Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
IUBMB CommentsContains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids beta-oxidation. The enzyme is most active toward long-chain acyl-CoAs such as C14, C16 and C18, but is also active with very-long-chain acyl-CoAs up to 24 carbons. It shows no activity for substrates of less than 12 carbons. Its specific activity towards palmitoyl-CoA is more than 10-fold that of the long-chain acyl-CoA dehydrogenase . cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.8, long-chain acyl-CoA dehydrogenase.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
-
-
-
?
palmitoyl-CoA + electron-transfer flavoprotein
(2E)-2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
additional information
?
-
palmitoyl-CoA + electron-transfer flavoprotein
(2E)-2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
-
-
-
-
?
palmitoyl-CoA + electron-transfer flavoprotein
(2E)-2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
palmitoyl-CoA + electron-transfer flavoprotein
(2E)-2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
-
-
-
?
additional information
?
-
-
acyl-CoA dehydrogenases, ACADs, constitute a family of FAD-dependent flavoproteins that catalyze the alpha,beta-dehydrogenation of thioester substrates
-
-
?
additional information
?
-
the enzyme is a cardiolipin-binding protein
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
malfunction
electron transfer chain supercomplexes SC1-3 are disrupted in mitochondria from VLCAD-deficient mice
physiological function
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Primassin, S.; Ter Veld, F.; Mayatepek, E.; Spiekerkoetter, U.
Carnitine supplementation induces acylcarnitine production in tissues of very long-chain acyl-CoA dehydrogenase-deficient mice, without replenishing low free carnitine
Pediatr. Res.
63
632-637
2008
Mus musculus
brenda
Tajima, G.; Sakura, N.; Shirao, K.; Okada, S.; Tsumura, M.; Nishimura, Y.; Ono, H.; Hasegawa, Y.; Hata, I.; Naito, E.; Yamaguchi, S.; Shigematsu, Y.; Kobayashi, M.
Development of a new enzymatic diagnosis method for very-long-chain acyl-CoA dehydrogenase deficiency by detecting 2-hexadecenoyl-CoA production and its application in tandem mass spectrometry-based selective screening and newborn screening in Japan
Pediatr. Res.
64
667-672
2008
Homo sapiens
brenda
Li, Z.; Zhai, Y.; Fang, J.; Zhou, Q.; Geng, Y.; Sun, F.
Purification, crystallization and preliminary crystallographic analysis of very-long-chain acyl-CoA dehydrogenase from Caenorhabditis elegans
Acta Crystallogr. Sect. F
66
426-430
2010
Caenorhabditis elegans
brenda
Kabuyama, Y.; Suzuki, T.; Nakazawa, N.; Yamaki, J.; Homma, M.; Homma, Y.
Dysregulation of very long chain acyl-CoA dehydrogenase coupled with lipid peroxidation
Am. J. Physiol. Cell Physiol.
298
C107-C113
2010
Homo sapiens
brenda
Zhang, Y.; Bharathi, S.S.; Rardin, M.J.; Uppala, R.; Verdin, E.; Gibson, B.W.; Goetzman, E.S.
SIRT3 and SIRT5 regulate the enzyme activity and cardiolipin binding of very long-chain acyl-CoA dehydrogenase
PLoS ONE
10
e0122297
2015
Homo sapiens (P49748)
brenda
Isackson, P.; Sutton, K.; Hostetler, K.; Vladutiu, G.
Novel mutations in the gene encoding very long-chain acyl-CoA dehydrogenase identified in patients with partial carnitine palmitoyltransferase II deficiency
Muscle Nerve
47
224-229
2013
Homo sapiens (P49748)
brenda
Cardoso, A.; Kakimoto, P.; Kowaltowski, A.
Diet-sensitive sources of reactive oxygen species in liver mitochondria: role of very long chain acyl-CoA dehydrogenases
PLoS ONE
8
e77088
2013
Mus musculus (P50544)
brenda
Kakimoto, P.A.; Tamaki, F.K.; Cardoso, A.R.; Marana, S.R.; Kowaltowski, A.J.
H2O2 release from the very long chain acyl-CoA dehydrogenase
Redox Biol.
4
375-380
2015
Homo sapiens (P49748)
brenda
Wang, Y.; Palmfeldt, J.; Gregersen, N.; Makhov, A.M.; Conway, J.F.; Wang, M.; McCalley, S.P.; Basu, S.; Alharbi, H.; St Croix, C.; Calderon, M.J.; Watkins, S.; Vockley, J.
Mitochondrial fatty acid oxidation and the electron transport chain comprise a multifunctional mitochondrial protein complex
J. Biol. Chem.
294
12380-12391
2019
Homo sapiens (P49748), Mus musculus (P50544)
brenda
Hagemeijer, M.C.; Oussoren, E.; Ruijter, G.J.G.; Onkenhout, W.; Huidekoper, H.H.; Ebberink, M.S.; Waterham, H.R.; Ferdinandusse, S.; de Vries, M.C.; Huigen, M.C.D.G.; Kluijtmans, L.A.J.; Coene, K.L.M.; Blom, H.J.
Abnormal VLCADD newborn screening resembling MADD in four neonates with decreased riboflavin levels and VLCAD activity
JIMD Rep.
61
12-18
2021
Homo sapiens (P49748), Homo sapiens
brenda
1.3.8.9 very-long-chain acyl-CoA dehydrogenase
more
top
