Yuzugullu Karakus, Y, Goc, G, Balci, S et al. (4 more authors) (2018) Identification of the site of oxidase substrate binding in Scytalidium thermophilum catalase. Acta crystallographica. Section D, Structural biology, 74 (Pt 10). pp. 979-985. ISSN 2059-7983
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2018, Author(s). This is an open access article under the terms of the Creative Commons Attribution License (CC-BY). |
Keywords: | catalase; Scytalidium thermophilum; oxidase; 3-amino-1,2,4-triazole; NADPH; binding pocket; lateral channel |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Synthetic Biology (Leed) |
Depositing User: | Symplectic Publications |
Date Deposited: | 17 Oct 2018 10:51 |
Last Modified: | 17 Oct 2018 10:51 |
Status: | Published |
Publisher: | International Union of Crystallography |
Identification Number: | 10.1107/s2059798318010628 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:137252 |