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Catalysts 2019, 9(3), 234; https://doi.org/10.3390/catal9030234

Characterisation of the First Archaeal Mannonate Dehydratase from Thermoplasma acidophilum and Its Potential Role in the Catabolism of D-Mannose

1
Department of Molecular Sciences, Macquarie University, Sydney, New South Wales 2109, Australia
2
Biomolecular Discovery and Design Research Centre, Macquarie University, Sydney, New South Wales 2109, Australia
*
Author to whom correspondence should be addressed.
Received: 13 February 2019 / Revised: 23 February 2019 / Accepted: 24 February 2019 / Published: 3 March 2019
(This article belongs to the Special Issue Novel Enzyme and Whole-Cell Biocatalysts)
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Abstract

Mannonate dehydratases catalyse the dehydration reaction from mannonate to 2-keto-3-deoxygluconate as part of the hexuronic acid metabolism in bacteria. Bacterial mannonate dehydratases present in this gene cluster usually belong to the xylose isomerase-like superfamily, which have been the focus of structural, biochemical and physiological studies. Mannonate dehydratases from archaea have not been studied in detail. Here, we identified and characterised the first archaeal mannonate dehydratase (TaManD) from the thermoacidophilic archaeon Thermoplasma acidophilum. The recombinant TaManD enzyme was optimally active at 65 °C and showed high specificity towards D-mannonate and its lactone, D-mannono-1,4-lactone. The gene encoding for TaManD is located adjacent to a previously studied mannose-specific aldohexose dehydrogenase (AldT) in the genome of T. acidophilum. Using nuclear magnetic resonance (NMR) spectroscopy, we showed that the mannose-specific AldT produces the substrates for TaManD, demonstrating the possibility for an oxidative metabolism of mannose in T. acidophilum. Among previously studied mannonate dehydratases, TaManD showed closest homology to enzymes belonging to the xylose isomerase-like superfamily. Genetic analysis revealed that closely related mannonate dehydratases among archaea are not located in a hexuronate gene cluster like in bacteria, but next to putative aldohexose dehydrogenases, implying a different physiological role of mannonate dehydratases in those archaeal species. View Full-Text
Keywords: mannonate dehydratase; mannose metabolism; Thermoplasma acidophilum; mannono-1,4-lactone; 2-keto-3-deoxygluconate; aldohexose dehydrogenase mannonate dehydratase; mannose metabolism; Thermoplasma acidophilum; mannono-1,4-lactone; 2-keto-3-deoxygluconate; aldohexose dehydrogenase
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Kopp, D.; Willows, R.; Sunna, A. Characterisation of the First Archaeal Mannonate Dehydratase from Thermoplasma acidophilum and Its Potential Role in the Catabolism of D-Mannose. Catalysts 2019, 9, 234.

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