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酿酒酵母辅酶A合成蛋白复合体

Coenzyme A-synthesizing protein complex of Saccharomyces cerevisiae.

作者信息

Bucovaz E T, Tarnowski S J, Morrison W C, Macleod R M, Morrison J C, Sobhy C M, Rhoades J L, Fryer J E, Wakim J M, Whybrew W D

出版信息

Mol Cell Biochem. 1980 Mar 20;30(1):7-26. doi: 10.1007/BF00215301.

Abstract

The coenzyme A-synthesizing protein complex (CoA-SPC) is a multienzyme complex of Saccharomyces cerevisiae (Bakers' yeast), which has a molecular weight in excess of 200,000 as determined by Sephadex G-200 column chromatography. This multienzyme complex, which is insoluble in the crude yeast cell lysate, has been purified 229-fold. A cellular component of the yeast cell lysate, referred to as t-Factor, with a molecular weight of 400-1000 and chloride ion are involved in the solubilization of CoA-SPC. The CoA-SPC requires L-cysteine, D-pantothenic acid and ATP as substrates. The terminal CoA-SPC-bound intermediate is dephospho-CoA, which is subsequently phosphorylated and released from the complex as CoA. The sequence of reactions for the synthesis of CoA by the CoA-SPC differs significantly from those previously proposed for other systems. It could be that the reaction sequence is unique for the yeast cell.

摘要

辅酶A合成蛋白复合体(CoA-SPC)是酿酒酵母(面包酵母)的一种多酶复合体,通过葡聚糖凝胶G-200柱层析测定,其分子量超过200,000。这种多酶复合体不溶于粗酵母细胞裂解物,已被纯化了229倍。酵母细胞裂解物中的一种细胞成分,称为t因子,分子量为400-1000,以及氯离子参与了CoA-SPC的溶解。CoA-SPC需要L-半胱氨酸、D-泛酸和ATP作为底物。与CoA-SPC结合的末端中间体是脱磷酸辅酶A,随后它被磷酸化并以辅酶A的形式从复合体中释放出来。CoA-SPC合成辅酶A的反应序列与先前为其他系统提出的反应序列有显著差异。可能这种反应序列在酵母细胞中是独特的。

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