Understanding the biotechnological potential of bifunctional enzyme: catalase-phenol oxidase

Chi Trinh, Chi Trinh
Smith, Mark
Pearson, Arwen
Ögel, Zümrüt Begüm
Mc Pherson, Michael J.
Catalases are common enzymes in all aerobic and many anaerobic organisms. Their main function is the decomposition of hydrogen peroxide into oxygen and water. Four classes of catalases have been defined including monofunctional heme-containing catalases, catalase–peroxidases, manganese catalases, and minor catalases. Although they have been studied for many years, a secondary peroxide-independent oxidative function of catalase is regarded as a new term discovery in the literature. Catalase–phenol oxidase (CATPO) is among the monofunctional heme-containing catalases and shows phenol oxidase activity resembling catechol oxidases, but also as well as having some features of laccases. The active site of the enzyme is buried deep inside a structurally highly conserved homotetramer. Channels leading to the active site have been identified as potential routes for substrate flow and product release, although evidence in support of this model is limited. Analysis of the crystal structure identified six residues lying in main channel which are likely to be directly or indirectly involved in substrate binding and catalysis. Eight single replacement mutants of CATPO from Scytalidium thermophilum have been prepared, isolated and then characterized kinetically, spectroscopically and crystallographically. We have obtained crystals of recombinant CATPO that diffract to 1.4 Å and are pursuing crystals of CATPO mutants.


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Citation Formats
Y. YÜZÜGÜLLÜ, C. T. Chi Trinh, M. Smith, A. Pearson, Z. B. Ögel, and M. J. Mc Pherson, “Understanding the biotechnological potential of bifunctional enzyme: catalase-phenol oxidase,” NEW BIOTECHNOLOGY, pp. 0–0, 2012, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/50078.