The framework of polysaccharide monooxygenase structure and chemistry.

Elise A Span, Michael A Marletta

Journal: Current opinion in structural biology 2016;35():93-9

PMID: 26615470

Full Text on Elsevier Science View on PubMed

Abstract

Polysaccharide monooxygenases, or PMOs (also known as lytic PMOs or LPMOs), are a group of enzymes discovered in recent years to catalyze the oxidative degradation of carbohydrate polymers. The PMO catalytic domain has a β-sandwich fold that bears a strong resemblance to both immunoglobulin (Ig) and fibronectin type III (FnIII) domains. PMOs are secreted by fungi and bacteria, and there is recent evidence for their roles in pathogenesis, in addition to biomass processing. This review addresses the biological origins and functions of emerging PMO families, as well as describes the aspects of PMO structure that support the chemistry of copper-catalyzed, oxidative polysaccharide degradation.

Address: Biophysics Graduate Group, University of California, Berkeley, Berkeley, CA 94720, United States.; Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720, United States; Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720, United States. Electronic address: [email protected].

DOI: 10.1016/j.sbi.2015.10.002

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MeSH Terms: Catalytic Domain, Mixed Function Oxygenases, Polysaccharides