Histidine modifying agents abolish pyruvate dehydrogenase kinase activity.
Biochem Biophys Res Commun
; 267(2): 500-3, 2000 Jan 19.
Article
en En
| MEDLINE
| ID: mdl-10631090
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.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Piruvato Deshidrogenasa (Lipoamida)
/
Inhibidores de Proteínas Quinasas
/
Histidina
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
2000
Tipo del documento:
Article
País de afiliación:
Estados Unidos