ArticleThe Journal of biological chemistry2012
Functional association of catalytic and ancillary modules dictates enzymatic activity in glycoside hydrolase family 43 β-xylosidase.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 34 citations in OpenAlex.
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- A strategy to enhance and modify fatty acid synthesis in Corynebacterium glutamicum and Escherichia coli: overexpression of acyl-CoA thioesterases.Microbial cell factories · 2023Article
- Characterization of a GH Family 43 β-Xylosidase Having a Novel Carbohydrate-binding Module fromJournal of applied glycoscience · 2022Article
- Caldicellulosiruptor bescii Adheres to Polysaccharides via a Type IV Pilin-Dependent Mechanism.Applied and environmental microbiology · 2020Article
- β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides.International journal of molecular sciences · 2019Review
- Determination of glycoside hydrolase specificities during hydrolysis of plant cell walls using glycome profiling.Biotechnology for biofuels · 2017Article
- Adaptor Scaffoldins: An Original Strategy for Extended Designer Cellulosomes, Inspired from Nature.mBio · 2016Article
- Article
- Multifunctional cellulase catalysis targeted by fusion to different carbohydrate-binding modules.Biotechnology for biofuels · 2015Article
- The importance of the Abn2 calcium cluster in the endo-1,5-arabinanase activity from Bacillus subtilis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Draft Genome Sequence of the Lignocellulose Decomposer Thermobifida fusca Strain TM51.Genome announcements · 2013Article
- A novel α-L-arabinofuranosidase of family 43 glycoside hydrolase (Ct43Araf) from Clostridium thermocellum.PloS one · 2013Article
- Deconstruction of lignocellulose into soluble sugars by native and designer cellulosomes.mBio · 2012Article
- Purification and characterization of a recombinant β-D-xylosidase from Thermobifida fusca TM51.The protein journal · 2012Article
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8 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-Xylosidases are hemicellulases that hydrolyze short xylo-oligosaccharides into xylose units, thus complementing endoxylanase degradation of the hemicellulose component of lignocellulosic substrates. Here, we describe the cloning, characterization, and kinetic analysis of a glycoside hydrolase family 43 β-xylosidase (Xyl43A) from the aerobic cellulolytic bacterium, Thermobifida fusca. Temperature and pH optima of 55-60 °C and 5.5-6, respectively, were determined. The apparent K(m) value was 0.55 mM, using p-nitrophenyl xylopyranoside as substrate, and the catalytic constant (k(cat)) was 6.72 s(-1). T. fusca Xyl43A contains a catalytic module at the N terminus and an ancillary module (termed herein as Module-A) of undefined function at the C terminus. We expressed the two recombinant modules independently in Escherichia coli and examined their remaining catalytic activity and binding properties. The separation of the two Xyl43A modules caused the complete loss of enzymatic activity, whereas potent binding to xylan was fully maintained in the catalytic module and partially in the ancillary Module-A. Nondenaturing gel electrophoresis revealed a specific noncovalent coupling of the two modules, thereby restoring enzymatic activity to 66.7% (relative to the wild-type enzyme). Module-A contributes a phenylalanine residue that functions as an essential part of the active site, and the two juxtaposed modules function as a single functional entity.
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