1.3.8.8: long-chain acyl-CoA dehydrogenase
This is an abbreviated version!
For detailed information about long-chain acyl-CoA dehydrogenase, go to the full flat file.
Word Map on EC 1.3.8.8
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1.3.8.8
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medium-chain
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beta-oxidation
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carnitine
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acylcarnitine
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cardiomyopathy
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cardiac
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peroxisome
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triglyceride
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rhabdomyolysis
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hypoglycemia
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acadvl
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palmitoyltransferase
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proliferator-activated
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inborn
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trifunctional
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nbs
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3-hydroxyacyl-coa
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acidurias
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myopathic
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hypoketotic
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glutaric
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myoglobinuria
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dehydrogenase-deficient
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isovaleryl-coa
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bezafibrate
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lchad
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faods
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medicine
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mcadd
- 1.3.8.8
-
medium-chain
-
beta-oxidation
- carnitine
- acylcarnitine
- cardiomyopathy
- cardiac
- peroxisome
- triglyceride
- rhabdomyolysis
- hypoglycemia
- acadvl
- palmitoyltransferase
-
proliferator-activated
-
inborn
-
trifunctional
- nbs
- 3-hydroxyacyl-coa
- acidurias
-
myopathic
-
hypoketotic
-
glutaric
- myoglobinuria
-
dehydrogenase-deficient
- isovaleryl-coa
- bezafibrate
- lchad
-
faods
- medicine
-
mcadd
Reaction
Synonyms
ACAD 9, AcdB, acyl-CoA dehydrogenase 9, BACH, CTE-II, EC 1.3.99.13, EC 1.3.99.3, LCAD, long chain acyl coenzyme A dehydrogenase, long chain acyl-CoA dehydrogenase, long-chain acyl-CoA dehydrogenase, long-chain acyl-CoA hydrolase, long-chain acyl-coenzyme A dehydrogenase, MCAD, medium long-chain acyl-CoA dehydrogenase, More, MTE-II, palmitoyl-CoA dehydrogenase, palmitoyl-coenzyme A dehydrogenase, PtmO4, type-II acyl-CoA thioesterase, very long chain acyl-CoA dehydrogenase, very long-chain acyl-CoA dehydrogenase, very-long-chain acyl-CoA dehydrogenase, very-long-chain acyl-coenzyme A dehydrogenase, VLCAD, VLMCAD
ECTree
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Systematic Name
Systematic Name on EC 1.3.8.8 - long-chain acyl-CoA dehydrogenase
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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 from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms. The highest activity was found with C12, and the rates with C8 and C16 were 80 and 70%, respectively [2]. The enzyme from rat can accept substrates with C8-C22. It is most active with C14 and C16, and has no activity with C4, C6 or C24 [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.