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	VLCAD is a rate-limiting enzyme in fatty acid beta-oxidation and is regulated by phosphorylation at Ser586	723908	
1.3.8.9	physiological function	the enzyme is a diet-sensitive source of mitochondrial reactive oxygen species	741280	
1.3.8.9	malfunction	electron transfer chain supercomplexes SC1-3 are disrupted in mitochondria from VLCAD-deficient mice	763263	
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