Kinetics and Mechanism of Acetate Kinase from Bacillus stearothermophilus
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...
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| Veröffentlicht in: | JOURNAL OF CHEMICAL ENGINEERING OF JAPAN 1995, Vol.28(5), pp.517-524 |
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| container_title | JOURNAL OF CHEMICAL ENGINEERING OF JAPAN |
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| creator | Ishikawa, Haruo Shiroshima, Masahiro Widjaja, Arief Nakajima, Hiroshi Tsurutani, Ryoichi |
| description | 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. |
| doi_str_mv | 10.1252/jcej.28.517 |
| format | Article |
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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.</description><identifier>ISSN: 0021-9592</identifier><identifier>EISSN: 1881-1299</identifier><identifier>DOI: 10.1252/jcej.28.517</identifier><identifier>CODEN: JCEJAQ</identifier><language>eng</language><publisher>Tokyo: The Society of Chemical Engineers, Japan</publisher><subject>Allosteric Enzyme ; Analytical, structural and metabolic biochemistry ; ATP Regeneration ; Biochemical Engineering ; Biological and medical sciences ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Random Bi Bi ; Reaction Rate ; Transferases</subject><ispartof>JOURNAL OF CHEMICAL ENGINEERING OF JAPAN, 1995, Vol.28(5), pp.517-524</ispartof><rights>1995 The Society of Chemical Engineers, Japan</rights><rights>1996 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 1995</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c551t-f8d86a1cc2903b4e1e208631f89c592947e81e57a58cd995411d951abc597ed83</citedby><cites>FETCH-LOGICAL-c551t-f8d86a1cc2903b4e1e208631f89c592947e81e57a58cd995411d951abc597ed83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2932132$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Ishikawa, Haruo</creatorcontrib><creatorcontrib>Shiroshima, Masahiro</creatorcontrib><creatorcontrib>Widjaja, Arief</creatorcontrib><creatorcontrib>Nakajima, Hiroshi</creatorcontrib><creatorcontrib>Tsurutani, Ryoichi</creatorcontrib><title>Kinetics and Mechanism of Acetate Kinase from Bacillus stearothermophilus</title><title>JOURNAL OF CHEMICAL ENGINEERING OF JAPAN</title><description>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.</description><subject>Allosteric Enzyme</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>ATP Regeneration</subject><subject>Biochemical Engineering</subject><subject>Biological and medical sciences</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. 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| subjects | Allosteric Enzyme Analytical, structural and metabolic biochemistry ATP Regeneration Biochemical Engineering Biological and medical sciences Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Random Bi Bi Reaction Rate Transferases |
| title | Kinetics and Mechanism of Acetate Kinase from Bacillus stearothermophilus |
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