydrolase Family 31 ◽  
Hydrolase Family

scholarly journals A Novel α-Glucosidase of the Glycoside Hydrolase Family 31 from Aspergillus sojae

2019 ◽  
Vol 66 (2) ◽  
pp. 73-81
Author(s):  
Atsushi Kawano ◽  
Yuji Matsumoto ◽  
Nozomi Nikaido ◽  
Akihiro Tominaga ◽  
Takashi Tonozuka ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Aspergillus Sojae ◽  
Glycoside Hydrolase Family 31 ◽  
Hydrolase Family

scholarly journals Structural and enzymatic characterization of a glycoside hydrolase family 31 α-xylosidase from Cellvibrio japonicus involved in xyloglucan saccharification

2011 ◽  
Vol 436 (3) ◽  
pp. 567-580 ◽  
Author(s):  
Johan Larsbrink ◽  
Atsushi Izumi ◽  
Farid M. Ibatullin ◽  
Azadeh Nakhai ◽  
Harry J. Gilbert ◽  
...  
Keyword(s):  
Cell Wall ◽  
Glycoside Hydrolase ◽  
Plant Cell Wall ◽  
Biomass Conversion ◽  
Primary Cell Wall ◽  
Glycoside Hydrolase Family ◽  
Cellvibrio Japonicus ◽  
Glycoside Hydrolase Family 31 ◽  
Hydrolase Family

The desire for improved methods of biomass conversion into fuels and feedstocks has re-awakened interest in the enzymology of plant cell wall degradation. The complex polysaccharide xyloglucan is abundant in plant matter, where it may account for up to 20% of the total primary cell wall carbohydrates. Despite this, few studies have focused on xyloglucan saccharification, which requires a consortium of enzymes including endo-xyloglucanases, α-xylosidases, β-galactosidases and α-L-fucosidases, among others. In the present paper, we show the characterization of Xyl31A, a key α-xylosidase in xyloglucan utilization by the model Gram-negative soil saprophyte Cellvibrio japonicus. CjXyl31A exhibits high regiospecificity for the hydrolysis of XGOs (xylogluco-oligosaccharides), with a particular preference for longer substrates. Crystallographic structures of both the apo enzyme and the trapped covalent 5-fluoro-β-xylosyl-enzyme intermediate, together with docking studies with the XXXG heptasaccharide, revealed, for the first time in GH31 (glycoside hydrolase family 31), the importance of a PA14 domain insert in the recognition of longer oligosaccharides by extension of the active-site pocket. The observation that CjXyl31A was localized to the outer membrane provided support for a biological model of xyloglucan utilization by C. japonicus, in which XGOs generated by the action of a secreted endo-xyloglucanase are ultimately degraded in close proximity to the cell surface. Moreover, the present study diversifies the toolbox of glycosidases for the specific modification and saccharification of cell wall polymers for biotechnological applications.

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