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

Applied Microbiology and Biotechnology
Makoto HibiJun Ogawa

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.

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Aug 9, 2011·Applied and Environmental Microbiology·Makoto HibiJun Ogawa

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Citations

Aug 6, 2013·Chemistry & Biology·Yi-Ling DuKatherine S Ryan
Oct 3, 2014·Bioscience, Biotechnology, and Biochemistry·Takatoshi KimuraJun Ogawa
Dec 13, 2016·Chemical Reviews·Man-Cheng TangYi Tang
Jan 24, 2016·Applied and Environmental Microbiology·Makoto HibiJun Ogawa
Apr 16, 2020·Applied Microbiology and Biotechnology·Ryotaro Hara, Kuniki Kino
Feb 6, 2021·Accounts of Chemical Research·Carter N Stout, Hans Renata
Jun 5, 2021·Organic & Biomolecular Chemistry·Lassi Matti Petteri HeiniläKaarina Sivonen
Feb 14, 2019·Journal of the American Chemical Society·Madison DavidsonWei-Chen Chang
Aug 21, 2021·Synlett : Accounts and Rapid Communications in Synthetic Organic Chemistry·Hans Renata
May 18, 2018·The Journal of Organic Chemistry·Christian R Zwick, Hans Renata

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