ORCID Profile
0000-0003-4577-9479
Current Organisation
University of York
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Publisher: Microbiology Society
Date: 15-03-2023
DOI: 10.1099/MIC.0.001308
Abstract: Microbes that have evolved to live on lignocellulosic biomass face unique challenges in the effective and efficient use of this material as food. The bacterium Shewanella sp. ANA-3 has the potential to utilize arabinan and arabinoxylan, and uptake of the monosaccharide, l -arabinose, derived from these polymers, is known to be mediated by a single ABC transporter. We demonstrate that the substrate binding protein of this system, GafA Sw , binds specifically to l -arabinofuranose, which is the rare furanose form of l -arabinose found in lignocellulosic biomass. The structure of GafA Sw was resolved to 1.7 Å and comparison to Escherichia coli YtfQ (GafA Ec ) revealed binding site adaptations that confer specificity for furanose over pyranose forms of monosaccharides, while selecting arabinose over another related monosaccharide, galactose. The discovery of a bacterium with a natural predilection for a sugar found abundantly in certain lignocellulosic materials suggests an intimate connection in the enzymatic release and uptake of the sugar, perhaps to prevent other microbes scavenging this nutrient before it mutarotates to l -arabinopyranose. This biological discovery also provides a clear route to engineer more efficient utilization of plant biomass components in industrial biotechnology.
Publisher: Springer Science and Business Media LLC
Date: 27-07-2020
DOI: 10.1038/S41598-020-68860-Z
Abstract: Body odour is a characteristic trait of Homo sapiens , however its role in human behaviour and evolution is poorly understood. Remarkably, body odour is linked to the presence of a few species of commensal microbes. Herein we discover a bacterial enzyme, limited to odour-forming staphylococci that are able to cleave odourless precursors of thioalcohols, the most pungent components of body odour. We demonstrated using phylogenetics, biochemistry and structural biology that this cysteine-thiol lyase (C-T lyase) is a PLP-dependent enzyme that moved horizontally into a unique monophyletic group of odour-forming staphylococci about 60 million years ago, and has subsequently tailored its enzymatic function to human-derived thioalcohol precursors. Significantly, transfer of this enzyme alone to non-odour producing staphylococci confers odour production, demonstrating that this C-T lyase is both necessary and sufficient for thioalcohol formation. The structure of the C-T lyase compared to that of other related enzymes reveals how the adaptation to thioalcohol precursors has evolved through changes in the binding site to create a constrained hydrophobic pocket that is selective for branched aliphatic thioalcohol ligands. The ancestral acquisition of this enzyme, and the subsequent evolution of the specificity for thioalcohol precursors implies that body odour production in humans is an ancient process.
Publisher: Elsevier BV
Date: 08-2006
Publisher: Hindawi Limited
Date: 10-10-2023
DOI: 10.1155/2023/9141112
Publisher: Wiley
Date: 21-07-2006
Location: United Kingdom of Great Britain and Northern Ireland
Location: Taiwan, Province of China
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Anthony Wilkinson.