A novel Fe(II)/alpha-ketoglutarate-dependent dioxygenase from Burkholderia ambifaria has beta-hydroxylating activity of N-succinyl L-leucine

作者：Hibi M; Kawashima T; Kasahara T; Sokolov P M; Smirnov S V; Kodera T; Sugiyama M; Shimizu S; Yokozeki K; Ogawa J^*

来源：Letters in Applied Microbiology, 2012, 55(6): 414-419.

DOI：10.1111/j.1472-765X.2012.03308.x

• Fe(II)/alpha-ketoglutarate-dependent dioxygenase
• N-substituted l-amino acid beta-hydroxylase
• Burkholderia ambifaria

An Fe(II)/alpha-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-beta-hydroxyleucine with >99% diastereoselectivity. SadA is the first enzyme catalysing beta-hydroxylation of aliphatic amino acid-related substances and a potent biocatalyst for the preparation of optically active beta-hydroxy amino acids.

• 出版日期2012-12