1.3.8.9	malfunction	electron transfer chain supercomplexes SC1-3 are disrupted in mitochondria from VLCAD-deficient mice	763263	
1.3.8.9	malfunction	phosphorylation of VLCAD at Ser586 is inhibited in myofibroblasts, resulting in a significant loss of enzyme activity coupled with lipid peroxidation.Thus Ser586 represents a critical site for VLCAD activity, whose dysregulation might contribute to the progression of idiopathic pulmonary fibrosis, IPF, a chronic interstitial lung disease, and other oxidative-stress mediated diseases	723908	
1.3.8.9	physiological function	the enzyme is a diet-sensitive source of mitochondrial reactive oxygen species	741280	
1.3.8.9	physiological function	the enzyme is involved in long-chain fatty acid beta-oxidation. It physically interacts with fatty acid beta-oxidation trifunctional protein (TFP), thereby creating a multifunctional energy protein complex. Reducing equivalents from the enzyme (VLCAD) in the form of FAD (FADH2) are transferred, through a series of redox reactions involving electron transfer flavoprotein (ETF) and electron flavoprotein dehydrogenase (ETFDH), to coenzymeQ (QH2) and then into electron transfer chain complex III	763263	
1.3.8.9	physiological function	VLCAD is a rate-limiting enzyme in fatty acid beta-oxidation and is regulated by phosphorylation at Ser586	723908