Asp295 Stabilizes the Active-Site Loop Structure of Pyruvate Dehydrogenase, Facilitating Phosphorylation of Ser292 by Pyruvate Dehydrogenase-Kinase

We have developed an in vitro system for detailed analysis of reversible phosphorylation of the plant mitochondrial pyruvate dehydrogenase complex, comprising recombinant Arabidopsis thalianaα2β2-heterotetrameric pyruvate dehydrogenase (E1) plus A. thaliana E1-kinase (AtPDK). Upon addition of MgATP,...

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Hlavní autoři: Hirani, Tripty A., Tovar-Méndez, Alejandro, Miernyk, Ján A., Randall, Douglas D.
Médium: Artigo
Jazyk:Inglês
Vydáno: SAGE-Hindawi Access to Research 2011
Témata:
Research Article
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3034952/
https://ncbi.nlm.nih.gov/pubmed/21318135
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.4061/2011/939068
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