ArticleThe Biochemical journal2001
The Pseudomonas cellulosa glycoside hydrolase family 51 arabinofuranosidase exhibits wide substrate specificity.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Effect of enzymatic modification on the structure and rheological properties of diluted alkali-soluble pectin fraction rich in RG-I.Scientific reports · 2024Article
- Functional Characterization of Endo- and Exo-Hydrolase Genes in Arabinan Degradation Gene Cluster ofInternational journal of molecular sciences · 2024Article
- The biosynthesis, degradation, and function of cell wall β-xylosylated xyloglucan mirrors that of arabinoxyloglucan.The New phytologist · 2023Article
- Arabinoxylo- and Arabino-Oligosaccharides-Specific α-L-Arabinofuranosidase GH51 Isozymes from the Amylolytic YeastJournal of microbiology and biotechnology · 2021Article
- The mechanism by which a distinguishing arabinofuranosidase can cope with internal di-substitutions in arabinoxylans.Biotechnology for biofuels · 2018Article
- The Mechanism by Which Arabinoxylanases Can Recognize Highly Decorated Xylans.The Journal of biological chemistry · 2016Article
- Polysaccharide degradation systems of the saprophytic bacterium Cellvibrio japonicus.World journal of microbiology & biotechnology · 2016Review
- Identification of the nucleophile catalytic residue of GH51 α-L-arabinofuranosidase from Pleurotus ostreatus.AMB Express · 2015Article
- An unusual xylan in Arabidopsis primary cell walls is synthesised by GUX3, IRX9L, IRX10L and IRX14.The Plant journal : for cell and molecular biology · 2015Article
- Glycan complexity dictates microbial resource allocation in the large intestine.Nature communications · 2015Article
- A novel bifunctional GH51 exo-α-l-arabinofuranosidase/endo-xylanase from Alicyclobacillus sp. A4 with significant biomass-degrading capacity.Biotechnology for biofuels · 2015Article
- Elucidation of the molecular basis for arabinoxylan-debranching activity of a thermostable family GH62 α-l-arabinofuranosidase from Streptomyces thermoviolaceus.Applied and environmental microbiology · 2014Article
- Plant surface cues prime Ustilago maydis for biotrophic development.PLoS pathogens · 2014Article
- Crystal structure and characterization of the glycoside hydrolase family 62 α-L-arabinofuranosidase from Streptomyces coelicolor.The Journal of biological chemistry · 2014Article
- Characterization of a hexameric exo-acting GH51 α-l-arabinofuranosidase from the mesophilic Bacillus subtilis.Molecular biotechnology · 2013Article
- How nature can exploit nonspecific catalytic and carbohydrate binding modules to create enzymatic specificity.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Glycosyl transferases in family 61 mediate arabinofuranosyl transfer onto xylan in grasses.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structure and function of an arabinoxylan-specific xylanase.The Journal of biological chemistry · 2011Article
- The structure and function of an arabinan-specific alpha-1,2-arabinofuranosidase identified from screening the activities of bacterial GH43 glycoside hydrolases.The Journal of biological chemistry · 2011Article
- Circular permutation provides an evolutionary link between two families of calcium-dependent carbohydrate binding modules.The Journal of biological chemistry · 2010Article
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5 authors.
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No grant is acknowledged in the PubMed record.
Abstract
To investigate the mechanism by which Pseudomonas cellulosa releases arabinose from polysaccharides and oligosaccharides, a gene library of P. cellulosa genomic DNA was screened for 4-methylumbelliferyl-alpha-L-arabinofuranosidase (MUAase) activity. A single MUAase gene (abf51A) was isolated, which encoded a non-modular glycoside hydrolase family (GH) 51 arabinofuranosidase (Abf51A) of 57000 Da. The substrate specificity of the Abf51A showed that it preferentially removed alpha1,2- and alpha1,3-linked arabinofuranose side chains from either arabinan or arabinoxylan, and hydrolysed alpha1,5-linked arabino-oligosaccharides, although at a much lower rate. The activity of Abf51A against arabinoxylan was similar to a GH62 arabinofuranosidase encoded by a P. cellulosa gene. Glu-194 and Glu-321 of Abf51A are conserved in GH51 enzymes, and it has been suggested that these amino acids comprise the key catalytic acid/base and nucleophile residues, respectively. To evaluate this hypothesis the biochemical properties of E194A and E321A mutants of Abf51A were evaluated. The data were consistent with the view that Glu-194 and Glu-321 comprise the key catalytic residues of Abf51A. These data, in conjunction with the results presented in the accompanying paper [Beylot, Emami, McKie, Gilbert and Pell (2001) Biochem. J. 358, 599-605], indicate that P. cellulosa expresses a membrane-bound GH51 arabinofuranosidase that plays a pivotal role in releasing arabinose from a range of polysaccharides and oligosaccharides.
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