1. BRC Science Highlight
Discovery of a new type of bacterial enzyme able to cleave bonds in lignin
Objective Expand our knowledge of enzymes that cleave β-aryl ether bonds, the most abundant linkage in lignin.
Approach
Identify glutathione S-transferase (GST) enzymes required to cleave β-aryl ether bonds in Novosphingobium aromaticivorans.
Describe the properties and phylogenetic distribution of a newly discovered class of β-etherase GSTs.
Results/Impacts
A newly discovered heterodimeric β(R)-aryl etherase GST (BaeAB) is catalytically comparable to – or more efficient than – other known enzymes.
The subunits of this β-etherase are phylogenetically distinct from each other and from those in other reported β-etherases.
Understanding these enzymes will inform new strategies for processing lignin into commodity chemicals.
Notes:
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Phylogenetic tree of GSTs known or predicted to catalyze reactions involved in the sphingomonad pathway for breaking the β-aryl ether bond.
Kontur, W. S. et al. “A heterodimeric glutathione S-transferase that stereospecifically breaks lignin’s β(R)-aryl ether bond reveals the diversity of bacterial β-etherases.” Journal of Biological Chemistry 294, (2019) [DOI: /jbc.RA ].
GLBRC February 2019