l-Leucine 5-hydroxylase of Nostoc punctiforme is a novel type of Fe(II)/α-ketoglutarate-dependent dioxygenase that is useful as a biocatalyst
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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.
Keywordsl-Leucine 5-hydroxylase Fe(II)/α-ketoglutarate-dependent dioxygenase (2S,4S)-5-Hydroxyleucine (2S)-5-Hydroxynorleucine Nostocyclopeptide
This work was partially supported by Grants-in-Aid for Scientific Research (no. 21780070 and 24688010 to M. Hibi, and no. 22658027 and 23248014 to J. Ogawa) from the Ministry of Education, Culture, Sports, Science and Technology of Japan.
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