1.3.8.7: medium-chain acyl-CoA dehydrogenase
This is an abbreviated version!
For detailed information about medium-chain acyl-CoA dehydrogenase, go to the full flat file.
Word Map on EC 1.3.8.7
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1.3.8.7
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carnitine
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beta-oxidation
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infant
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acylcarnitines
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children
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peroxisome
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urine
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mcadd
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inborn
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error
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proliferator-activated
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hypoglycemia
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acidurias
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triglyceride
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flavoproteins
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fad
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phenylketonuria
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octanoylcarnitine
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palmitoyltransferase
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acidemia
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glutaric
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octanoyl-coa
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octanoic
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hypoketotic
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nbs
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vlcad
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decompensation
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coma
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pparalpha
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methylmalonic
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isovaleric
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very-long-chain
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decanoic
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isovaleryl-coa
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syrup
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reye-like
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lethargy
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3-hydroxyacyl-coa
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maple
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homocystinuria
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guthrie
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biotinidase
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acadvl
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3-methylcrotonyl-coa
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phenylpropionic
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butyryl-coa
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alpha-proton
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medicine
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analysis
- 1.3.8.7
- carnitine
-
beta-oxidation
- infant
- acylcarnitines
- children
- peroxisome
- urine
-
mcadd
-
inborn
- error
-
proliferator-activated
- hypoglycemia
- acidurias
- triglyceride
- flavoproteins
- fad
- phenylketonuria
- octanoylcarnitine
- palmitoyltransferase
- acidemia
-
glutaric
- octanoyl-coa
-
octanoic
-
hypoketotic
- nbs
- vlcad
- decompensation
- coma
- pparalpha
-
methylmalonic
-
isovaleric
-
very-long-chain
-
decanoic
- isovaleryl-coa
- syrup
-
reye-like
- lethargy
- 3-hydroxyacyl-coa
-
maple
- homocystinuria
-
guthrie
- biotinidase
- acadvl
- 3-methylcrotonyl-coa
-
phenylpropionic
- butyryl-coa
-
alpha-proton
- medicine
- analysis
Reaction
Synonyms
ACAD-9, ACADM, ACD, acyl CoA dehydrogenase, acyl coenzyme A dehydrogenase, acyl dehydrogenase, acyl-CoA dehydrogenase, acyl-CoA dehydrogenase-9, dehydrogenase, acyl coenzyme A, EC 1.3.2.2, EC 1.3.99.3, FadE, fatty acyl coenzyme A dehydrogenase, fatty-acyl-CoA dehydrogenase, general ACAD, general acyl CoA dehydrogenase, LCAD, LipB, MCAD, MCADH, medium chain acyl-CoA dehydrogenase, medium chain-specific acyl-CoA oxidase, medium-chain acyl CoA dehydrogenase, medium-chain acyl-CoA dehydrogenase, medium-chain acyl-coenzyme A dehydrogenase, medium-chain coenzyme A dehydrogenase, pMCAD, PP_1893, PP_2039, PP_2048, PP_2437
ECTree
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Cofactor
Cofactor on EC 1.3.8.7 - medium-chain acyl-CoA dehydrogenase
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7,8-dichloro-FAD
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artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand
8-amino-FAD
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artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand
8-chloro-FAD
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artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand
8-cyano-FAD
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artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand
8-methoxy-FAD
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artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand
ribityl-2'-deoxy-8-chloro-FAD
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artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand
ribityl-2'-deoxy-8-cyano-FAD
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artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand
FAD
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FAD can be removed by a treatment of the enzyme with a suspension of charcoal in an acid-ammonium sulfate/potassium bromide mixture
FAD
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reconstitution of the apoenzyme with 8-chloro-FAD, 8-bromo-FAD or 2-thio-FAD yields an active holoenzyme
FAD
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investigation on the interaction of acyl-CoA with medium-chain acyl-CoA dehydrogenases reconstituted with artificial FADs such as 8-CN-, 7,8-Cl2-, 8-Cl-, 8-OCH3- and 8-NH2-FAD. 8-NH2-FAD-MCAD does not oxidize acyl-CoA, but the wavelength of the absorption maximum of the flavin is altered by acyl-CoAs binding
FAD
FAD has an important structural role on the tetramer stability and also in maintaining the volume of the enzyme catalytic pockets. The presence of substrate changes the dynamics of the catalytic pockets and increases FAD affinity
FAD
FAD has an important structural role on the tetramer stability and also in maintaining the volume of the enzyme catalytic pockets. The presence of substrate changes the dynamics of the catalytic pockets and increases FAD affinity