FUNCTION OF PHOSPHORYLATION SITES ON PYRUVATE-DEHYDROGENASE

被引:57
作者
TEAGUE, WM [1 ]
PETTIT, FH [1 ]
YEAMAN, SJ [1 ]
REED, LJ [1 ]
机构
[1] UNIV TEXAS,DEPT CHEM,AUSTIN,TX 78712
关键词
D O I
10.1016/0006-291X(79)91672-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Evidence is presented that dephosphorylation of the three phosphorylation sites on bovine kidney pyruvate dehydrogenase by pyruvate dehydrogenase phosphatase is random. The relative rates of dephosphorylation were in the order site 2 > site 3 > site 1. Phosphorylation site 2, and possibly site 3, function, in addition to site 1, as inactivating sites. However, the presence of phosphoryl groups at sites 2 and 3 did not significantly affect the rate of dephosphorylation at site 1 or the rate of reactivation of the enzyme by the phosphatase. The rate-limiting step in the reactivation of phosphorylated pyruvate dehydrogenase is apparently the dephosphorylation at site 1. © 1979.
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收藏
页码:244 / 252
页数:9
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