ArticleJournal of bacteriology2010
Biochemical and domain analyses of FSUAxe6B, a modular acetyl xylan esterase, identify a unique carbohydrate binding module in Fibrobacter succinogenes S85.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 31 citations in OpenAlex.
- Nonspecific Binding of a Putative S-Layer Protein to Plant Cell Wall Polysaccharides-Implication for Growth Competence ofInternational journal of molecular sciences · 2025Article
- Catalytic Efficiency Improvement in Cellobiohydrolase I by Cross-Species Domain Exchange Engineering.International journal of molecular sciences · 2025Article
- Effects of Different Yeast Selenium Levels on Rumen Fermentation Parameters, Digestive Enzyme Activity and Gastrointestinal Microflora of Sika Deer during Antler Growth.Microorganisms · 2023Article
- Multi-omics revealed the effects of dietary energy levels on the rumen microbiota and metabolites in yaks under house-feeding conditions.Frontiers in microbiology · 2023Article
- Identification of WxL and S-Layer Proteins fromInternational journal of molecular sciences · 2022Article
- CE16 acetylesterases: in silico analysis, catalytic machinery prediction and comparison with related SGNH hydrolases.3 Biotech · 2021Article
- Degradation of complex arabinoxylans by human colonic Bacteroidetes.Nature communications · 2021Article
- Deciphering the unique cellulose degradation mechanism of the ruminal bacterium Fibrobacter succinogenes S85.Scientific reports · 2019Article
- Synergism of glycoside hydrolase secretomes from two thermophilic bacteria cocultivated on lignocellulose.Applied and environmental microbiology · 2014Article
- Inference of phenotype-defining functional modules of protein families for microbial plant biomass degraders.Biotechnology for biofuels · 2014Article
- Acetylation of woody lignocellulose: significance and regulation.Frontiers in plant science · 2013Article
- Multifunctionality and diversity of GDSL esterase/lipase gene family in rice (Oryza sativa L. japonica) genome: new insights from bioinformatics analysis.BMC genomics · 2012Article
- Biochemical and mutational analyses of a multidomain cellulase/mannanase from Caldicellulosiruptor bescii.Applied and environmental microbiology · 2012Article
- Biochemical analyses of multiple endoxylanases from the rumen bacterium Ruminococcus albus 8 and their synergistic activities with accessory hemicellulose-degrading enzymes.Applied and environmental microbiology · 2011Article
- The complete genome sequence of Fibrobacter succinogenes S85 reveals a cellulolytic and metabolic specialist.PloS one · 2011Article
- Domain analysis of a modular alpha-L-Arabinofuranosidase with a unique carbohydrate binding strategy from the fiber-degrading bacterium Fibrobacter succinogenes S85.Journal of bacteriology · 2010Article
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acetyl xylan esterase (EC 3.1.1.72) is a member of a set of enzymes required to depolymerize hemicellulose, especially xylan that is composed of a main chain of beta-1,4-linked xylopyranoside residues decorated with acetyl side groups. Fibrobacter succinogenes S85 Axe6B (FSUAxe6B) is an acetyl xylan esterase encoded in the genome of this rumen bacterium. The enzyme is a modular protein comprised of an esterase domain, a carbohydrate-binding module, and a region of unknown function. Sequences that are homologous to the region of unknown function are paralogously distributed, thus far, only in F. succinogenes. Therefore, the sequences were designated Fibrobacter succinogenes-specific paralogous module 1 (FPm-1). The FPm-1s are associated with at least 24 polypeptides in the genome of F. succinogenes S85. A bioinformatics search showed that most of the FPm-1-appended polypeptides are putative carbohydrate-active enzymes, suggesting a potential role in carbohydrate metabolism. Truncational analysis of FSUAxe6B, together with catalytic and substrate binding studies, has allowed us to delineate the functional modules in the polypeptide. The N-terminal half of FSUAxe6B harbors the activity that cleaves side chain acetyl groups from xylan-like substrates, and the binding of insoluble xylan was determined to originate from FPm-1. Site-directed mutagenesis studies of highly conserved active-site residues in the esterase domain suggested that the esterase activity is derived from a tetrad composed of Ser(44), His(273), Glu(194), and Asp(270), with both Glu(194) and Asp(270) functioning as helper acids, instead of a single carboxylate residue proposed to initiate catalysis.
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