| 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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MedLine Citation:
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PMID: 22584432 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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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. |
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Authors:
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Makoto Hibi; Takashi Kawashima; Pavel M Sokolov; Sergey V Smirnov; Tomohiro Kodera; Masakazu Sugiyama; Sakayu Shimizu; Kenzo Yokozeki; Jun Ogawa |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2012-5-16 |
Journal Detail:
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Title: Applied microbiology and biotechnology Volume: - ISSN: 1432-0614 ISO Abbreviation: - Publication Date: 2012 May |
Date Detail:
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Created Date: 2012-5-15 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 8406612 Medline TA: Appl Microbiol Biotechnol Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Industrial Microbiology, Graduate School of Agriculture, Kyoto University, Kitashirakawa-oiwakecho, Sakyo-ku, Kyoto, 606-8502, Japan. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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