腺嘌呤核苷酸对植物乙酰辅酶 A 羧化酶的调节。
Regulation of Plant Acetyl-CoA Carboxylase by Adenylate Nucleotides.
机构信息
Department of Biochemistry and Biophysics, University of California, Davis, California 95616.
出版信息
Plant Physiol. 1983 May;72(1):50-5. doi: 10.1104/pp.72.1.50.
Abstract
The assay of acetyl-CoA carboxylase (EC 6.4.1.2) does not follow ideal zero-order kinetics when assayed in a crude extract from wheat (Triticum aestivum L.) germ. Our results show that the lack of ideality is the consequence of contamination by ATPase and adenylate kinase. These enzyme activities generate significant amounts of ADP and AMP in the assay mixture, thus limiting the availability of ATP for the carboxylase reaction. Moreover, ADP and AMP are competitive inhibitors, with respect to ATP, of acetyl-CoA carboxylase. Similar relationships between adenylate nucleotides and acetyl-CoA carboxylase are found in isolated chloroplasts. There is no evidence that acetyl-CoA carboxylase activity in the extracts of the plant systems examined is altered by covalent modification, such as a phosphorylation-dephosphorylation cycle. A scheme is presented that illustrates the dependency of acetyl-CoA carboxylase and fatty acid synthesis on the energy demands of the chloroplasts in vivo.
摘要
当用从小麦（Triticum aestivum L.）胚芽的粗提物中测定乙酰辅酶 A 羧化酶（EC 6.4.1.2）时，其测定不符合理想的零级动力学。我们的结果表明，这种不理想性是由于 ATP 酶和腺苷酸激酶的污染所致。这些酶活性在测定混合物中产生大量的 ADP 和 AMP，从而限制了羧化酶反应中 ATP 的可用性。此外，ADP 和 AMP 是乙酰辅酶 A 羧化酶相对于 ATP 的竞争性抑制剂。在分离的叶绿体中也发现了类似的腺嘌呤核苷酸与乙酰辅酶 A 羧化酶之间的关系。没有证据表明所研究的植物系统提取物中的乙酰辅酶 A 羧化酶活性受到共价修饰（如磷酸化-去磷酸化循环）的改变。本文提出了一个方案，说明了乙酰辅酶 A 羧化酶和脂肪酸合成与叶绿体在体内的能量需求之间的依赖关系。
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