Role of Central Channel on Catalytic Activity of Scytalidium Catalase | Chapter 6 | Contemporary Research and Perspectives in Biological Science Vol. 9

Catalase, an antioxidant metalloenzyme, primarily functions to decompose hydrogen peroxide into water and molecular oxygen. Catalases have been studied for more than a century. Throughout this period, these enzymes have been identified, purified, and described by many organisms. It has been discovered that catalases currently defined as monofunctional are in fact not monofunctional but also have secondary oxidase/peroxidase activity. For example, the thermophilic fungus Scytalidium thermophilum produces an enzyme catalase parallel to growth, which also has phenol oxidase activity in addition to its primary function. The enzyme was named CATPO (catalase/phenol oxidase) because of its dual activity. To investigate the role of secondary activity in the catalytic mechanism, we focused on the central channel, which is one of the channels leading to the active site and is thought to be involved in oxidative activity. Accordingly, the amino acid in the central channel (T372) was selected as the target for this purpose and a point mutation to A372 was performed. The catalase activity of the T372A variant decreased by 10% compared to the wild type CATPO. Phenol oxidase activity was also reduced by 38% in T372A. The results show that the central channel influences catalytic activity and indicate that the threonine residue is important for activity.

 

Author (s) Details

Elif KALE BAKIR
Department of Biology, Faculty of Arts and Sciences, Kocaeli University, 41001, Kocaeli, Turkey.

 

Bedirhan OZTURK
Department of Biology, Institute of Science, Kocaeli University, 41001, Kocaeli, Turkey.

 

Yonca YUZUGULLU KARAKUS
Department of Biology, Faculty of Arts and Sciences, Kocaeli University, 41001, Kocaeli, Turkey.

 

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