Special Issue "Lytic Polysaccharide Monooxygenases: Diversity and Molecular Events"
Deadline for manuscript submissions: 30 June 2021.
Interests: plant cell wall degrading enzymes; industrial biotechnology; protein chemistry; lytic polysaccharide monooxygenases
Lytic polysaccharide monooxygenases (LPMOs) are mononuclear copper enzymes that catalyze the oxidative cleavage of glycosidic bonds. They are characterized by two histidine residues that coordinate copper in a configuration termed the Cu-histidine brace. Although first identified in bacteria and fungi, LPMOs have since been found in all biological kingdoms. LPMOs are now included in commercial enzyme cocktails used in industrial biorefineries. This has led to increased process yield due to the synergistic action of LPMOs with glycoside hydrolases. However, the introduction of LPMOs makes control of the enzymatic step in industrial stirred-tank reactors more challenging, and the operational stability of the enzymes is reduced. It is clear that much is still to be learned about the interaction between LPMOs and their complex natural and industrial environments, and fundamental scientific studies are required toward this end. Several atomic-resolution structures have been solved providing detailed information on the Cu-coordination sphere and the interaction with the polysaccharide substrate. However, the molecular mechanisms of LPMOs are still the subject of intense investigation, the key question being how the proteinaceous environment controls the copper cofactor toward activation of the O–O bond in O2 and cleavage of the glycosidic bonds in polysaccharides. This Special Issue will focus on characterization of LPMOs and the molecular events involved in catalysis.
Prof. Katja Salomon Johansen
Manuscript Submission Information
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- catalytic mechanism
- roles in biological
- biotechnological application