ArticleThe Biochemical journal2006
Structural insight into the ligand specificity of a thermostable family 51 arabinofuranosidase, Araf51, from Clostridium thermocellum.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Functional and structural characterization of AtAbf43C: an exo-1,5-α-L-arabinofuranosidase from Acetivibrio thermocellus DSM1313.The Biochemical journal · 2025Article
- The Bifidobacterium adolescentis BAD_1527 gene encodes GH43_22 α-L-arabinofuranosidase of AXH-m type.AMB Express · 2024Article
- Structure and function characterization of the α-L-arabinofuranosidase from the white-rot fungus Trametes hirsuta.Applied microbiology and biotechnology · 2023Article
- Production of a Fungal Punicalagin-Degrading Enzyme by Solid-State Fermentation: Studies of Purification and Characterization.Foods (Basel, Switzerland) · 2023Article
- The In Silico Characterization of Monocotyledonous α-l-Arabinofuranosidases on the Example of Maize.Life (Basel, Switzerland) · 2023Article
- Biochemical and Molecular Dynamics Study of a Novel GH 43 α-l-Arabinofuranosidase/β-Xylosidase FromFrontiers in bioengineering and biotechnology · 2022Article
- Modulation of the Activity and Regioselectivity of a Glycosidase: Development of a Convenient Tool for the Synthesis of Specific Disaccharides.Molecules (Basel, Switzerland) · 2021Article
- Characterization of Two α-l-Arabinofuranosidases fromMicroorganisms · 2021Article
- Two Key Amino Acids Variant of α-l-arabinofuranosidase fromMolecules (Basel, Switzerland) · 2021Article
- The Role of Arabinogalactan Type II Degradation in Plant-Microbe Interactions.Frontiers in microbiology · 2021Review
- Structure of a GH51 α-L-arabinofuranosidase from Meripilus giganteus: conserved substrate recognition from bacteria to fungi.Acta crystallographica. Section D, Structural biology · 2020Article
- Characterization and functional analysis of two novel thermotolerant α-L-arabinofuranosidases belonging to glycoside hydrolase family 51 from Thielavia terrestris and family 62 from Eupenicillium parvum.Applied microbiology and biotechnology · 2020Article
- Cloning and Characterization of a Ginsenoside-Hydrolyzing α-L-Arabinofuranosidase, CaAraf51, From Cellulosimicrobium aquatile Lyp51.Current microbiology · 2020Article
- Molecular Characterization, Regioselective and Synergistic Action of First Recombinant Type III α-L-arabinofuranosidase of Family 43 Glycoside Hydrolase (PsGH43_12) from Pseudopedobacter saltans.Molecular biotechnology · 2020Article
- Identification of a Key Enzyme for the Hydrolysis of β-(1→3)-Xylosyl Linkage in Red Alga Dulse Xylooligosaccharide fromMarine drugs · 2020Article
- Enzymatic Mechanism for Arabinan Degradation and Transport in the Thermophilic Bacterium Caldanaerobius polysaccharolyticus.Applied and environmental microbiology · 2017Article
- Differential expression of α-L-arabinofuranosidases during maize (Zea mays L.) root elongation.Planta · 2015Article
- A novel bifunctional GH51 exo-α-l-arabinofuranosidase/endo-xylanase from Alicyclobacillus sp. A4 with significant biomass-degrading capacity.Biotechnology for biofuels · 2015Article
- Genomics review of holocellulose deconstruction by aspergilli.Microbiology and molecular biology reviews : MMBR · 2014Review
- GH51 arabinofuranosidase and its role in the methylglucuronoarabinoxylan utilization system in Paenibacillus sp. strain JDR-2.Applied and environmental microbiology · 2014Article
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6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The digestion of the plant cell wall requires the concerted action of a diverse repertoire of enzyme activities. An important component of these hydrolase consortia are arabinofuranosidases, which release L-arabinofuranose moieties from a range of plant structural polysaccharides. The anaerobic bacterium Clostridium thermocellum, a highly efficient plant cell wall degrader, possesses a single alpha-L-arabinofuranosidase (EC 3.2.1.55), CtAraf51A, located in GH51 (glycoside hydrolase family 51). The crystal structure of the enzyme has been solved in native form and in 'Michaelis' complexes with both alpha-1,5-linked arabinotriose and alpha-1,3 arabinoxylobiose, both forming a hexamer in the asymmetric unit. Kinetic studies reveal that CtAraf51A, in contrast with well-characterized GH51 enzymes including the Cellvibrio japonicus enzyme [Beylot, McKie, Voragen, Doeswijk-Voragen and Gilbert (2001) Biochem. J. 358, 607-614], catalyses the hydrolysis of alpha-1,5-linked arabino-oligosaccharides and the alpha-1,3 arabinosyl side chain decorations of xylan with equal efficiency. The paucity of direct hydrogen bonds with the aglycone moiety and the flexible conformation adopted by Trp(178), which stacks against the sugar at the +1 subsite, provide a structural explanation for the plasticity in substrate specificity displayed by the clostridial arabinofuranosidase.
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