THE EFFECT OF PHOSPHORYLATION ON PYRUVATE-DEHYDROGENASE

被引：14

作者：

KOROTCHKINA, LG ^{[1
]}

KHAILOVA, LS ^{[1
]}

SEVERIN, SE ^{[1
]}

机构：

[1] RUSSIAN ACAD SCI, AN BAKH BIOCHEM INST, MOSCOW 117071, RUSSIA

来源：

FEBS LETTERS | 1995年 / 364卷 / 02期

关键词：

PYRUVATE DEHYDROGENASE; PROTEIN KINASE; PHOSPHORYLATION; CIRCULAR DICHROISM;

D O I：

10.1016/0014-5793(95)00382-J

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：

Phosphorylation of the pyruvate dehydrogenase component (E1) of the muscle pyruvate dehydrogenase complex (PDC) by E1-kinase inhibits substrate conversion both in oxidative and non-oxidative reactions. Circular dichroism spectra were used to monitor the effect of phosphorylation on the following stages of the process: holoform formation from apo-E1 and thiamine pyrophosphate (TPP), substrate binding and active site deacetylation, It has been shown that phosphorylation of E1 reduces its affinity for TPP and prevents holo-E1 interaction, with pyruvate. Phosphorylated and dephosphorylated PDC convert 2-hydroxyethyl-TPP in similar ways involving half of their active sites; all active sites of El function in the presence of deacetylating agents. The data obtained suggest that the phosphorylation and substrate binding sites interact with each other.

引用

页码：185 / 188

页数：4

共 16 条

[1]

CATE RL, 1978, J BIOL CHEM, V253, P496

[2]

JAGANNATHAN V, 1952, J BIOL CHEM, V196, P551

[3]

JUNI E, 1956, J BIOL CHEM, V218, P365

[4]

KHAILOVA LS, 1989, ANN NY ACAD SCI, V573, P36, DOI 10.1111/j.1749-6632.1989.tb14985.x

[5]

KHAILOVA LS, 1982, BIOCHEM INT, V5, P525

[6]

KHAILOVA LS, 1991, BIOCHEMISTRY AND PHYSIOLOGY OF THIAMIN DIPHOSPHATE ENZYMES, P251

[7]

KHAILOVA LS, 1977, IOKHIMIYA, V42, P113

[8]

KHAILOVA LS, 1976, BIOKHIMIYA, V56, P1840

[9]

KOROCHKINA LG, 1991, BIOKHIMIYA, V56, P491

[10]

NEMERYA NS, 1984, BIOCHEM INT, V8, P369

← 1 2 →