The framework of polysaccharide monooxygenase structure and chemistry

Elise A Span; Michael A Marletta

doi:10.1016/j.sbi.2015.10.002

The framework of polysaccharide monooxygenase structure and chemistry

Curr Opin Struct Biol. 2015 Dec:35:93-9. doi: 10.1016/j.sbi.2015.10.002. Epub 2015 Nov 23.

Authors

Elise A Span¹, Michael A Marletta²

Affiliations

¹ Biophysics Graduate Group, University of California, Berkeley, Berkeley, CA 94720, United States.
² 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: marletta@berkeley.edu.

PMID: 26615470
DOI: 10.1016/j.sbi.2015.10.002

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.

Publication types

Research Support, Non-U.S. Gov't
Review

MeSH terms

Catalytic Domain
Mixed Function Oxygenases / chemistry*
Mixed Function Oxygenases / classification
Mixed Function Oxygenases / metabolism*
Polysaccharides / metabolism*

Substances

Polysaccharides
Mixed Function Oxygenases