Available online at www.sciencedirect.com ScienceDirect Protein lipoylation: an evolutionarily conserved metabolic regulator of health and disease 1 1 Elizabeth A Rowland , Caroline K Snowden and Ileana M Cristea Lipoylation is a rare, but highly conserved lysine metabolic pathways. This theme of conservation is seen posttranslational modiﬁcation. To date, it is known to occur on across the lipoylated complexes, the proteins that add or only four multimeric metabolic enzymes in mammals, yet these remove this modiﬁcation, as well as the function of proteins are staples in the core metabolic landscape. The lipoylation [4 ,5,6,7 ,8 ]. Given this striking evolutionary dysregulation of these mitochondrial proteins is linked to a conservation for this rare modiﬁcation, it is perhaps not range of human metabolic disorders. Perhaps most striking is surprising that these lipoylated enzymes are critically that lipoylation itself, the proteins that add or remove the linked to maintenance of health and development of modiﬁcation, as well as the proteins it decorates are all disease. PDH dysregulation is known to contribute to evolutionarily conserved from bacteria to humans, highlighting numerous human metabolic disorders, cancer, viral infec- the importance of this essential cofactor. Here, we discuss the tion, and Alzheimer’s disease [9,10
Current Opinion in Chemical Biology – Elsevier
Published: Feb 1, 2018
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