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Methods Enzymol. 2011;494:301-26. doi: 10.1016/B978-0-12-385112-3.00015-9.

2-oxoacid metabolism in methanogenic CoM and CoB biosynthesis.

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  • 1Oak Ridge National Laboratory, Biosciences Division and University of Tennessee Knoxville, Microbiology Department, Oak Ridge, Tennessee, USA.


Coenzyme M (CoM) and coenzyme B (CoB) are essential for methane production by the euryarchaea that employ this specialized anaerobic metabolism. Two pathways are known to produce CoM, 2-mercaptoethanesulfonate, and both converge on the 2-oxoacid sulfopyruvate. These cells have recruited the rich biochemistry of amino acid and 2-oxoacid metabolizing enzymes to produce a compound that resembles oxaloacetate, but with a more stable and acidic sulfonate group. 7-Mercaptoheptanoylthreonine phosphate, CoB, likewise owes its carbon backbone to a 2-oxoacid. Three enzymes recruited from leucine biosynthesis have evolved to catalyze the elongation of 2-oxoglutarate to 2-oxosuberate in CoB biosynthesis. This chapter describes the enzymology, synthesis, and analytical techniques used to study 2-oxoacid metabolism in these pathways. Protein structure and mechanistic information from enzymes provide insight into the evolution of new enzymatic activity, and the evolution of substrate specificity from promiscuous enzyme scaffolds.

Copyright © 2011 Elsevier Inc. All rights reserved.

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