Identification of the site of oxidase substrate binding in Scytalidium thermophilum catalase
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, cilt.74, ss.979-985, 2018 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 74
- Basım Tarihi: 2018
- Doi Numarası: 10.1107/s2059798318010628
- Dergi Adı: ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Sayfa Sayıları: ss.979-985
- Anahtar Kelimeler: catalase, Scytalidium thermophilum, oxidase, 3-amino-1,2,4-triazole, NADPH, binding pocket, lateral channel, MACROMOLECULAR CRYSTALLOGRAPHY EXPERIMENTS, X-RAY-DIFFRACTION, PENICILLIUM VITALE, ESCHERICHIA-COLI, PHENOL OXIDASE, REFINEMENT, PROTEIN, AMINOTRIAZOLE, PARAMETERS, DIVERSITY
- Kocaeli Üniversitesi Adresli: Evet
Özet
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 angstrom 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.