ArticleActa crystallographica. Section D, Structural biology2018
Identification of the site of oxidase substrate binding in Scytalidium thermophilum catalase.
Article in Acta crystallographica. Section D, Structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 8 citations in OpenAlex.
- Structural insights for enhanced ROS detoxification of eKatE, a recently identified catalase in atypical E. coli.The FEBS journal · 2026Article
- Investigation of how gate residues in the main channel affect the catalytic activity of Scytalidium thermophilum catalase.Acta crystallographica. Section D, Structural biology · 2024Article
- Monofunctional Heme-Catalases.Antioxidants (Basel, Switzerland) · 2022Review
- Pyrolysis molecule ofSaudi journal of biological sciences · 2019Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
The catalase from Scytalidium thermophilum is a homotetramer containing a heme d in each active site. Although the enzyme has a classical monofunctional catalase fold, it also possesses oxidase activity towards a number of small organics, including catechol and phenol. In order to further investigate this, the crystal structure of the complex of the catalase with the classical catalase inhibitor 3-amino-1,2,4-triazole (3TR) was determined at 1.95 Å resolution. Surprisingly, no binding to the heme site was observed; instead, 3TR occupies a binding site corresponding to the NADPH-binding pocket in mammalian catalases at the entrance to a lateral channel leading to the heme. Kinetic analysis of site-directed mutants supports the assignment of this pocket as the binding site for oxidase substrates.
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Registered trials
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