L-leucine 5-hydroxylase of Nostoc punctiforme is a novel type of Fe(II)/α-ketoglutarate-dependent dioxygenase that is useful as a biocatalyst.

Makoto Hibi, Takashi Kawashima, Pavel M Sokolov, Sergey V Smirnov, Tomohiro Kodera, Masakazu Sugiyama, Sakayu Shimizu, Kenzo Yokozeki, Jun Ogawa

Index: Appl. Microbiol. Biotechnol. 97(6) , 2467-72, (2013)

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Abstract

L-Leucine 5-hydroxylase (LdoA) previously found in Nostoc punctiforme PCC 73102 is a novel type of Fe(II)/α-ketoglutarate-dependent dioxygenase. LdoA catalyzed regio- and stereoselective hydroxylation of L-leucine and L-norleucine into (2S,4S)-5-hydroxyleucine and (2S)-5-hydroxynorleucine, respectively. Moreover, LdoA catalyzed sulfoxidation of L-methionine and L-ethionine in the same manner as previously described L-isoleucine 4-hydroxylase. Therefore LdoA should be a promising biocatalyst for effective production of industrially useful amino acids.