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Identification of the site of oxidase substrate binding in Scytalidium thermophilum catalase

DOI: 10.1107/S2059798318010628 DOI Help

Authors: Yonca Yuzugullu Karakus (Kocaeli University) , Gunce Goc (Kocaeli University) , Sinem Balci (Kocaeli University) , Briony A. Yorke (Universität Hamburg) , Chi H. Trinh (University of Leeds) , Michael J. Mcpherson (University of Leeds) , Arwen Pearson (Universität Hamburg) , Briony A. Yorke (Universität Hamburg)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section D Structural Biology , VOL 74 , PAGES 979 - 985

State: Published (Approved)
Published: October 2018
Diamond Proposal Number(s): 6386

Open Access Open Access

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.

Journal Keywords: catalase; Scytalidium thermophilum; oxidase; 3-amino-1,2,4-triazole; NADPH; binding pocket; lateral channel

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography

Other Facilities: ESRF

Documents:
S2059798318010628.pdf