Histidine modifying agents abolish pyruvate dehydrogenase kinase activity

被引：13

作者：

Mooney, BP

David, NR

Thelen, JJ

Miernyk, JA

Randall, DD

机构：

[1] Univ Missouri, Dept Biochem, Columbia, MO 65211 USA

[2] ARS, Plant Genet Res Unit, USDA, Columbia, MO 65211 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2000年 / 267卷 / 02期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1006/bbrc.1999.1994

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：

Pyruvate dehydrogenase kinase (PDK) specifically phosphorylates the E1 alpha subunit of the pyruvate dehydrogenase complex (PDC). Sequence analysis of cloned PDKs led to the proposal that they are mechanistically related to prokaryotic 2-component His-kinases. The reaction mechanism of protein His-kinases involves autophosphorylation of a specific His residue followed by phosphotransfer to an Asp residue. Treatment of recombinant Arabidopsis thaliana PDR with the His-directed reagents diethyl pyrocarbonate (DEPC) and dichloro-(2,2':6',2''-terpyridine)platinum(II) dihydrate led to a marked inhibition of autophosphorylation. In addition, DEPC treatment abolished the ability of PDK to trans-phosphorylate and inactivate PDC. These results validate the prediction that PDKs require His residues for activity.

引用

页码：500 / 503

页数：4

共 20 条

[1] NONINVASIVE TAGGING OF PROTEINS WITH AN INORGANIC CHROMOPHORE - SELECTIVITY OF CHLORO(TERPYRIDINE)PLATINUM(II) TOWARD AMINO-ACIDS, PEPTIDES, AND CYTOCHROMES-C [J].