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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Folding and stability of different oligomeric states of thiamin diphosphate dependent homomeric pyruvate decarboxylase
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Folding and stability of different oligomeric states of thiamin diphosphate dependent homomeric pyruvate decarboxylase

机译：硫胺二磷酸依赖性同聚丙酮酸脱羧酶的不同寡聚状态的折叠性和稳定性

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摘要

The folding and stability of recombinant homomeric (alpha-only) pyruvate decarboxylase from yeast was investigated. Different oligomeric states (tetramers, dimers and monomers) of the enzyme occur under defined conditions. The enzymatic activity is used as a sensitive probe for structural differences between the active and inactive form (mis-assembled forms. aggregates) of the folded protein. Unfolding kinetics starting from the native protein comprise both the dissociation of the oligomers into monomers and their subsequent denaturation, which could be monitored by stopped-flow kinetics. In the course of unfolding, the tetramers do not directly dissociate into monomers, but via a stable dimeric state. Starting from the unfolded state, a reactivation of homomeric pyruvate decarboxylase requires both refolding to monomers and their correct association to enzymatically active dimers or tetramers. The reactivation yield under the in vitro conditions used follows an optimum behavior. (C) 2002 Elsevier Science B.V All rights reserved. [References: 32]
机译：研究了来自酵母的重组同源（仅阿尔法）丙酮酸脱羧酶的折叠性和稳定性。酶的不同低聚状态（四聚体，二聚体和单体）在定义的条件下发生。酶活性用作折叠蛋白的活性形式和非活性形式（组装错误的形式，聚集体）之间结构差异的灵敏探针。从天然蛋白开始的展开动力学包括寡聚物解离成单体和它们随后的变性，这可以通过停止流动动力学来监测。在展开过程中，四聚体不直接解离成单体，而是通过稳定的二聚体状态解离。从未折叠状态开始，同源丙酮酸脱羧酶的重新活化既需要重新折叠成单体，也需要它们与酶活性二聚体或四聚体正确结合。在所用体外条件下的再活化产率遵循最佳行为。 （C）2002 Elsevier Science B.V保留所有权利。 [参考：32]

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