Abstract
MarH is an essential epimerase that catalyzes the isomerization of 3R-β-methyl-indolepyruvate (β-MeInPy) to 3S-β-MeInPy, which is the important precursor for biosynthesis of Maremycins. Biophysical study of the structure of MarH would be informative for better understanding of its catalytic mechanism and feasible application of the enzyme in isomerization reaction. Here, we report the backbone and side-chain NMR chemical shift assignments of MarH, which lays a foundation for further structural and mechanical study of the enzyme.
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