巴基斯坦卢比
丙酮酸激酶
糖酵解
生物化学
磷酸甘油酸变位酶
生物
激酶
厌氧糖酵解
丙酮酸脱氢酶激酶
磷酸烯醇丙酮酸羧激酶
丙酮酸羧化酶
细胞生物学
新陈代谢
化学
酶
作者
Matthew G. Vander Heiden,Jason W. Locasale,Kenneth D. Swanson,Hadar Sharfi,Gregory J. Heffron,Daniel Amador‐Noguez,Heather R. Christofk,Gerhard Wagner,Joshua D. Rabinowitz,John M. Asara,Lewis C. Cantley
出处
期刊:Science
[American Association for the Advancement of Science]
日期:2010-09-16
卷期号:329 (5998): 1492-1499
被引量:39
标识
DOI:10.1126/science.1188015
摘要
Glucose Metabolism Revisited Cancer cells are revved up to reproduce rapidly and typically consume glucose rapidly by glycolysis. Why then do cancer cells express an isoform of a rate-limiting enzyme in glycolysis, pyruvate kinase M2, which has decreased activity? Vander Heiden et al. (p. 1492 ) propose that consequent accumulation of phosphoenolpyruvate, with the help of an enzymatic activity that remains to be characterized, can lead to phosphate transfer to phosphoglycerate mutase, another glycolytic enzyme, providing the cell with a different way to make pyruvate. This may allow cancer cells to produce pyruvate without generating excess adenosine triphosphate, which can act through feedback to inhibit glycolyis.
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