A novel Fe(II)/α-ketoglutarate-dependent dioxygenase from<i>Burkholderia ambifaria</i>has β-hydroxylating activity of<i>N</i>-succinyl l-leucine

Abstract

An Fe(II)/α-ketoglutarate-dependent dioxygenase, SadA, was obtained from Burkholderia ambifaria AMMD and heterologously expressed in Escherichia coli. Purified recombinant SadA had catalytic activity towards several N-substituted l-amino acids, which was especially strong with N-succinyl l-leucine. With the NMR and LC-MS analysis, SadA converted N-succinyl l-leucine into N-succinyl l-threo-β-hydroxyleucine with >99% diastereoselectivity. SadA is the first enzyme catalysing β-hydroxylation of aliphatic amino acid-related substances and a potent biocatalyst for the preparation of optically active β-hydroxy amino acids.