Characterization of the oxaloacetate decarboxylase and pyruvate kinase-like activities of Saccharomyces cerevisiae and Anaerobiospirillum succiniciproducens phosphoenolpyruvate carboxykinases
Characterization of the oxaloacetate decarboxylase and pyruvate kinase-like activities of Saccharomyces cerevisiae and Anaerobiospirillum succiniciproducens phosphoenolpyruvate carboxykinases
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DOI：
10.1023/a:1020602222808
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发表时间：
1999-08-01
期刊：
影响因子：
--
通讯作者：
Cardemil, E
中科院分区：
文献类型：
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作者：
Jabalquinto, AM;Laivenieks, M;Cardemil, E
磷酸烯醇丙酮酸羧激酶（PEPCKs）的两个成员（酿酒酵母和琥珀酸厌氧螺旋菌）在草酰乙酸（OAA）脱羧酶和丙酮酸激酶样活性方面进行了比较研究。丙酮酸激酶样活性依赖于Mn2+的存在；在相同浓度下，Mg2+无效。这些活性被两种金属离子的组合协同激活。对琥珀酸链球菌和酿酒链球菌PEPCKs活性的V-max分别为主反应的0.13%和1.2%。OAA脱羧酶活性与核苷酸无关，且活性由Mn2+和Mg2+依次递减。AMP是这些反应的活化剂。琥珀酸葡萄球菌PEPCKs和酿酒葡萄球菌PEPCKs中OAA脱羧酶活性的V-max分别为pep生成反应的4%和0.2%。
Two members of the ATP-dependent class of phosphoenolpyruvate carboxykinases (PEPCKs) (Saccharomyces cerevisiae and Anaerobiospirillum succiniciproducens) have been comparatively studied with regard to their oxaloacetate (OAA) decarboxylase and pyruvate kinase-like activities. The pyruvate kinase-like activities were dependent on the presence of Mn2+; at the same concentrations Mg2+ was not effective. These activities were synergistically activated by a combination of both metal ions. V-max, for these activities in A. succiniciproducens and S. cerevisiae PEPCKs was 0.13% and 1.2% that of the principal reaction, respectively. The OAA decarboxylase activity was nucleotide independent and, with decreasing order of effectiveness, these activities were supported by Mn2+ and Mg2+. AMP is an activator of these reactions. V-max for the OAA decarboxylase activities in A. succiniciproducens and S. cerevisiae PEPCKs was 4% and 0.2% that of the PEP-forming reaction, respectively.