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Histidine modifying agents abolish pyruvate dehydrogenase kinase activity.

Abstract：

:Pyruvate dehydrogenase kinase (PDK) specifically phosphorylates the E1alpha 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 PDK 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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Mooney BP,David NR,Thelen JJ,Miernyk JA,Randall DD

doi

10.1006/bbrc.1999.1994

subject

Has Abstract

pub_date

2000-01-19 00:00:00

pages

500-3

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(99)91994-0

journal_volume

267

pub_type

杂志文章

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