Motif-Guided Identification of a Glycoside Hydrolase Family 1 α-L-Arabinofuranosidase inBifidobacterium adolescentis

2013 ◽  
Vol 77 (8) ◽  
pp. 1709-1714 ◽  
Author(s):  
Hirokazu SUZUKI ◽  
Ayano MURAKAMI ◽  
Ken-ichi YOSHIDA
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family

Cloning and characterization of a novel cellobiase gene, cba3, encoding the first known β-glucosidase of glycoside hydrolase family 1 of Cellulomonas biazotea

Gene ◽  
2012 ◽  
Vol 493 (1) ◽  
pp. 52-61 ◽  
Author(s):  
Anthony K.N. Chan ◽  
Yule Y. Wang ◽  
K.L. Ng ◽  
Zhibiao Fu ◽  
W.K.R. Wong
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Cellulomonas Biazotea ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family

Substrate specificity of glycoside hydrolase family 1 β-glucosidase AtBGlu42 from Arabidopsis thaliana and its molecular mechanism

2021 ◽  
Author(s):  
Shu Horikoshi ◽  
Wataru Saburi ◽  
Jian Yu ◽  
Hideyuki Matsuura ◽  
James R Ketudat Cairns ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Glycoside Hydrolase ◽  
Sequence Similarity ◽  
Glycoside Hydrolase Family ◽  
Its Sequence ◽  
Cell Wall Metabolism ◽  
Bioactive Substances ◽  
Chain Length Specificity ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family

ABSTRACT Plants possess many glycoside hydrolase family 1 (GH1) β-glucosidases, which physiologically function in cell wall metabolism and activation of bioactive substances, but most remain uncharacterized. One GH1 isoenzyme AtBGlu42 in Arabidopsis thaliana has been identified to hydrolyze scopolin using the gene deficient plants, but no enzymatic properties were obtained. Its sequence similarity to another functionally characterized enzyme Os1BGlu4 in rice suggests that AtBGlu42 also acts on oligosaccharides. Here, we show that the recombinant AtBGlu42 possesses high kcat/Km not only on scopolin, but also on various β-glucosides, cellooligosaccharides, and laminarioligosaccharides. Of the cellooligosaccharides, cellotriose was the most preferred. The crystal structure, determined at 1.7 Å resolution, suggests that Arg342 gives unfavorable binding to cellooligosaccharides at subsite +3. The mutants R342Y and R342A showed the highest preference on cellotetraose or cellopentaose with increased affinities at subsite +3, indicating that the residues at this position have an important role for chain length specificity.

scholarly journals Sphingadienine-1-phosphate levels are regulated by a novel glycoside hydrolase family 1 glucocerebrosidase widely distributed in seed plants

2021 ◽  
pp. 101236
Author(s):  
Jinichiro Koga ◽  
Makoto Yazawa ◽  
Koji Miyamoto ◽  
Emi Yumoto ◽  
Tomoyoshi Kubota ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Seed Plants ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family

scholarly journals Protein-carbohydrate Interactions Leading to Hydrolysis and Transglycosylation in Plant Glycoside Hydrolase Family 1 Enzymes

2012 ◽  
Vol 59 (2) ◽  
pp. 51-62 ◽  
Author(s):  
James R. Ketudat Cairns ◽  
Salila Pengthaisong ◽  
Sukanya Luang ◽  
Sompong Sansenya ◽  
Anupong Tankrathok ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family

Functional genomic analysis of Arabidopsis thaliana glycoside hydrolase family 1

2004 ◽  
Vol 55 (3) ◽  
pp. 343-367 ◽  
Author(s):  
Zhiwei Xu ◽  
Luis Escamilla-Trevi�o ◽  
Lihui Zeng ◽  
Mallikarjun Lalgondar ◽  
David Bevan ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Glycoside Hydrolase ◽  
Genomic Analysis ◽  
Glycoside Hydrolase Family ◽  
Functional Genomic ◽  
Functional Genomic Analysis ◽  
Glycoside Hydrolase Family 1 ◽  
Hydrolase Family
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