草酰乙酸及其结构类似物对柠檬酸裂解酶的失活作用

Robert Eisenthal, S.S. Tate, S.P. Datta
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引用次数: 9

摘要

1.1. 研究了草酰乙酸对柠檬酸裂解酶(柠檬酸-草酰乙酸裂解酶,EC 4.1.3.6)的失活作用。在pH 7 ~ 9时,对不同总草酰乙酸和镁浓度的失活pH谱进行了研究,结果表明烯醇类草酰乙酸的镁配合物参与了失活。考察了草酰乙酸酮和烯醇结构类似物的抑制作用:l-苹果酸、α、α-二甲基草酰乙酸、酒石酸盐、α、α-二氟草酰乙酸盐、丙酮酸盐、酮丙酸盐和异苹果酸盐。这些结果以及其他二价金属阳离子的影响表明,失活位点与柠檬酸盐裂解的活性位点相同。失活是不可逆的,并且与时间和浓度有关。游离的草酰乙酸不会使酶失活。该失活现象具有很高的结构特异性,需要具有可电离α-羟基的直链四碳二羧酸,以及二价金属阳离子的存在。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Inactivation of citrate lyase by oxaloacetate and its structural analogues

  • 1.

    1. The inactivation of citrate lyase (citrate-oxaloacetate lyase, EC 4.1.3.6) by oxaloacetate has been investigated.

  • 2.

    2. Studies of the pH profiles of inactivation at pH 7–9 with varying total oxaloacetate and magnesium concentrations show that the magnesium complexes of enolic oxaloacetate are involved.

  • 3.

    3. The inhibitory effects of the following structural analogues of the keto and enol forms of oxaloacetate were examined: l-malate, α,α-dimethyloxaloacetate, tartronate, α,α-difluorooxaloacetate, pyruvate, ketomalonate, and isomalate. These results, and the effect of other divalent metal cations, indicate that the site of the inactivation is identical with the active site for citrate cleavage.

  • 4.

    4. The inactivation is irreversible and is time and concentration dependent. Free oxaloacetate does not inactivate the enzyme.

  • 5.

    5. The inactivation phenomenon has high structural specificity, requiring a straight-chain, four-carbon dicarboxylic acid with an ionisable α-hydroxy group, and the presence of a divalent metal cation.

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