『徳島大学 教育・研究者情報データベース (EDB)』---[学外] /
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EID=262419EID:262419, Map:0, LastModified:2014年2月4日(火) 16:06:18, Operator:[大家 隆弘], Avail:TRUE, Censor:0, Owner:[川上 竜巳], Read:継承, Write:継承, Delete:継承.
種別 (必須): 学術論文 (審査論文) [継承]
言語 (必須): 英語 [継承]
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著者 (必須): 1.川上 竜巳 ([徳島大学.大学院社会産業理工学研究部.生物資源産業学域.食料科学系.食料科学分野]/[徳島大学.生物資源産業学部])
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2. (英) Noguchi Chiaki (日) (読)
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3. (英) Higashi Marie (日) (読)
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4. (英) Sakuraba Haruhiko (日) (読)
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5. (英) Ohshima Toshihisa (日) (読)
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題名 (必須): (英) Comparative analysis of the catalytic components in the archaeal dye-linked L-proline dehydrogenase complexes.  (日)    [継承]
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要約 (任意): (英) Two types of hetero-oligomeric dye-linked L-proline dehydrogenases (44 and types) are expressed in the hyperthermophilic archaea belonging to Thermococcales. In both enzymes, the subunit (PDH) is responsible for catalyzing L-proline dehydrogenation. The genes encoding the two enzyme types form respective clusters that are completely conserved among Pyrococcus and Thermococcus strains. To compare the enzymatic properties of PDHs from 44- and -type enzyme complexes, eight PDHs (four of each type) from Pyrococcus furiosus DSM3638, Pyrococcus horikoshii OT-3, Thermococcus kodakaraensis KOD1 JCM12380 and Thermococcus profundus DSM9503 were expressed in Escherichia coli cells and purified to homogeneity using one-step Ni-chelating chromatography. The 44-type PDHs showed greater thermostability than most of the -type PDHs: the former retained more than 80 % of their activity after heating at 70 °C for 20 min, while the latter showed different thermostabilities under the same conditions. In addition, the 44-type PDHs utilized ferricyanide as the most preferable electron acceptor, whereas -type PDHs preferred 2, 6-dichloroindophenol, with one exception. These results indicate that the differences in the enzymatic properties of the PDHs likely reflect whether they were from an - or 44-type complex, though the wider divergence observed within -type PDHs based on the phylogenetic analysis may also be responsible for their inconsistent enzymatic properties. By contrast, differences in the kinetic parameters among the PDHs did not reflect the complex type. Interestingly, the k cat value for free 44-type PDH from P. horikoshii was much larger than the value for the same subunit within the 44-complex. This indicates that the isolated PDH could be a useful element for an electrochemical system for detection of L-proline.  (日)    [継承]
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誌名 (必須): Applied Microbiology and Biotechnology ([Springer-Verlag])
(pISSN: 0175-7598, eISSN: 1432-0614)

ISSN (任意): 1432-0614
ISSN: 0175-7598 (pISSN: 0175-7598, eISSN: 1432-0614)
Title: Applied microbiology and biotechnology
Title(ISO): Appl Microbiol Biotechnol
Supplier: Springer Online Journal Archive
Publisher: Springer Berlin Heidelberg
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(必須): 3419 3427 [継承]
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年月日 (必須): 西暦 2013年 0月 初日 (平成 25年 0月 初日) [継承]
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DOI (任意): 10.1007/s00253-012-4201-2    (→Scopusで検索) [継承]
PMID (任意): 22752365    (→Scopusで検索) [継承]
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備考 (任意): 1.(英) Article.ELocationID: 10.1007/s00253-012-4201-2  (日)    [継承]
2.(英) Article.Affiliation: Analytical Research Center for Experimental Sciences, Saga University, 1 Honjo-machi, Saga, 840-8502, Japan.  (日)    [継承]
3.(英) Article.PublicationTypeList.PublicationType: Journal Article  (日)    [継承]

標準的な表示

和文冊子 ● Ryushi Kawakami, Chiaki Noguchi, Marie Higashi, Haruhiko Sakuraba and Toshihisa Ohshima : Comparative analysis of the catalytic components in the archaeal dye-linked L-proline dehydrogenase complexes., Applied Microbiology and Biotechnology, Vol.97, No.8, 3419-3427, 2013.
欧文冊子 ● Ryushi Kawakami, Chiaki Noguchi, Marie Higashi, Haruhiko Sakuraba and Toshihisa Ohshima : Comparative analysis of the catalytic components in the archaeal dye-linked L-proline dehydrogenase complexes., Applied Microbiology and Biotechnology, Vol.97, No.8, 3419-3427, 2013.

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