ArticleCurrent microbiology2017
A Novel Acetaldehyde Dehydrogenase with Salicylaldehyde Dehydrogenase Activity from Rhodococcus ruber Strain OA1.
Article in Current microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- Expression, purification and crystallization of a novel metagenome-derived salicylaldehyde dehydrogenase from Alpine soil.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Update of the list of QPS-recommended biological agents intentionally added to food or feed as notified to EFSA 11: suitability of taxonomic units notified to EFSA until September 2019.EFSA journal. European Food Safety Authority · 2020Article
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5 authors at 1 institution in 1 country.
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Abstract
Salicylaldehyde dehydrogenase (sALDH) can oxidize salicylaldehyde, which is an intermediate in the naphthalene catabolism in bacteria. However, genes encoding sALDH have not been discovered so far in Rhodococcus. Here, we report the discovery of a novel aldehyde dehydrogenase (ALDH) gene in the naphthalene degrader Rhodococcus ruber OA1 based on phylogenetic analysis. Interestingly, apart from ALDH activity, ALDH of R. ruber OA1 (OA1-ALDH) also showed sALDH activity. Moreover, its sALDH specific activity was higher than its ALDH specific activity. Based on a comparison with the ALDH of Thermomonospora curvata DSM 43,183, a putative active site Cys123 and NAD
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