Regulation of phenylalanine hydroxylase: conformational changes upon phosphorylation detected by H/D exchange and mass spectrometry.
Regulation of phenylalanine hydroxylase: conformational changes upon phosphorylation detected by H/D exchange and mass spectrometry.
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DOI：
10.1016/j.abb.2013.03.006
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发表时间：
2013-07-15
影响因子：
3.9
通讯作者：
Fitzpatrick, Paul F.
中科院分区：
文献类型：
--
作者：
Li, Jun;Fitzpatrick, Paul F.
关键词：
苯丙氨酸羟化酶催化肝脏中过量的苯丙氨酸羟化为酪氨酸。该酶受苯丙氨酸和Ser 16磷酸化的别构调节。通过质谱监测的氢/氘交换已用于深入了解磷酸化后的任何结构变化。在催化和调节结构域中的肽显示增加的氘掺入到磷酸化蛋白质中。与苯丙氨酸激活的酶相比，氘被掺入到更少的肽中，并且掺入更慢。这表明，苯丙氨酸羟化酶磷酸化后的构象变化不同于苯丙氨酸活化后的构象变化，且变化范围较小。
The enzyme phenylalanine hydroxylase catalyzes the hydroxylation of excess phenylalanine in the liver to tyrosine. The enzyme is regulated allosterically by phenylalanine and by phosphorylation of Ser16. Hydrogen/deuterium exchange monitored by mass spectrometry has been used to gain insight into any structural change upon phosphorylation. Peptides in both the catalytic and regulatory domains show increased deuterium incorporation into the phosphorylated protein. Deuterium is incorporated into fewer peptides than when the enzyme is activated by phenylalanine, and the incorporation is slower. This establishes that the conformational change upon phosphorylation of phenylalanine hydroxylase is different from and less extensive than that upon phenylalanine activation.
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影响因子：
5.6
作者：
Andersen, OA;Stokka, AJ;Hough, E
通讯作者：
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DOI：
10.1016/0006-291x(83)91050-1
发表时间：
1983-01-01
影响因子：
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作者：
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通讯作者：
Fitzpatrick, Paul F.
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通讯作者：
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