Kinetics and Mechanism of Acetate Kinase From Bacillus Stearothermophilus.
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- Ishikawa Haruo
- Department of Chemical Engineering, University of Osaka Prefecture
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- Shiroshima Masahiro
- Department of Chemical Engineering, University of Osaka Prefecture
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- Widjaja Arief
- Department of Chemical Engineering, University of Osaka Prefecture
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- Nakajima Hiroshi
- Biochemistry Department, Unitika Research and Development Center
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- Tsurutani Ryoichi
- Biochemistry Department, Unitika Research and Development Center
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The initial rates of ATP regeneration catalyzed by acetate kinase (ATP: acetate phosphotransferase; EC 2.7.2.1) from Bacillus stearothermophilus were measured under a wide range of MgADP–, acetyl phosphate, MgATP2– and acetate concentrations. The experimental results showed that the enzyme exhibited positive co-operativity for MgATP2– and no co-operativity for MgADP–, acetyl phosphate and acetate. Furthermore, the initial rates of the forward reaction, in which MgATP2– and acetate were produced from MgADP– and acetyl phosphate, were inhibited by MgATP2– and acetate, and those of the reverse reaction were inhibited by MgADP– and acetyl phosphate. The initial rate data were correlated well by using the rate equation derived based on the assumption that the reaction obeys the general reaction scheme based on the Random Bi Bi mechanism, and on the previous experimental result that the enzyme behaves like a dimeric enzyme, even though it is a tetrameric enzyme.
収録刊行物
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- JOURNAL OF CHEMICAL ENGINEERING OF JAPAN
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JOURNAL OF CHEMICAL ENGINEERING OF JAPAN 28 (5), 517-524, 1995
公益社団法人 化学工学会
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詳細情報 詳細情報について
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- CRID
- 1390001204565948160
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- NII論文ID
- 10002134325
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- NII書誌ID
- AA00709658
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- COI
- 1:CAS:528:DyaK2MXptVCnsLk%3D
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- ISSN
- 18811299
- 00219592
- http://id.crossref.org/issn/00219592
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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
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可