Linn T C, Pettit F H, Reed L J
Proc Natl Acad Sci U S A. 1969 Jan;62(1):234-41. doi: 10.1073/pnas.62.1.234.
This paper reports the discovery that the activity of the multienzyme pyruvate dehydrogenase complex from beef kidney mitochondria is regulated by a phosphorylation-dephosphorylation reaction sequence. The site of this regulation is the pyruvate dehydrogenase component of the complex. Phosphorylation and concomitant inactivation of pyruvate dehydrogenase are catalyzed by an ATP-specific kinase (i.e., a pyruvate dehydrogenase kinase), and dephosphorylation and concomitant reactivation are catalyzed by a phosphatase (i.e., a pyruvate dehydrogenase phosphatase). The kinase and the phosphatase appear to be regulatory subunits of the pyruvate dehydrogenase complex.
本文报道了一项发现，即来自牛肾线粒体的多酶丙酮酸脱氢酶复合体的活性受磷酸化-去磷酸化反应序列调控。该调控位点是复合体中的丙酮酸脱氢酶组分。丙酮酸脱氢酶的磷酸化及伴随的失活由一种ATP特异性激酶（即丙酮酸脱氢酶激酶）催化，而去磷酸化及伴随的重新激活则由一种磷酸酶（即丙酮酸脱氢酶磷酸酶）催化。激酶和磷酸酶似乎是丙酮酸脱氢酶复合体的调节亚基。
