1.3.8.9: very-long-chain acyl-CoA dehydrogenase
This is an abbreviated version!
For detailed information about very-long-chain acyl-CoA dehydrogenase, go to the full flat file.
Word Map on EC 1.3.8.9
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1.3.8.9
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acylcarnitine
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medium-chain
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carnitine
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beta-oxidation
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rhabdomyolysis
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hypoglycemia
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nbs
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acyl-coenzyme
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vlcad-deficient
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hypoketotic
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trifunctional
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faods
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dehydrogenase-deficient
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tetradecenoylcarnitine
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hadha
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myoglobinuria
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lchad
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scadd
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diagnostics
- 1.3.8.9
- acylcarnitine
-
medium-chain
- carnitine
-
beta-oxidation
- rhabdomyolysis
- hypoglycemia
- nbs
-
acyl-coenzyme
-
vlcad-deficient
-
hypoketotic
-
trifunctional
-
faods
-
dehydrogenase-deficient
-
tetradecenoylcarnitine
- hadha
- myoglobinuria
- lchad
-
scadd
- diagnostics
Reaction
Synonyms
ACADVL, acyl-CoA:(acceptor) 2,3-oxidoreductase, EC 1.3.99.3, MCAD, very long chain acyl-CoA dehydrogenase, very long-chain acyl-CoA dehydrogenase, very-long-chain acyl-CoA dehydrogenase, VLCAD, VLCADD
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General Information
General Information on EC 1.3.8.9 - very-long-chain acyl-CoA dehydrogenase
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malfunction
physiological function
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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
malfunction
electron transfer chain supercomplexes SC1-3 are disrupted in mitochondria from VLCAD-deficient mice
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VLCAD is a rate-limiting enzyme in fatty acid beta-oxidation and is regulated by phosphorylation at Ser586
physiological function
the enzyme is a diet-sensitive source of mitochondrial reactive oxygen species
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
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