Table of Contents
Catalysts, Volume 9, Issue 3 (March 2019)
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Cover Story (view full-size image) We functionally characterised the first archaeal mannonate dehydratase from the thermoacidophilic [...] Read more. We functionally characterised the first archaeal mannonate dehydratase from the thermoacidophilic archaeon Thermoplasma acidophilum (TaManD). In contrast to mannonate dehydratases in bacteria, the gene encoding for TaManD is located adjacent to the mannose-specific aldohexose dehydrogenase AldT. AldT produce the substrates, D-mannono-1,4-lactone and D-mannonate for TaManD via oxidation of mannose. TaManD can convert both substrates into the cellular intermediate 2-keto-3-deoxygluconte (KDG). The two enzymatic steps resemble the first reactions in the non-phosphorylative carbohydrate pathways found in archaea. This work demonstrates a feasible conversion of D-mannose to KDG and suggests a role of TaManD in a putative catabolism of D-mannose. View this paper.