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Information on EC 1.3.8.9 - very-long-chain acyl-CoA dehydrogenase and Organism(s) Mus musculus and UniProt Accession P50544

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IUBMB Comments
Contains 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.
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Mus musculus
UNIPROT: P50544
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
vlcadd, acadvl, very-long-chain acyl-coa dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
very long chain acyl-CoA dehydrogenase
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very-long-chain acyl-CoA dehydrogenase
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ACADVL
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-
very long-chain acyl-CoA dehydrogenase
-
-
VLCAD
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-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
very-long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
Contains 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 [1]. 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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
palmitoyl-CoA + electron-transfer flavoprotein
(2E)-2-hexadecenoyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
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-
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
electron transfer chain supercomplexes SC1-3 are disrupted in mitochondria from VLCAD-deficient mice
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ACADV_MOUSE
656
0
70875
Swiss-Prot
Mitochondrion (Reliability: 1)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team