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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.

Wordmap for 1.3.8.9

Word Map on EC 1.3.8.9 Wordmap for 1.3.8.9

Reaction

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a very-long-chain acyl-CoA
+
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electron-transfer flavoprotein
=
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a very-long-chain trans-2,3-dehydroacyl-CoA
+
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reduced electron-transfer flavoprotein

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

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.8 With a flavin as acceptor
                EC 1.3.8.91.3.8.9 very-long-chain acyl-CoA dehydrogenase

Reference

Reference on EC 1.3.8.9 - very-long-chain acyl-CoA dehydrogenase

for references in articles please use BRENDA:EC1.3.8.9

Please use the Reference Search for a specific query.

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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
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
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
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)
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
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
Manually annotated by BRENDA team