Publications by authors named "Ilya Kolyadenko"
Article Synopsis
- Laccases are important industrial enzymes, but their effectiveness is limited due to stability and functioning conditions, typically performing best in acidic environments and under 60 °C.
- Researchers studied a specific two-domain laccase (2D) from SgfSL that operates in alkaline conditions and elevated temperatures, identifying how polar residues near its trinuclear center (TNC) affect its activity.
- Mutations in the 2D laccase notably altered its activity and efficiency in oxidizing specific substrates, enhancing understanding of laccase structure and functioning, and paving the way for targeted enzyme engineering.
Interleukin-17 (IL-17) is a cytokine produced by the Th17 cells. It is involved in chronic inflammation in patients with autoimmune diseases, such as rheumatoid arthritis, systemic lupus erythematosus, multiple sclerosis, and psoriasis. The antibodies targeting IL-17 and/or IL-17R are therapy tools for these diseases.
View Article and Find Full Text PDFLaccases catalyze the oxidation of substrates with the concomitant reduction of oxygen to water. Recently, we found that polar residues located in tunnels leading to Cu2 and Cu3 ions control oxygen entrance (His 165) and proton transport (Arg 240) of two-domain laccase (2D) from (SgfSL). In this work, we have focused on optimizing the substrate-binding pocket (SBP) of SgfSL while simultaneously adjusting the oxygen reduction process.
View Article and Find Full Text PDFMulti-copper oxidases are capable of coupling the one-electron oxidation of four substrate equivalents to the four-electron reduction of dioxygen to two molecules of water. This process takes place at the trinuclear copper center of the enzymes. Previously, the main catalytic stages for three-domain (3D) laccases have been identified.
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