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dc.contributorVirginia Techen
dc.contributor.authorSusanti, Dwien
dc.contributor.authorLoganathan, Ushaen
dc.contributor.authorCompton, Austinen
dc.contributor.authorMukhopadhyay, Biswarupen
dc.description.abstractFlavin-containing Trx reductase (TrxR) of Thermoplasma acidophilum (Ta), a thermoacidophilic facultative anaerobic archaeon, lacks the structural features for the binding of 2′-phosphate of nicotinamide adenine dinucleotide phosphate (NADPH), and this feature has justified the observed lack of activity with NADPH; NADH has also been reported to be ineffective. Our recent phylogenetic analysis identified Ta-TrxR as closely related to the NADHdependent enzymes of Thermotoga maritima and Desulfovibrio vulgaris, both being anaerobic bacteria. This observation instigated a reexamination of the activity of the enzyme, which showed that Ta-TrxR is NADH dependent; the apparent Km for NADH was 3.1 μM, a physiologically relevant value. This finding is consistent with the observation that NADH:TrxR has thus far been found primarily in anaerobic bacteria and archaea.en
dc.publisherACS Publicationsen
dc.rightsCreative Commons Attribution-NonCommercial 4.0 Internationalen
dc.titleA Reexamination of Thioredoxin Reductase from Thermoplasma acidophilum, a Thermoacidophilic Euryarchaeon, Identifies It as an NADH-Dependent Enzymeen
dc.typeArticle - Refereeden
dc.title.serialACS Omegaen

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Creative Commons Attribution-NonCommercial 4.0 International
License: Creative Commons Attribution-NonCommercial 4.0 International