ArticleActa crystallographica. Section D, Structural biology2018
Structure and function of a glycoside hydrolase family 8 endoxylanase from Teredinibacter turnerae.
Article in Acta crystallographica. Section D, Structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- In Silico Study of Potential Binding Sites of the Family GH126 Enzyme CPF_2247 fromMolecules (Basel, Switzerland) · 2026Article
- Production of High-Value Antibiotics byACS sustainable chemistry & engineering · 2025Article
- Complete genome sequences of two shipworm endosymbiont strains,Microbiology resource announcements · 2025Article
- Lactate cross-feeding betweenApplied and environmental microbiology · 2024Article
- Structural snapshot of a glycoside hydrolase family 8 endo-β-1,4-glucanase capturing the state after cleavage of the scissile bond.Acta crystallographica. Section D, Structural biology · 2022Article
- Mechanistic strategies of microbial communities regulating lignocellulose deconstruction in a UK salt marsh.Microbiome · 2021Article
- Cloning of novel bacterial xylanases from lignocellulose-enriched compost metagenomic libraries.AMB Express · 2019Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The biological conversion of lignocellulosic matter into high-value chemicals or biofuels is of increasing industrial importance as the sector slowly transitions away from nonrenewable sources. Many industrial processes involve the use of cellulolytic enzyme cocktails - a selection of glycoside hydrolases and, increasingly, polysaccharide oxygenases - to break down recalcitrant plant polysaccharides. ORFs from the genome of Teredinibacter turnerae, a symbiont hosted within the gills of marine shipworms, were identified in order to search for enzymes with desirable traits. Here, a putative T. turnerae glycoside hydrolase from family 8, hereafter referred to as TtGH8, is analysed. The enzyme is shown to be active against β-1,4-xylan and mixed-linkage (β-1,3,β-1,4) marine xylan. Kinetic parameters, obtained using high-performance anion-exchange chromatography with pulsed amperometric detection and 3,5-dinitrosalicyclic acid reducing-sugar assays, show that TtGH8 catalyses the hydrolysis of β-1,4-xylohexaose with a k
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