Abstract
Mammalian mitochondrial pyruvate dehydrogenase complexes (PDCs) are regulated in part by reversible phosphorylation (1–3). Pyruvate dehydrogenase kinase (EC 2. 7. 1. 99) is an integral component of these complexes. This kinase catalyzes the multi-site phosphorylation of the E1α-subunit of the pyruvate dehydrogenase (EC 1.2.4.1, PDH) component of the complex, resulting in complete inactivation (4). Dephosphorylation, catalyzed by phospho-pyruvate dehydrogenase phosphatase, reactivates the complex. Regulation of mammalian PDH-kinase plays an important role in the overall regulation of PDC activity (5,6).
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Miernyk, J.A., Randall, D.D. (1987). Some Properties of Plant Mitochondrial Pyruvate Dehydrogenase Kinases. In: Moore, A.L., Beechey, R.B. (eds) Plant Mitochondria. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-3517-5_38
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DOI: https://doi.org/10.1007/978-1-4899-3517-5_38
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