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酿酒酵母中的蛋白水解分解代谢物失活

Proteolytic catabolite inactivation in Saccharomyces cerevisiae.

作者信息

Holzer H

机构信息

Biochemisches Institut, Universität Freiburg, West Germany.

出版信息

Revis Biol Celular. 1989;21:305-19.

PMID:2561496
Abstract

Fermentable sugars, when added to cells of Saccharomyces cerevisiae growing on a non-fermentable carbon source, cause repression of the synthesis of certain enzymes ("catabolite repression") and in addition inactivation of a smaller group of enzymes ("catabolite inactivation"). Enzymes for which "catabolite inactivation" has been observed are listed herein. In five cases, it has been shown that the mechanism of catabolite inactivation is proteolytic in nature. Our present knowledge on the conditions and the mechanisms of initiation of inactivation and the biological significance of the proteolytic inactivation is summarized for these five enzymes: cytoplasmic malate dehydrogenase, aminopeptidase I, fructose-1,6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase and isocitrate lyase. With the exception of aminopeptidase I, these enzymes are key enzymes of gluconeogenesis in S. cerevisiae. It is obvious that gluconeogenesis is no longer necessary, if a fermentable carbon source is available.

摘要

当将可发酵糖添加到以不可发酵碳源生长的酿酒酵母细胞中时,会导致某些酶的合成受到抑制(“分解代谢物阻遏”),此外还会使一小部分酶失活(“分解代谢物失活”)。本文列出了已观察到“分解代谢物失活”的酶。在五个案例中,已表明分解代谢物失活的机制本质上是蛋白水解的。针对这五种酶总结了我们目前关于失活起始条件和机制以及蛋白水解失活的生物学意义的知识:细胞质苹果酸脱氢酶、氨肽酶I、果糖-1,6-二磷酸酶(FBPase)、磷酸烯醇式丙酮酸羧激酶和异柠檬酸裂解酶。除氨肽酶I外,这些酶是酿酒酵母中糖异生的关键酶。显然,如果有可发酵碳源,糖异生就不再必要。

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