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 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.

Structural and biochemical characterization of novel bacterial α-galactosidases belonging to glycoside hydrolase family 31

2015 ◽  
Vol 469 (1) ◽  
pp. 145-158 ◽  
Author(s):  
Takatsugu Miyazaki ◽  
Yuichi Ishizaki ◽  
Megumi Ichikawa ◽  
Atsushi Nishikawa ◽  
Takashi Tonozuka
Keyword(s):  
Substrate Specificity ◽  
Crystal Structures ◽  
Glycoside Hydrolase ◽  
Biochemical Characterization ◽  
Glycoside Hydrolase Family ◽  
Galactosidase Activity ◽  
Gh31 Family ◽  
Glycoside Hydrolase Family 31 ◽  
Hydrolase Family

We identified two bacterial enzymes as the first members that displayed α-galactosidase activity and the crystal structures provided insights into their novel substrate specificity. This is the first report of α-galactosidases which belong to the GH31 family.

scholarly journals Characterization of Fusarium oxysporum β-1,6-Galactanase, an Enzyme That Hydrolyzes Larch Wood Arabinogalactan

2007 ◽  
Vol 73 (9) ◽  
pp. 3109-3112 ◽  
Author(s):  
Tatsuji Sakamoto ◽  
Yuya Taniguchi ◽  
Shiho Suzuki ◽  
Hideshi Ihara ◽  
Haruhiko Kawasaki
Keyword(s):  
Fusarium Oxysporum ◽  
Glycoside Hydrolase ◽  
Recombinant Enzyme ◽  
Glycoside Hydrolase Family ◽  
Type Ii ◽  
High Similarity ◽  
Degrading Enzyme ◽  
Larch Wood ◽  
Hydrolase Family

ABSTRACT A type II arabinogalactan-degrading enzyme (FoGal1) was purified from Fusarium oxysporum 12S, and the corresponding cDNA was isolated. FoGal1 had high similarity to enzymes of glycoside hydrolase family 5. Treatment of larch wood arabinogalactan with the recombinant enzyme indicated that FoGal1 is a β-1,6-galactanase that preferentially debranches β-1,6-galactobiose from the substrate.

scholarly journals Biochemical characterization of a glycoside hydrolase family 43 β-D-galactofuranosidase from the fungus Aspergillus niger

2021 ◽  
Author(s):  
Gregory S Bulmer ◽  
Fang Wei Yuen ◽  
Naimah Begum ◽  
Bethan S Jones ◽  
Sabine S Flitsch ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Glycoside Hydrolase ◽  
Biochemical Characterization ◽  
Maximum Activity ◽  
Glycoside Hydrolase Family ◽  
Enzyme Specificity ◽  
Fungal Enzymes ◽  
Glycoside Hydrolase Family 43 ◽  
Hydrolase Family

β-D-Galactofuranose (Galf) and its polysaccharides are found in bacteria, fungi and protozoa but do not occur in mammalian tissues, and thus represent a specific target for anti-pathogenic drugs. Understanding the enzymatic degradation of these polysaccharides is therefore of great interest, but the identity of fungal enzymes with exclusively galactofuranosidase activity has so far remained elusive. Here we describe the identification and characterization of a galactofuranosidase from the industrially important fungus Aspergillus niger. Phylogenetic analysis of glycoside hydrolase family 43 subfamily 34 (GH43_34) members revealed the occurrence of three distinct clusters and, by comparison with specificities of characterized bacterial members, suggested a basis for prediction of enzyme specificity. Using this rationale, in tandem with molecular docking, we identified a putative β-D-galactofuranosidase from A. niger which was recombinantly expressed in Escherichia coli. The Galf-specific hydrolase, encoded by xynD demonstrates maximum activity at pH 5, 25 °C towards 4-Nitrophenyl-β-galactofuranoside (pNP-βGalf), with a Km of 17.9 ± 1.9 mM and Vmax of 70.6 ± 5.3 μmol min-1. The characterization of this first fungal GH43 galactofuranosidase offers further molecular insight into the degradation of Galf-containing structures and may inform clinical treatments against fungal pathogens.

Characterization of a Theme C Glycoside Hydrolase Family 9 Endo-Beta-Glucanase from a Biogas Reactor Metagenome

2018 ◽  
Vol 37 (5) ◽  
pp. 454-460
Author(s):  
Carola Schröder ◽  
Christin Burkhardt ◽  
Philip Busch ◽  
Georg Schirrmacher ◽  
Jörg Claren ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Beta Glucanase ◽  
Glycoside Hydrolase Family 9 ◽  
Biogas Reactor ◽  
Hydrolase Family

Cloning, Expression and Characterization of a Glycoside Hydrolase Family 39 Xylosidase from Bacillus Halodurans C-125

2007 ◽  
pp. 189-198
Author(s):  
Kurt Wagschal ◽  
Diana Franqui-Espiet ◽  
Charles C. Lee ◽  
George H. Robertson ◽  
Dominic W. S. Wong
Keyword(s):  
Glycoside Hydrolase ◽  
Bacillus Halodurans ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family
Sign in / Sign up

Export Citation Format

Share Document