ArticleExtremophiles : life under extreme conditions2013
Molecular characterization of a thermostable aldehyde dehydrogenase (ALDH) from the hyperthermophilic archaeon Sulfolobus tokodaii strain 7.
Article in Extremophiles : life under extreme conditions, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 19 citations in OpenAlex.
- Challenges, optimization, and delivery strategies in the heterologous expression of aldehyde dehydrogenase: therapeutic applications for acetaldehyde detoxification.Biotechnology letters · 2026Review
- Aldehyde dehydrogenase activity is induced by oxygen exposure in the anaerobic archaeon Methanosarcina acetivorans.World journal of microbiology & biotechnology · 2025Article
- Crystal structure of thermostable acetaldehyde dehydrogenase from the hyperthermophilic archaeon Sulfolobus tokodaii.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Antarctic aldehyde dehydrogenase from Flavobacterium PL002 as a potent catalyst for acetaldehyde determination in wine.Scientific reports · 2022Article
- Structure Prediction and Characterization of Thermostable Aldehyde Dehydrogenase from Newly IsolatedMicroorganisms · 2022Article
- Study of ALDH fromCells · 2021Article
- Construction of an alternative glycerol-utilization pathway for improved β-carotene production in Escherichia coli.Journal of industrial microbiology & biotechnology · 2018Article
- Functional characterization of a vanillin dehydrogenase in Corynebacterium glutamicum.Scientific reports · 2015Article
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4 authors at 1 institution in 1 country.
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Abstract
Aldehyde dehydrogenase (ALDH) is a widely distributed enzyme in nature. Although many ALDHs have been reported until now, the detailed enzymatic properties of ALDH from Archaea remain elusive. Herein, we describe the characterization of an ALDH from the hyperthermophilic archaeon Sulfolobus tokodaii. The enzyme (stALDH) could utilize various aldehydes as substrates, and maximal activity was found with acetaldehyde and the coenzyme NAD. The optimal temperature and pH were 80 °C and 8, respectively, and high thermostability was found with the half-life at 90 °C to be 4 h. The enzyme was considerably resistant to nitroglycerin (GTN) inhibition, which could be restored by reducing agent DTT or (±)-α-lipoic acid. Coenzyme NAD or NADP could regulate the enzymatic thermostability, as well as the esterase activity. Molecular modeling suggested that the enzyme harbored similar structural arrangement with its eukaryotic and bacterial counterparts. Sequence alignment showed the conserved catalytic residues E240 and C274 and cofactor interactive sites N142, K165, I168 and E370, the function of which were verified by site-directed mutagenesis analysis. This is the most thermostable ALDH reported until now and the unique property of this enzyme is potentially beneficial in the fields of biotechnology and biomedicine.
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