Purification and Characterization of Fumarase from<i>Corynebacterium glutamicum</i>
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- GENDA Tomoko
- Biological Institute, Faculty of Education, Yamaguchi University
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- WATABE Shoji
- Basic Laboratory Science, Faculty of Health Sciences, Yamaguchi University School of Medicine
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- OZAKI Hachiro
- Biological Institute, Faculty of Education, Yamaguchi University
書誌事項
- タイトル別名
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- Purification and Characterization of Fumarase from Corynebacterium glutamicum
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抄録
Fumarase (EC 4.2.1.2) from Corynebacterium glutamicum (Brevibacterium flavum) ATCC 14067 was purified to homogeneity. Its amino-terminal sequence (residues 1 to 30) corresponded to the sequence (residues 6 to 35) of the deduced product of the fumarase gene of C. glutamicum (GenBank accession no. BAB98403). The molecular mass of the native enzyme was 200 kDa. The protein was a homotetramer, with a 50-kDa subunit molecular mass. The homotetrameric and stable properties indicated that the enzyme belongs to a family of Class II fumarase. Equilibrium constants (Keq) for the enzyme reaction were determined at pH 6.0, 7.0, and 8.0, resulting in Keq=6.4, 6.1, and 4.6 respectively in phosphate buffer and in 16, 19, and 17 in non-phosphate buffers. Among the amino acids and nucleotides tested, ATP inhibited the enzyme competitively, or in mixed-type, depending on the buffer. Substrate analogs, meso-tartrate, D-tartrate, and pyromellitate, inhibited the enzyme competitively, and D-malate in mixed-type.
収録刊行物
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 70 (5), 1102-1109, 2006
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206472818560
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- NII論文ID
- 10018530992
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- NII書誌ID
- AA10824164
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- COI
- 1:STN:280:DC%2BD283os1ygug%3D%3D
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- ISSN
- 13476947
- 09168451
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- NDL書誌ID
- 7925895
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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