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type Journal Article
authors Zhao J, Ji W, Ji X, Zhang Q
title Biochemical Characterization of an Arginine 2,3‐aminomutase with Dual Substrate Specificity
journal Chin. J. Chem.
Activity arg.aminomutase
Family arg.aminomutase
sel selected
ui NotFoundInPubMed
year (2020)
volume 38
pages in press
keywords DOI: 10.1002/cjoc.202000119
abstract The radical S‐adenosylmethionine (SAM) aminomutases represent an important pathway for the biosynthesis of β‐amino acids. In this study, we report biochemical characterization of BlsG involved in blasticidin S biosynthesis as a radical SAM arginine 2,3‐aminomutase. We showed that BlsG acts on both L‐arginine and L‐lysine with comparable catalytic efficiencies. Similar dual substrate specificity was also observed for the lysine 2,3‐aminomutase from Escherichia coli (LAMEC). The catalytic efficiency of LAMEC is similar to BlsG, but is significantly lower than the enzyme from Clostridium subterminale (LAMCS), the latter acts only on L‐lysine and not on L‐arginine. Moreover, we showed that enzymes can be grouped into two major phylogenetic clades, each corresponding to a certain C3 stereochemistry of the β‐amino acid product. Our study expands the radical SAM aminomutase members and provides insights into enzyme evolution, supporting a trade‐off between substrate promiscuity and catalytic efficiency.
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last changed 2020/04/23 09:14

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