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Literature summary for 1.3.8.9 extracted from

  • 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 (2019), J. Biol. Chem., 294, 12380-12391 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.3.8.9

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-
mitochondrion
-
 Mus musculus 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P49748
-
-
Mus musculus P50544
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Mus musculus
-
Hep-G2 cell
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
very-long-chain acyl-CoA dehydrogenase
-
 Homo sapiens
very-long-chain acyl-CoA dehydrogenase
-
 Mus musculus
VLCAD
-
 Homo sapiens
VLCAD
-
 Mus musculus

General Information

General Information Comment Organism
malfunction electron transfer chain supercomplexes SC1-3 are disrupted in mitochondria from VLCAD-deficient mice Mus musculus
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 Homo sapiens
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 Mus musculus