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MetabolomicsABHD11/ROLIP maintains the TCA cycle by preserving functional lipoylation of the 2-oxoglutarate dehydrogenase complex
2-oxoglutarate (2-OG) relates mitochondrial metabolism to cell function: conversion of 2-OG to succinyl-CoA by the 2-OG dehydrogenase complex (OGDHc) is rate-limiting for the Tricarboxylic Acid (TCA) cycle, but 2-OG is also required for oxygen sensitive enzymes (2-OG dependent dioxygenases) that hav...
2020-08-10 | MTBLS1875 | MetaboLights
ProteomicsABHD11 maintains 2-oxoglutarate metabolism by preserving functional lipoylation of the 2-oxoglutarate dehydrogenase complex
2-oxoglutarate (2-OG or α-ketoglutarate) relates mitochondrial metabolism to cell function by modulating the activity of 2-OG dependent dioxygenases involved in the hypoxia response and DNA/histone modifications. However, metabolic pathways that regulate these oxygen and 2-OG sensitive enzymes remai...
ORGANISM(S): Homo sapiens (Human) 
2020-07-27 | PXD020128 | Pride
Α-ketoglutarate Lipid peroxidation 2-oxoglutarate dehydrogenase complex Lipoic acid Hypoxia inducible factor 2-oxoglutarate Abhd11 Lipoylation Α-ketoglutarate dehydrogenase complex 
ProteomicsQuantitative Site-specific Chemoproteomic Profiling of Protein Lipoylation
Protein lipoylation is an evolutionarily conserved post-translational modification (PTM) from prokaryotes and eukary-otes. Lipoylation is known to contribute to several human diseases including metabolic disorders, cancer and Alz-heimer’s disease. While individual lipoylated proteins have been bioch...
ORGANISM(S): Homo Sapiens Escherichia Coli 
2022-02-05 | PXD031466 |
ProteomicsChemical Tagging of Protein Lipoylation
Protein lipoylation is a post-translational modification of emerging importance in both prokaryotes and eukaryotes. However, effective methods for labeling and analyzing, particularly in large scale, protein lipoylation remain limited. Here, we report the development of iLCL (iodoacetamide-assisted ...
ORGANISM(S): Mus musculus (Mouse) Escherichia coli 
2020-11-16 | PXD021948 | Pride
Chemical proteomics Chemoselective ligation Lipoylation 
GenomicsATAD3A Limits Aortic Dissection via Mito-Lysosome Contacts and Lipoylation
ATAD3A Limits Aortic Dissection via Mito-Lysosome Contacts and Lipoylation
PRJNA1458662 | ENA
UnknownEngineered bacterial lipoate protein ligase A (lplA) restores lipoylation in cell models of lipoylation deficiency.
Not available
S-EPMC11665675 | biostudies-literature
TranscriptomicsATAD3A Limits Aortic Dissection via Mito-Lysosome Contacts and Lipoylation
Background: Aortic aneurysm and dissection (AAD) is a fatal vascular emergency with limited mechanism-based therapies. The mitochondrial AAA⁺ ATPase ATAD3A, enriched at organelle contact sites, has been implicated in mitochondrial signaling, but its role in AAD remains unclear. Methods: AAD was indu...
ORGANISM(S): Mus musculus 
2026-06-20 | GSE329337 | GEO
UnknownMitochondrial lipoylation integrates age-associated decline in brown fat thermogenesis.
Not available
S-EPMC7169975 | biostudies-literature
UnknownGenetic dissection of the mitochondrial lipoylation pathway in yeast.
Not available
S-EPMC7831266 | biostudies-literature
ProteomicsMitochondrial NADPH fuels mitochondrial fatty acid synthesis and lipoylation to power oxidative metabolism
1. Sample ID: 1005942, 1005943 - Description: The samples are HeLa cells transfected with pcDNA-FRT-T0 containing DLAT-HA. They were used to investigate whether NADK2 is required for DLAT lipoylation. 2. Sample ID: 1187969-1187973 - Description: The samples are HeLa cells transfected with pcDNA-FRT...
ORGANISM(S): Homo sapiens (Human) 
2025-03-03 | PXD060981 | Pride
Hadph Mitochondrial fatty acid synthesis Protein lipolyation 
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