ArticleApplied and environmental microbiology2012
Homologous Alkalophilic and Acidophilic L-Arabinose isomerases reveal region-specific contributions to the pH dependence of activity and stability.
Article in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 19 citations in OpenAlex.
- Characterization of an L-arabinose isomerase from Bacillus coagulans NL01 and its application for D-tagatose production.BMC biotechnology · 2016Article
- The secreted L-arabinose isomerase displays anti-hyperglycemic effects in mice.Microbial cell factories · 2015Article
- Crystallization and preliminary X-ray crystallographic analysis of L-arabinose isomerase from thermophilic Geobacillus kaustophilus.Acta crystallographica. Section F, Structural biology communications · 2014Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To study the pH dependence of l-arabinose isomerase (AI) activity and stability, we compared homologous AIs with their chimeras. This study demonstrated that an ionizable amino acid near the catalytic site determines the optimal pH (pH(opt)) for activity, whereas the N-terminal surface R residues play an important role in determining the pH(opt) for stability.
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Registered trials
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