l-Leucine 5-hydroxylase of Nostoc punctiforme is a novel type of Fe(II)/[alpha]-ketoglutarate-dependent dioxygenase that is useful as a biocatalyst

l-Leucine 5-hydroxylase (LdoA) previously found in Nostoc punctiforme PCC 73102 is a novel type of Fe(II)/[alpha]-ketoglutarate-dependent dioxygenase. LdoA catalyzed regio- and stereoselective hydroxylation of l-leucine and l-norleucine into (2S,4S)-5-hydroxyleucine and (2S)-5-hydroxynorleucine, res...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 2013-03, Vol.97 (6), p.2467
Main Authors: Hibi, Makoto, Kawashima, Takashi, Sokolov, Pavel M, Smirnov, Sergey V, Kodera, Tomohiro, Sugiyama, Masakazu, Shimizu, Sakayu, Yokozeki, Kenzo, Ogawa, Jun
Format: Article
Language:English
Subjects:
Amino acids
Biocatalysts
Biotechnology
Chemicals
Cloning
E coli
Enzymes
Glycerol
NMR
Nuclear magnetic resonance
Peptides
Physiology
Proteins
Studies
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Summary:l-Leucine 5-hydroxylase (LdoA) previously found in Nostoc punctiforme PCC 73102 is a novel type of Fe(II)/[alpha]-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. [PUBLICATION ABSTRACT]
ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-012-4136-7