A novel Fe(II)/α‐ketoglutarate‐dependent dioxygenase from Burkholderia ambifaria has β‐hydroxylating activity of N‐succinyl l‐leucine |
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| Authors: | M Hibi T Kawashima T Kasahara PM Sokolov SV Smirnov T Kodera M Sugiyama S Shimizu K Yokozeki J Ogawa |
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| Institution: | 1. Industrial Microbiology, Graduate School of Agriculture, Kyoto University, Kyoto, Japan;2. Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan;3. Ajinomoto‐Genetika Research Institute, Moscow, Russia;4. Institute of Food Sciences & Technologies Food Product Division, Ajinomoto Co., Inc., Kawasaki, Japan;5. Research Institute for Bioscience Products & Fine Chemicals, Ajinomoto Co., Inc., Kawasaki, Japan;6. Research Institute for Bioscience Products & Fine Chemicals, Ajinomoto Co., Inc., Kawasaki, Japan |
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| 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. |
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| Keywords: | Fe(II)/α ‐ketoglutarate‐dependent dioxygenase N‐substituted l‐amino acid β ‐hydroxylase
Burkholderia ambifaria
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