Crystal Structures of Glycoside Hydrolase Family 51 α-L-Arabinofuranosidase fromThermotoga maritima

2012 ◽  
Vol 76 (2) ◽  
pp. 423-428 ◽  
Author(s):  
Do-Hyun IM ◽  
Kei-ichi KIMURA ◽  
Fumitaka HAYASAKA ◽  
Tomonari TANAKA ◽  
Masato NOGUCHI ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 51

scholarly journals Screening of a Novel Glycoside Hydrolase Family 51 α-L-Arabinofuranosidase from Paenibacillus polymyxa KF-1: Cloning, Expression, and Characterization

Catalysts ◽  
2018 ◽  
Vol 8 (12) ◽  
pp. 589 ◽  
Author(s):  
Yanbo Hu ◽  
Yan Zhao ◽  
Shuang Tian ◽  
Guocai Zhang ◽  
Yumei Li ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Synergistic Effects ◽  
Paenibacillus Polymyxa ◽  
Mass Spectrometry Analysis ◽  
Glycoside Hydrolase Family ◽  
Spectrometry Analysis ◽  
Degrading Enzymes ◽  
Wheat Arabinoxylan ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 51

Paenibacillus polymyxa exhibits remarkable hemicellulolytic activity. In the present study, 13 hemicellulose-degrading enzymes were identified from the secreted proteome of P. polymyxa KF-1 by liquid chromatography-tandem mass spectrometry analysis. α-L-arabinofuranosidase is an important member of hemicellulose-degrading enzymes. A novel α-L-arabinofuranosidase (PpAbf51b), belonging to glycoside hydrolase family 51, was identified from P. polymyxa. Recombinant PpAbf51b was produced in Escherichia coli BL21 (DE3) and was found to be a tetramer using gel filtration chromatography. PpAbf51b hydrolyzed neutral arabinose-containing polysaccharides, including sugar beet arabinan, linear-1,5-α-L-arabinan, and wheat arabinoxylan, with L-arabinose as the main product. The products from hydrolysis indicate that PpAbf51b functions as an exo-α-L-arabinofuranosidase. Combining PpAbf51b and Trichoderma longibrachiatum endo-1,4-xylanase produced significant synergistic effects for the degradation of wheat arabinoxylan. The α-L-arabinofuranosidase identified from the secretome of P. polymyxa KF-1 is potentially suitable for application in biotechnological industries.

Pseudomonas cellulosa expresses a single membrane-bound glycoside hydrolase family 51 arabinofuranosidase

2001 ◽  
Vol 358 (3) ◽  
pp. 599-605 ◽  
Author(s):  
Marie-Helene BEYLOT ◽  
Kaveh EMAMI ◽  
Vincent A. McKIE ◽  
Harry J. GILBERT ◽  
Gavin PELL
Keyword(s):  
Sugar Beet ◽  
Glycoside Hydrolase ◽  
Northern Blot Analysis ◽  
Glycoside Hydrolase Family ◽  
Wild Type ◽  
Mutant Bacterium ◽  
Membrane Bound ◽  
Hydrolase Family ◽  
Wild Type Bacterium ◽  
Glycoside Hydrolase Family 51

In the accompanying paper [Beylot, McKie, Voragen, Doeswijk-Voragen and Gilbert (2001) Biochem. J. 358, 607–614] the chromosome of Pseudomonas cellulosa was shown to contain two genes, abf51A and abf62A, that encode arabinofuranosidases belonging to glycoside hydrolase families 51 and 62, respectively. In this report we show that expression of Abf51A is induced by arabinose and arabinose-containing polysaccharides. Northern-blot analysis showed that abf51A was efficiently transcribed, whereas no transcript derived from abf62A was detected in the presence of arabinose-containing polysaccharides. Zymogram and Western-blot analyses revealed that Abf51A was located on the outer membrane of P. cellulosa. To investigate the importance of Abf51A in the release of arabinose from poly- and oligosaccharides, transposon mutagenesis was used to construct an abf51A-inactive mutant of P. cellulosa (Δabf51A). The mutant did not grow on linear arabinan or sugar beet arabinan, and utilized arabinoxylan much more slowly than the wild-type bacterium. Arabinofuranosidase activity in Δabf51A against aryl-α-arabinofuranosides, arabinan and α1,5-linked arabino-oligosaccharides was approx. 1% of the wild-type bacterium. The mutant bacterium did not exhibit arabinofuranosidase activity against arabinoxylan, supporting the view that abf62A is not expressed in P. cellulosa. These data indicate that P. cellulosa expresses a membrane-bound glycoside hydrolase family 51 arabinofuranosidase that plays a pivotal role in releasing arabinose from polysaccharides and arabino-oligosaccharides.

Crystal structures of the GH6 Orpinomyces sp. Y102 CelC7 enzyme with exo and endo activity and its complex with cellobiose

2019 ◽  
Vol 75 (12) ◽  
pp. 1138-1147
Author(s):  
Hsiao-Chuan Huang ◽  
Liu-Hong Qi ◽  
Yo-Chia Chen ◽  
Li-Chu Tsai
Keyword(s):  
Enzymatic Hydrolysis ◽  
Crystal Structures ◽  
Active Site ◽  
Binding Sites ◽  
Glycoside Hydrolase ◽  
Catalytic Domain ◽  
Glycoside Hydrolase Family ◽  
Substrate Binding Sites ◽  
Key Residues ◽  
Hydrolase Family

The catalytic domain (residues 128–449) of the Orpinomyces sp. Y102 CelC7 enzyme (Orp CelC7) exhibits cellobiohydrolase and cellotriohydrolase activities. Crystal structures of Orp CelC7 and its cellobiose-bound complex have been solved at resolutions of 1.80 and 2.78 Å, respectively. Cellobiose occupies subsites +1 and +2 within the active site of Orp CelC7 and forms hydrogen bonds to two key residues: Asp248 and Asp409. Furthermore, its substrate-binding sites have both tunnel-like and open-cleft conformations, suggesting that the glycoside hydrolase family 6 (GH6) Orp CelC7 enzyme may perform enzymatic hydrolysis in the same way as endoglucanases and cellobiohydrolases. LC-MS/MS analysis revealed cellobiose (major) and cellotriose (minor) to be the respective products of endo and exo activity of the GH6 Orp CelC7.

scholarly journals The Pseudomonas cellulosa glycoside hydrolase family 51 arabinofuranosidase exhibits wide substrate specificity

2001 ◽  
Vol 358 (3) ◽  
pp. 607 ◽  
Author(s):  
Marie-Helene BEYLOT ◽  
Vincent A. McKIE ◽  
Alphons G.J. VORAGEN ◽  
Chantal H.L. DOESWIJK-VORAGEN ◽  
Harry J. GILBERT
Keyword(s):  
Substrate Specificity ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 51 ◽  
Wide Substrate Specificity

Crystal structures of glycoside hydrolase family 3 β-glucosidase 1 from Aspergillus aculeatus

2013 ◽  
Vol 452 (2) ◽  
pp. 211-221 ◽  
Author(s):  
Kentaro Suzuki ◽  
Jun-Ichi Sumitani ◽  
Young-Woo Nam ◽  
Toru Nishimaki ◽  
Shuji Tani ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Glycoside Hydrolase ◽  
Degree Of Polymerization ◽  
Cellulosic Biomass ◽  
Protein Crystal ◽  
Structural Basis ◽  
Glycoside Hydrolase Family ◽  
Aspergillus Aculeatus ◽  
Technical Improvement ◽  
Hydrolase Family

GH3 (glycoside hydrolase family 3) BGLs (β-glucosidases) from filamentous fungi have been widely and commercially used for the supplementation of cellulases. AaBGL1 (Aspergillus aculeatus BGL1) belongs to the GH3 and shows high activity towards cellooligosaccharides up to high degree of polymerization. In the present study we determined the crystal structure of AaBGL1. In addition to the substrate-free structure, the structures of complexes with glucose and various inhibitors were determined. The structure of AaBGL1 is highly glycosylated with 88 monosaccharides (18 N-glycan chains) in the dimer. The largest N-glycan chain comprises ten monosaccharides and is one of the largest glycans ever observed in protein crystal structures. A prominent insertion region exists in a fibronectin type III domain, and this region extends to cover a wide surface area of the enzyme. The subsite +1 of AaBGL1 is highly hydrophobic. Three aromatic residues are present at subsite +1 and are located in short loop regions that are uniquely present in this enzyme. There is a long cleft extending from subsite +1, which appears to be suitable for binding long cellooligosaccharides. The crystal structures of AaBGL1 from the present study provide an important structural basis for the technical improvement of enzymatic cellulosic biomass conversion.

scholarly journals Crystal Structures of a Glycoside Hydrolase Family 20 Lacto-N-biosidase fromBifidobacterium bifidum

2013 ◽  
Vol 288 (17) ◽  
pp. 11795-11806 ◽  
Author(s):  
Tasuku Ito ◽  
Takane Katayama ◽  
Mitchell Hattie ◽  
Haruko Sakurama ◽  
Jun Wada ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family

scholarly journals Pseudomonas cellulosa expresses a single membrane-bound glycoside hydrolase family 51 arabinofuranosidase

2001 ◽  
Vol 358 (3) ◽  
pp. 599 ◽  
Author(s):  
Marie-Helene BEYLOT ◽  
Kaveh EMAMI ◽  
Vincent A. McKIE ◽  
Harry J. GILBERT ◽  
Gavin PELL
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Single Membrane ◽  
Membrane Bound ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 51
Sign in / Sign up

Export Citation Format

Share Document