Abstract |
The PDH ( pyruvate dehydrogenase) multi- enzyme complex catalyses a key regulatory step in oxidative glycolysis. Phosphorylation of the E1 subunit of the complex on serine residues results in the inactivation of enzyme activity. A family of four dedicated PDH kinase isoenzymes exists, each of which displays a distinct tissue-specific expression profile. AZD7545 is one of a series of PDH kinase inhibitors developed for the treatment of type 2 diabetes. The isoenzyme-selectivity profile of AZD7545 and related compounds is described and the consequences for their in vivo mode of action are discussed.
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Authors | J A Morrell, J Orme, R J Butlin, T E Roche, R M Mayers, E Kilgour |
Journal | Biochemical Society transactions
(Biochem Soc Trans)
Vol. 31
Issue Pt 6
Pg. 1168-70
(Dec 2003)
ISSN: 0300-5127 [Print] England |
PMID | 14641019
(Publication Type: Journal Article)
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Chemical References |
- Enzyme Inhibitors
- Protein Kinase Inhibitors
- Pyruvate Dehydrogenase Acetyl-Transferring Kinase
- Protein Kinases
- Protein Serine-Threonine Kinases
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Topics |
- Animals
- Enzyme Inhibitors
(pharmacology)
- Liver
(drug effects, enzymology)
- Muscle, Skeletal
(drug effects, enzymology)
- Protein Kinase Inhibitors
- Protein Kinases
- Protein Serine-Threonine Kinases
- Pyruvate Dehydrogenase Acetyl-Transferring Kinase
- Rats
- Rats, Wistar
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