Role of subsite +1 residues in pH dependence and catalytic activity of the glycoside hydrolase family 1 β-glucosidase BGL1A from the basidiomycetePhanerochaete chrysosporium

2008 ◽  
Vol 99 (6) ◽  
pp. 1295-1302 ◽  
Author(s):  
Takeshi Tsukada ◽  
Kiyohiko Igarashi ◽  
Shinya Fushinobu ◽  
Masahiro Samejima
Keyword(s):  
Catalytic Activity ◽  
Glycoside Hydrolase ◽  
Ph Dependence ◽  
Glycoside Hydrolase Family ◽  
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 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

scholarly journals The Role of Conserved Arginine Residue in Loop 4 of Glycoside Hydrolase Family 10 Xylanases

2005 ◽  
Vol 69 (5) ◽  
pp. 904-910 ◽  
Author(s):  
Mamoru NISHIMOTO ◽  
Motomitsu KITAOKA ◽  
Shinya FUSHINOBU ◽  
Kiyoshi HAYASHI
Keyword(s):  
Glycoside Hydrolase ◽  
Arginine Residue ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 10 ◽  
Hydrolase Family
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