Back to Search
Start Over
The effect of phosphorylation on pyruvate dehydrogenase.
- Source :
-
FEBS letters [FEBS Lett] 1995 May 08; Vol. 364 (2), pp. 185-8. - Publication Year :
- 1995
-
Abstract
- 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 E1 function in the presence of deacetylating agents. The data obtained suggest that the phosphorylation and substrate binding sites interact with each other.
- Subjects :
- Adenosine Triphosphate pharmacology
Animals
Binding Sites
Circular Dichroism
Columbidae
In Vitro Techniques
Kinetics
Muscles enzymology
Phosphorylation
Protein Kinases metabolism
Protein Serine-Threonine Kinases
Pyruvate Dehydrogenase Acetyl-Transferring Kinase
Pyruvates metabolism
Pyruvic Acid
Substrate Specificity
Thiamine Pyrophosphate metabolism
Pyruvate Dehydrogenase Complex chemistry
Pyruvate Dehydrogenase Complex metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 364
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 7750568
- Full Text :
- https://doi.org/10.1016/0014-5793(95)00382-j