U.S. Department of Energy Office of Biological and Environmental Research

BER Research Highlights

Evolution of Substrate Specificity in Bacterial Lytic Polysaccharide Monooxygenases
Published: August 06, 2014
Posted: January 12, 2015

Cellulose is one of the most abundant polysaccharides in nature and one of the primary components of plant cell walls. The biofuels industry has devoted significant efforts to establish processes to convert these energy-rich molecules into sugars that can be fermented into biofuels or other bioproducts. However, the hydrolysis of these polysaccharides, a key step in converting them to biofuels, is difficult due to their crystalline structure, the stability of some bonds within their structure, and how closely they are associated with structure-modifying molecules such as hemicellulose and lignin. Efficient hydrolysis requires a cocktail of different enzymes. Enzymes capable of hydrolyzing these polymers have been identified in various organisms, especially bacteria and fungi, but the pathways for deconstruction of certain polysaccharides, such as cellulose and chitin, are only partially understood. Researchers at the Department of Energy’s Great Lakes Bioenergy Research Center analyzed the sequences, structures, and evolution of two families of enzymes, fungal AA9 and bacterial AA10, both lytic polysaccharide monooxygenases (LPMOs), to understand the factors that influence substrate specificity in these families and to characterize the selective pressures that may have led to their functional diversification. Their sequence similarity suggests that both families share a distant common ancestor and that certain clades within the AA10 family are specialized for different substrates, while others went through a diversifying selection at surface-exposed regions of the protein. Understanding the diversity of these lignocellulosic-degrading enzymes in nature provides information that can help improve enzymatic cocktails used in the biofuels industry.

Reference: Book, A. J., R. M. Yennamalli, T. E. Takasuka, C. R. Currie, G. N. Phillips, and B. G. Fox. 2014. “Evolution of Substrate Specificity in Bacterial AA10 Lytic Polysaccharide Monooxygenases,” Biotechnology for Biofuels 7,109. DOI: 10.1186/1754-6834-7-109. (Reference link)

Contact: Kent Peters, SC-23.2, (301) 903-5549
Topic Areas:

  • Research Area: Genomic Analysis and Systems Biology
  • Research Area: Sustainable Biofuels and Bioproducts
  • Research Area: DOE Bioenergy Research Centers (BRC)
  • Research Area: Structural Biology, Biomolecular Characterization and Imaging

Division: SC-23.2 Biological Systems Science Division, BER


BER supports basic research and scientific user facilities to advance DOE missions in energy and environment. More about BER

Recent Highlights

Aug 24, 2019
New Approach for Studying How Microbes Influence Their Environment
A diverse group of scientists suggests a common framework and targeting of known microbial processes [more...]

Aug 08, 2019
Nutrient-Hungry Peatland Microbes Reduce Carbon Loss Under Warmer Conditions
Enzyme production in peatlands reduces carbon lost to respiration under future high temperatures. [more...]

Aug 05, 2019
Amazon Forest Response to CO2 Fertilization Dependent on Plant Phosphorus Acquisition
AmazonFACE Model Intercomparison. The Science Plant growth is dependent on the availabi [more...]

Jul 29, 2019
A Slippery Slope: Soil Carbon Destabilization
Carbon gain or loss depends on the balance between competing biological, chemical, and physical reac [more...]

Jul 15, 2019
Field Evaluation of Gas Analyzers for Measuring Ecosystem Fluxes
How gas analyzer type and correction method impact measured fluxes. The Science A side- [more...]

List all highlights (possible long download time)