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Information on EC 1.3.8.7 - medium-chain acyl-CoA dehydrogenase
for references in articles please use BRENDA:EC1.3.8.7
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EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.8 With a flavin as acceptor
1.3.8.7 medium-chain acyl-CoA dehydrogenase
IUBMB Comments
Contains a tightly-bound FAD cofactor. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C8 to C12 compounds . The enzyme from rat does not accept C16 at all and is most active with C6-C8 compounds . cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.
The enzyme appears in viruses and cellular organisms
- 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 Schemes
showSynonyms
medium-chain acyl-coa dehydrogenase, acadm, medium chain acyl-coa dehydrogenase, acyl coa dehydrogenase, medium-chain acyl-coenzyme a dehydrogenase, acyl coenzyme a dehydrogenase, mcadh, medium-chain acyl coa dehydrogenase, acyl dehydrogenase, pmcad, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACADM
acyl CoA dehydrogenase
acyl coenzyme A dehydrogenase
-
-
-
-
acyl dehydrogenase
-
-
-
-
acyl-CoA dehydrogenase
dehydrogenase, acyl coenzyme A
-
-
-
-
EC 1.3.2.2
-
-
formerly
-
EC 1.3.99.3
-
-
formerly
-
FadE
fatty acyl coenzyme A dehydrogenase
-
-
-
-
fatty-acyl-CoA dehydrogenase
-
-
-
-
general ACAD
general acyl CoA dehydrogenase
-
-
-
-
MCAD
medium chain acyl-CoA dehydrogenase
medium-chain acyl-CoA dehydrogenase
medium-chain acyl-coenzyme A dehydrogenase
PP_1893
PP_2039
PP_2048
PP_2437
acyl CoA dehydrogenase
-
-
-
-
MCAD
-
-
-
-
MCAD
-
-
medium-chain acyl-CoA dehydrogenase
-
-
-
-
medium-chain acyl-coenzyme A dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
mechanism, proton abstraction from C-2 of the substrate and hydride transfer from C-3 to the N-5 position of the flavin
-
a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
mechanism, proton abstraction from C-2 of the substrate and hydride transfer from C-3 to the N-5 position of the flavin
-
a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
mechanism, proton abstraction from C-2 of the substrate and hydride transfer from C-3 to the N-5 position of the flavin
-
a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
the catalytic base responsible for the alpha-proton abstraction is E376 in medium-chain acyl-CoA dehydrogenase, while that in long-chain acyl-CoA dehydrogenase is E255
-
a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
charge transfer complex between reduced flavin as the donor and trans-2-octenoyl-CoA as the acceptor
-
a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dehydrogenation
-
-
-
-
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
oxidation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
2-methyl-branched fatty acid beta-oxidation, adipate degradation, fatty acid salvage, oleate beta-oxidation
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SYSTEMATIC NAME
IUBMB Comments
medium-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase
Contains a tightly-bound FAD cofactor. 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 4 to 16 carbon atoms, but is most active with C8 to C12 compounds [2]. The enzyme from rat does not accept C16 at all and is most active with C6-C8 compounds [4]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.
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CAS REGISTRY NUMBER
COMMENTARY
9027-65-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(4Z,7Z,10Z,13Z,16Z,19Z)-4,7,10,13,16,19-docosahexaenoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
(5Z,8Z,11Z,14Z,17Z) -5,8,11,14,17-icosapentaenoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
2,6-dimethylheptanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
4,8,12-trimethyltridecanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
4-cis,7-cis-decadienoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans,4-cis,7cis-decatrienoyl-CoA + reduced acceptor
-
Substrates: cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
Products: -
Products: -
?
4-cis-decenoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans,4-cis-decadienoyl-CoA + reduced acceptor
-
Substrates: cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
Products: -
Products: -
?
4-decynoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
trans-2-ene-4-decynoyl-CoA + reduced acceptor
-
Substrates: cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
Products: -
Products: -
?
4-oxaoctanoyl-CoA + phenazine methosulfate + 2,6-dichlorophenolindophenol
4-thia-trans-2-octenoyl-CoA + reduced 2,6-dichlorophenolindophenol
-
Substrates: poor substrate, oxidized at about 10% of the rate of octanoyl-CoA
Products: -
Products: -
?
4-thiaoctanoyl-CoA + phenazine methosulfate + 2,6-dichlorophenolindophenol
4-thia-trans-2-octenoyl-CoA + reduced 2,6-dichlorophenolindophenol
-
Substrates: oxidized 1.5fold faster than octanoyl-CoA
Products: -
Products: -
?
5-cis-decenoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans,5-cis-decadienoyl-CoA + reduced acceptor
-
Substrates: cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
Products: -
Products: -
?
6-cis-decenoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans,6-cis-decadienoyl-CoA + reduced acceptor
-
Substrates: cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
Products: -
Products: -
?
acyl-CoA + electron transfer flavoprotein
2,3-dehydroacyl-CoA + reduced electron transfer flavoprotein
all-cis-4,7,10,13-hexadecatetraenoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans-all-cis-4,7,10,13-hexadecapentaenoyl-CoA + reduced acceptor
-
Substrates: cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
Products: -
Products: -
?
arachidonoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
arachidoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
beta-(2-furyl)propionyl-CoA + electron transfer flavoprotein + 2,6-dichloroindophenol
trans-beta-(2-furyl)acryloyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
beta-(2-furyl)propionyl-CoA + O2
trans-beta-(2-furyl)acryloyl-CoA + H2O2
-
Substrates: slow oxidase activity
Products: -
Products: -
?
beta-(2-furyl)propionyl-CoA + pyocyanine
trans-beta-(2-furyl)acryloyl-CoA + reduced pyocanine
-
Substrates: -
Products: -
Products: -
?
butanoyl-CoA + electron-transfer flavoprotein
crotonoyl-CoA + reduced electron-transfer flavoprotein
-
Substrates: -
Products: -
Products: -
r
crotonyl-CoA + H2O
L-3-hydroxy-butyryl-CoA
-
Substrates: enoyl-CoA hydratase activity
Products: -
Products: -
?
decanoyl-CoA + 2,6-dichlorophenolindophenol
2-decenoyl-CoA + reduced 2,6-dichorophenolindophenol
-
Substrates: -
Products: -
Products: -
r
decanoyl-CoA + electron transfer flavoprotein
(2E)-2-decenoyl-CoA + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
decanoyl-CoA + electron transfer flavoprotein
decenoyl-CoA + reduced electron transfer flavoprotein
decanoyl-CoA + ferricenium hexafluorophosphate
2-decenoyl-CoA + ferrocenium hexafluorophosphate
-
Substrates: -
Products: -
Products: -
r
decanoyl-CoA + ferrocenium hexafluorophosphate
trans-dec-2-enoyl-CoA + reduced ferrocenium hexafluorophosphate
-
Substrates: -
Products: -
Products: -
r
decanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-trans-decenoyl-CoA + reduced acceptor
docosanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
dodecanoyl-CoA + electron transfer flavoprotein
dodecenoyl-CoA + reduced electron transfer flavoprotein
dodecanoyl-CoA + electron-transfer flavoprotein
+ trans-dodec-2-enoyl-CoA reduced electron-transfer flavoprotein
-
Substrates: -
Products: -
Products: -
r
dodecanoyl-CoA + tetrazolium salt
trans-dodec-2-enoyl-CoA + reduced tetrazolium salt
-
Substrates: -
Products: -
Products: -
r
elaidoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
furylpropionyl-CoA + ferricenium hexafluorophosphate
furylacryloyl-CoA + ferrocenium hexafluorophosphate
heptadecanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
hexadecanoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans-hexadecenoyl-CoA + reduced acceptor
hexanoyl-CoA + 2,6-dichloroindophenol
2-hexenoyl-CoA + reduced 2,6-dichloroindophenol
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + 2,6-dichlorophenolindophenol
trans-hex-2-enoyl-CoA + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
r
hexanoyl-CoA + electron transfer flavoprotein
(2E)-2-hexenoyl-CoA + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + ferricenium
trans-hex-2-enoyl-CoA + ferrocenium
-
Substrates: -
Products: -
Products: -
r
hexanoyl-CoA + ferricenium hexafluorophosphate
trans-hex-2-enoyl-CoA + ferrocenium hexafluorophosphate
-
Substrates: -
Products: -
Products: -
r
hexanoyl-CoA + ferrocenium hexafluorophosphate
trans-hex-2-enoyl-CoA + reduced ferrocenium hexafluorophosphate
-
Substrates: -
Products: -
Products: -
r
hexanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-trans-hexenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + tetrazolium salt
trans-hex-2-enoyl-CoA + reduced tetrazolium salt
-
Substrates: -
Products: -
Products: -
r
indolepropionyl-CoA + ferricenium hexafluorophosphate
indoleacryloyl-CoA + ferrocenium hexafluorophosphate
lauroyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
lauroyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-trans-dodecenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
linoleoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
myristoleoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
myristoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
n-octanoyl-CoA + acceptor
2-octenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
n-tetradecanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-tetradecenoyl-CoA + reduced acceptor
-
Substrates: best substrate for long-chain acyl-CoA dehydrogenase
Products: -
Products: -
?
nonanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
octanoyl 3'-dephospho-CoA + 2,6-dichloroindophenol
?
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced 2,6-dichloroindophenol
-
Substrates: optimal substrate for wild type enzyme
Products: -
Products: -
?
octanoyl-CoA + electron transferring flavoprotein
2-octenoyl-CoA + reduced electron transferring flavoprotein
octanoyl-CoA + ferricenium hexafluorophosphate
2-octenoyl-CoA + ferrocenium hexafluorophosphate
-
Substrates: medium chain acyl-CoA dehydrogenase from kidney
Products: -
Products: -
?
octanoyl-CoA + ferriocenium hexfluorophosphate
2-octenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + meldola's blue
trans-oct-2-enoyl-CoA + reduced meldola's blue
-
Substrates: -
Products: -
Products: -
r
octanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + phenazine ethosulfate
trans-oct-2-enoyl-CoA + reduced phenazine ethosulfate
-
Substrates: -
Products: -
Products: -
r
octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + recombinant beta-Y16L electron transferring flavoprotein
trans-oct-2-enoyl-CoA + reduced recombinant beta-Y16L electron transferring flavoprotein
-
Substrates: -
Products: -
Products: -
r
octanoyl-CoA + recombinant electron transferring flavoprotein
trans-oct-2-enoyl-CoA + reduced recombinant electron transferring flavoprotein
-
Substrates: -
Products: -
Products: -
r
oleoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
palmitoleoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
palmitoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
pentadecanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
phenylpropionyl-CoA + ferricenium hexafluorophosphate
? + reduced ferricenium hexafluorophosphate
-
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
tetradecanoyl-CoA + electron transfer flavoprotein
tetradecenoyl-CoA + reduced electron transfer flavoprotein
tetradecanoyl-CoA + tetrazolium salt
tetradecenoyl-CoA + reduced tetrazolium salt
-
Substrates: -
Products: -
Products: -
r
tetradecenoyl-CoA + reduced electron transfer flavoprotein
tetradecanoyl-CoA + electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
r
undecanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
-
Substrates: -
Products: -
Products: -
?
[4-(dimethylamino)phenyl]propionyl-CoA + ferricenium hexafluorophosphate
4-(dimethylamino)cinnamoyl-CoA + ferrocenium hexafluorophosphate
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: 2-p-iodophenyl-3-p-nitrophenyl-5-phenyl-2H-tetrazolium chloride as final electron acceptor
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: electron acceptor: phenazine methosulfate
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: chain-length specificity depending on electron acceptor: with phenazine methosulfate hexanoyl-CoA, with electron transfer flavoprotein, octanoyl-CoA
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: intermediary electron acceptor: 2,6-dichloroindophenol
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: final electron acceptor: 8-dimethylamino-2,3-benzophenoxazinium chloride, trivial name meldola's blue
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: specific for chain lengths C6-C8
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: electron acceptor: phenazine methosulfate
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: specific for chain lengths C4-C13
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: specific for chain lengths C6-C12
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: enzyme-substrate interactions
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: intermediary electron acceptor: 2,6-dichloroindophenol
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: electron acceptor: phenazine methosulfate or electron transfer flavoprotein
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: final electron acceptor: 8-dimethylamino-2,3-benzophenoxazinium chloride, trivial name meldola's blue
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: electron acceptor: phenazine methosulfate
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: enzyme-substrate interactions
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: intermediary electron acceptor: 2,6-dichloroindophenol
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: electron acceptor: phenazine methosulfate or electron transfer flavoprotein
Products: -
Products: -
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
-
Substrates: final electron acceptor: 8-dimethylamino-2,3-benzophenoxazinium chloride, trivial name meldola's blue
Products: -
Products: -
?
acyl-CoA + electron transfer flavoprotein
2,3-dehydroacyl-CoA + reduced electron transfer flavoprotein
-
Substrates: first step in beta-oxidation of fatty acids
Products: -
Products: -
?
acyl-CoA + electron transfer flavoprotein
2,3-dehydroacyl-CoA + reduced electron transfer flavoprotein
-
Substrates: first step in beta-oxidation of fatty acids
Products: -
Products: -
?
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
r
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
-
Substrates: reduction potential
Products: -
Products: -
?
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
-
Substrates: potentiometric measurements
Products: -
Products: -
?
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
decanoyl-CoA + acceptor
2-decenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
decanoyl-CoA + acceptor
2-decenoyl-CoA + reduced acceptor
-
Substrates: acceptors: phenazine methosulfate or electron transferring flavoprotein
Products: -
Products: -
?
decanoyl-CoA + acceptor
2-decenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
decanoyl-CoA + acceptor
2-decenoyl-CoA + reduced acceptor
-
Substrates: 72% of activity with hexanoyl-CoA
Products: -
Products: -
?
decanoyl-CoA + electron transfer flavoprotein
decenoyl-CoA + reduced electron transfer flavoprotein
Substrates: -
Products: -
Products: -
?
decanoyl-CoA + electron transfer flavoprotein
decenoyl-CoA + reduced electron transfer flavoprotein
Substrates: -
Products: -
Products: -
?
decanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-trans-decenoyl-CoA + reduced acceptor
-
Substrates: electron acceptor: Meldola's Blue and iodonitrotetrazoliumchloride, general and long-chain acyl-CoA dehydrogenase
Products: -
Products: -
?
decanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-trans-decenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
decanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-trans-decenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
dodecanoyl-CoA + acceptor
2-dodecenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
dodecanoyl-CoA + acceptor
2-dodecenoyl-CoA + reduced acceptor
-
Substrates: acceptors: phenazine methosulfate or electron transferring flavoprotein
Products: -
Products: -
?
dodecanoyl-CoA + acceptor
2-dodecenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
dodecanoyl-CoA + electron transfer flavoprotein
dodecenoyl-CoA + reduced electron transfer flavoprotein
Substrates: preferred substrate
Products: -
Products: -
?
dodecanoyl-CoA + electron transfer flavoprotein
dodecenoyl-CoA + reduced electron transfer flavoprotein
Substrates: preferred substrate
Products: -
Products: -
?
furylpropionyl-CoA + ferricenium hexafluorophosphate
furylacryloyl-CoA + ferrocenium hexafluorophosphate
-
Substrates: -
Products: -
Products: -
?
furylpropionyl-CoA + ferricenium hexafluorophosphate
furylacryloyl-CoA + ferrocenium hexafluorophosphate
-
Substrates: -
Products: -
Products: -
?
heptadecan-2-onyl-dethio-CoA + phenazine methosulfate + 2,6-dichloroindophenol
?
-
Substrates: -
Products: -
Products: -
?
heptadecan-2-onyl-dethio-CoA + phenazine methosulfate + 2,6-dichloroindophenol
?
-
Substrates: 58% of activity with hexadecanoyl-CoA
Products: -
Products: -
?
hexadecanoyl-CoA + acceptor
2-hexadecenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
hexadecanoyl-CoA + acceptor
2-hexadecenoyl-CoA + reduced acceptor
-
Substrates: acceptors: phenazine methosulfate or electron transferring flavoprotein, very low activity
Products: -
Products: -
?
hexadecanoyl-CoA + acceptor
2-hexadecenoyl-CoA + reduced acceptor
-
Substrates: 55% of activity with hexanoyl-CoA
Products: -
Products: -
?
hexadecanoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans-hexadecenoyl-CoA + reduced acceptor
-
Substrates: cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
Products: -
Products: -
?
hexadecanoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans-hexadecenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
-
Substrates: acceptors: phenazine methosulfate or electron transferring flavoprotein, best substrate with phenazine methosulfate
Products: -
Products: -
?
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
-
Substrates: 100% activity
Products: -
Products: -
?
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
-
Substrates: best substrate
Products: -
Products: -
?
indolepropionyl-CoA + ferricenium hexafluorophosphate
indoleacryloyl-CoA + ferrocenium hexafluorophosphate
-
Substrates: -
Products: -
Products: -
?
indolepropionyl-CoA + ferricenium hexafluorophosphate
indoleacryloyl-CoA + ferrocenium hexafluorophosphate
-
Substrates: -
Products: -
Products: -
?
indolepropionyl-CoA + ferricenium hexafluorophosphate
indoleacryloyl-CoA + ferrocenium hexafluorophosphate
-
Substrates: chromogenic substrate showing a strong absorption band in the near visible region
Products: -
Products: -
?
indolepropionyl-CoA + O2
indoleacryloyl-CoA + H2O2
-
Substrates: very low activity
Products: -
Products: -
?
indolepropionyl-CoA + O2
indoleacryloyl-CoA + H2O2
-
Substrates: very low activity
Products: -
Products: -
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
-
Substrates: best substrate with electron transferring flavoprotein
Products: -
Products: -
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
-
Substrates: fibroblast medium-chain acyl-CoA dehydrogenase is specific towards C6-C8 acyl-CoA esters
Products: -
Products: -
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
-
Substrates: best substrate for medium-chain acyl-CoA dehydrogenase
Products: -
Products: -
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
-
Substrates: no activity with tetradecanoyl-CoA and hexadecanoyl-CoA
Products: -
Products: -
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
-
Substrates: 82% of activity with hexanoyl-CoA
Products: -
Products: -
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
-
Substrates: no activity with tetradecanoyl-CoA and hexadecanoyl-CoA
Products: -
Products: -
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
-
Substrates: phenazine methosulfate substituted by electron transfer flavoprotein
Products: -
Products: -
?
octadecanoyl-CoA + acceptor
2-octadecenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
octadecanoyl-CoA + acceptor
2-octadecenoyl-CoA + reduced acceptor
-
Substrates: acceptors: phenazine methosulfate or electron transferring flavoprotein, extremely low activity
Products: -
Products: -
?
octanoyl-CoA + acceptor
2-octenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + acceptor
2-octenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + acceptor
2-octenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + electron transferring flavoprotein
2-octenoyl-CoA + reduced electron transferring flavoprotein
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + electron transferring flavoprotein
2-octenoyl-CoA + reduced electron transferring flavoprotein
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + electron transferring flavoprotein
2-octenoyl-CoA + reduced electron transferring flavoprotein
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + ferricenium
2-octenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
octanoyl-CoA + ferricenium
2-octenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
pentanoyl-CoA + acceptor
2-pentenoyl-CoA + reduced acceptor
-
Substrates: acceptors: phenazine methosulfate or electron transferring flavoprotein
Products: -
Products: -
?
pentanoyl-CoA + acceptor
2-pentenoyl-CoA + reduced acceptor
-
Substrates: 68% of activity with hexanoyl-CoA
Products: -
Products: -
?
pentanoyl-CoA + acceptor
2-pentenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
phenylpropionyl-CoA + acceptor
? + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
phenylpropionyl-CoA + acceptor
? + reduced acceptor
-
Substrates: 110% activity
Products: -
Products: -
?
tetradecanoyl-CoA + acceptor
2-tetradecenoyl-CoA + reduced acceptor
-
Substrates: -
Products: -
Products: -
?
tetradecanoyl-CoA + acceptor
2-tetradecenoyl-CoA + reduced acceptor
-
Substrates: acceptors: phenazine methosulfate or electron transferring flavoprotein, low activity
Products: -
Products: -
?
tetradecanoyl-CoA + electron transfer flavoprotein
tetradecenoyl-CoA + reduced electron transfer flavoprotein
Substrates: -
Products: -
Products: -
?
tetradecanoyl-CoA + electron transfer flavoprotein
tetradecenoyl-CoA + reduced electron transfer flavoprotein
Substrates: -
Products: -
Products: -
?
[4-(dimethylamino)phenyl]propionyl-CoA + ferricenium hexafluorophosphate
4-(dimethylamino)cinnamoyl-CoA + ferrocenium hexafluorophosphate
-
Substrates: -
Products: -
Products: -
?
[4-(dimethylamino)phenyl]propionyl-CoA + ferricenium hexafluorophosphate
4-(dimethylamino)cinnamoyl-CoA + ferrocenium hexafluorophosphate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: involved in the formation of unsaturated fatty acid
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows a preference towards esters of even chain length and very low activity with C3C9 acyl-CoA esters as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows a preference towards esters of even chain length and very low activity with C3C9 acyl-CoA esters as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows a preference towards esters of even chain length and very low activity with C3C9 acyl-CoA esters as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows a preference towards esters of even chain length and very low activity with C3C9 acyl-CoA esters as substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme shows a preference towards esters of even chain length and very low activity with C3C9 acyl-CoA esters as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows a preference towards esters of even chain length and very low activity with C3C9 acyl-CoA esters as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows a preference towards esters of even chain length and very low activity with C3C9 acyl-CoA esters as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows a preference towards esters of even chain length and very low activity with C3C9 acyl-CoA esters as substrates
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme shows a preference towards esters of even chain length and very low activity with C3C9 acyl-CoA esters as substrates
Products: -
Products: -
?
additional information
?
-
-
Substrates: a Y42H mutation is frequently found in babies identified by newborn screening with MS/MS. Y42H is a temperature sensitive mutation, which is mild at low temperatures, but may have deleterious effects at increased temperatures
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme for the beta-oxidation of fatty acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: acts on a wide range of chain lengths (C16-C4)
Products: -
Products: -
?
additional information
?
-
-
Substrates: beta-oxidation enzymes encoded by the pim gene cluster including acyl CoA dehydrogenase are active with medium-chain-length dicarboxylic acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate/product binding results in ligand polarization and positive flavin potential shifts, which activate the enzyme for electron transfer
Products: -
Products: -
?
additional information
?
-
-
Substrates: acts on a wide range of chain lengths (C16-C4)
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acyl-CoA + electron transfer flavoprotein
2,3-dehydroacyl-CoA + reduced electron transfer flavoprotein
octanoyl-CoA + electron transferring flavoprotein
2-octenoyl-CoA + reduced electron transferring flavoprotein
-
Substrates: -
Products: -
Products: -
?
acyl-CoA + electron transfer flavoprotein
2,3-dehydroacyl-CoA + reduced electron transfer flavoprotein
-
Substrates: first step in beta-oxidation of fatty acids
Products: -
Products: -
?
acyl-CoA + electron transfer flavoprotein
2,3-dehydroacyl-CoA + reduced electron transfer flavoprotein
-
Substrates: first step in beta-oxidation of fatty acids
Products: -
Products: -
?
additional information
?
-
-
Substrates: a Y42H mutation is frequently found in babies identified by newborn screening with MS/MS. Y42H is a temperature sensitive mutation, which is mild at low temperatures, but may have deleterious effects at increased temperatures
Products: -
Products: -
?
additional information
?
-
-
Substrates: key enzyme for the beta-oxidation of fatty acids
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7,8-dichloro-FAD
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
FAD can be removed by a treatment of the enzyme with a suspension of charcoal in an acid-ammonium sulfate/potassium bromide mixture
FAD
-
reconstitution of the apoenzyme with 8-chloro-FAD, 8-bromo-FAD or 2-thio-FAD yields an active holoenzyme
FAD
-
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-(+)-(Methylenecyclopropyl)acetyl-CoA
-
stereospecific inactivation, faster inhibition with (R)-isomer than with (S)-isomer
1-ethyl-3(3-dimethylaminopropyl)-carbodiimide
-
90-96% inhibition of activity with electron transfer flavoprotein, not with phenazine methosulfate
3-butynoyl-CoA
-
concentration-dependent, progressive total inactivation, active site inhibitor
oct-4-en-2-ynoyl-CoA
-
irreversible inhibitor, active-site directed, enzyme protected by 2-octenoyl-CoA
p-hydroxymercuribenzoate
-
0.1 mM, almost complete inhibition of the apo-enzyme
(methylenecyclopropyl)acetyl-CoA
-
biphasic inhibition of medium-chain acyl-CoA dehydrogenase, rapid initial inactivation for 2 min, half-life: 1.3 min, followed by a slower decline, 95% activity lost after 30 min, no inhibition of long-chain acyl-CoA dehydrogenase
(R)-(-)-(methylenecyclopropyl)acetyl-CoA
-
0.0155 mM, almost complete inactivation after 5 min, stereospecific inactivation, faster inhibition with (R)-isomer than with (S)-isomer
(R)-(-)-(methylenecyclopropyl)acetyl-CoA
-
both (R)- and (S)-stereoisomers are potent inhibitors, inactivation is nonstereospecific
2-octynoyl-CoA
-
inactivation of the reduced dehydrogenase may involve a covalent adduct between dihydroflavin and 2-octynoyl-CoA
2-octynoyl-CoA
-
mechanism-based inhibitor, suicide-substrate that modifies Glu401
iodoacetic acid
-
S-carboxymethylated enzyme binds octanoyl-CoA but can no longer be reduced by it
iodoacetic acid
-
30 mM, half-live: 100 min, loss of 98% activity after 25 h, 0.12 mM octanoyl-CoA strongly protects, S-carboxmethylation of a single catalytically essential methionine inactivates the enzyme
Methylmercury iodide
-
0.1 mM, strong inhibition, half-time of inactivation: 2 min, octanoyl-CoA protects
N-ethylmaleimide
-
inhibitory to apo-enzyme, 2 mM, half-time of inactivation: 4 min, complete inactivation after 20 min
additional information
-
not inhibited by ATP, ADP, GTP, GDP, FAD, NAD+, NADP+, carnitine, acetyl-CoA, succinyl-CoA, citrate, isocitrate, succinate, alpha-ketoglutarate, malate, fumarate
-
additional information
-
not inhibited by saturated and 2,3-unsaturated branched chain acyl-CoA compounds
-
additional information
-
not inhibited by trans-2,trans-4-octadienoyl-CoA and oct-2-en-4-ynoyl-CoA
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
rosiglitazone
-
treatment with 10 mg per kg and day increases acyl-CoA dehydrogenase expression and activity in both epididymal and inguinal white adipose tissue but not in brown adipose tissue, liver or muscle. The effect is the same in wild-type and PPAR-alpha knock-out mice
additional information
-
administration of a high fat diet in heart failure rats increases MCAD activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00084
octanoyl-CoA
-
mutant enzyme Y375K, in 50 mM potassium phosphate buffer, pH 7.6
0.0022
octanoyl-CoA
-
25°C, with ferricenium as acceptor, pig enzyme reconstituted with 2'-deoxy-FAD
0.0023
octanoyl-CoA
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 7.6
0.00242
octanoyl-CoA
-
mutant enzyme Y375F, in 50 mM potassium phosphate buffer, pH 7.6
0.0025
octanoyl-CoA
-
25°C, with ferricenium as acceptor, recombinant wild-type enzyme
0.0026
octanoyl-CoA
-
25°C, with ferricenium as acceptor, pig enzyme reconstituted with commercial FAD
0.00684
octanoyl-CoA
-
mutant enzyme Y375A, in 50 mM potassium phosphate buffer, pH 7.6
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
12
electron-transfer flavoprotein
-
between pH 8.0 and pH 10.0 at a ionic strength between 11 mM and 50 mM, lower values at acidic pH and with higher ionic strength
18.3
ferricenium hexafluorophosphate
-
medium chain acyl-CoA dehydrogenase from kidney
0.1
meldola's blue
-
medium chain acyl-CoA dehydrogenase from kidney, terminal acceptor iodonitrotetrazolium
0.75
phenazine ethosulfate
-
medium chain acyl-CoA dehydrogenase from kidney, terminal acceptor 2,6-dichlorphenol-indophenol
3
phenazine methosulfate
-
medium chain acyl-CoA dehydrogenase from kidney, terminal acceptor 2,6-dichlorphenol-indophenol
2.33
electron transferring flavoprotein
-
medium chain acyl-CoA dehydrogenase from kidney, terminal acceptor 2,6-dichlorphenol-indophenol
0.038
octanoyl-CoA
-
mutant enzyme Y375K, in 50 mM potassium phosphate buffer, pH 7.6
0.047
octanoyl-CoA
-
25°C, with ferricenium as acceptor, pig enzyme reconstituted with 2'-deoxy-FAD
0.22
octanoyl-CoA
-
mutant enzyme Y375A, in 50 mM potassium phosphate buffer, pH 7.6
0.37
octanoyl-CoA
-
mutant enzyme Y375F, in 50 mM potassium phosphate buffer, pH 7.6
3.25
octanoyl-CoA
-
phenazine methosulfate and 2,6-dichlorophenolindophenol as electron acceptors
3.3
octanoyl-CoA
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 7.6
18.8
octanoyl-CoA
-
25°C, with ferricenium as acceptor, recombinant wild-type enzyme
20
octanoyl-CoA
-
25°C, with ferricenium as acceptor, pig enzyme reconstituted with commercial FAD
1.67
recombinant beta-Y16L electron transferring flavoprotein
-
T168A mutant enzyme
-
18.3
recombinant beta-Y16L electron transferring flavoprotein
-
wild-type enzyme
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.004
-
activity in extracts of strain CB13 grown on oleic acid as carbon source
0.043
0.08
-
activity in cells grown on triolein, barely detectable activity in glucose-grown cells
10.6
-
assessed by measuring the amount of product formed in the first 5 min by gas chromatographic analysis
4.46
-
substrate indolepropionyl-CoA, ferrocenium hexafluorophosphate as electron carrier
0.043
-
activity in extracts of strain CB15 grown on oleic acid as carbon source
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
-
T168A mutant enzyme, approx. 20% of maximum activity at pH 6.0, sigmoidal increase between pH 5.5 and pH 9.0, approx. 80% of maximal activity at pH 7.8
7 - 10
-
approx. 20% of maximum activity at pH 7.5, sigmoidal increase between pH 7.0 and pH 10.0, approx. 80% of maximal activity at pH 9.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
391199, 391203, 391256, 391268, 391270, 391271, 391272, 391282, 391324, 655491, 657278, 671331, 672585, 685352, 685980, 697048, 700546
-
-
brenda
-
391201, 391328, 391367, 391368, 391369, 391371, 654644, 654890, 674476, 684292, 684294, 685133, 686130, 686147, 688185, 688197, 688742, 689342, 690129, 697388, 698117
-
-
brenda
Japanese patients with medium-chain acyl-CoA dehydrogenase deficiency
-
-
brenda
K304E point mutation leading to a higher susceptibility of the mutant enzyme for degradation is one of several mutations, which are responsible for medium chain acyl-CoA dehydrogenase deficiency
-
-
brenda
skin fibroblast cell lines from healthy subjects and from patients with medium-chain, long-chain and with multiple-chain acyl-CoA dehydrogenase deficiency
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brenda
T168A mutation found in patients with medium-chain acyl-CoA deficiency
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brenda
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391273, 391311, 391312, 391313, 391314, 391317, 391318, 391319, 391320, 391321, 391322, 391327, 391329, 391331, 391335, 391336, 391339, 391342, 391344, 391346, 391349, 391350, 391351, 391352, 391353, 391354, 391355, 391356, 391357, 391358, 391359, 391362, 391363, 391364, 391365, 391367, 391368, 391370, 391372, 654353, 654679, 655926, 671331, 698667
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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391273, 391311, 391312, 391313, 391317, 391319, 391320, 391321, 391322, 391327, 391329, 391336, 391339, 391344, 391351, 391352, 391353, 391359, 391363, 655926, 654353, 698667
brenda
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brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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localized on GLU4-containing vesicles via association with insulin-regulated aminopeptidase in a manner dependent on its dileucine motif and plays a role in retention of GLUT4-containing vesicles to an intracellular compartment
brenda
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brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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medium-chain acyl-CoA dehydrogenase deficiency (OMIM 201450) is the most common inherited disorder of fatty acid metabolism presenting with hypoglycaemia, hepatopathy and Reye-like symptoms during catabolism, genotyping and phenotypes, overview. Functional effects of different medium-chain acyl-CoA dehydrogenase genotypes and identification of asymptomatic variants
metabolism
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acyl-CoA dehydrogenase catalyzes the first reaction step in mitochondrial fatty-acid beta-oxidation
physiological function
physiological function
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involved in fatty acid oxidation, essential energy generation
physiological function
genome sequence reveals 21 putative acyl-CoA dehydrogenases. A mutant with insertionally inactivated isoform PP_1893 grows and accumulates medium chain length polyhydroxyalkanoate on a range of fatty acids as the sole source of carbon and energy
physiological function
genome sequence reveals 21 putative acyl-CoA dehydrogenases. A mutant with insertionally inactivated isoform PP_2039 grows and accumulates medium chain length polyhydroxyalkanoate on a range of fatty acids as the sole source of carbon and energy
physiological function
genome sequence reveals 21 putative acyl-CoA dehydrogenases. A mutant with insertionally inactivated isoform PP_2048 grows and accumulates medium chain length polyhydroxyalkanoate on a range of fatty acids as the sole source of carbon and energy
physiological function
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genome sequence reveals 21 putative acyl-CoA dehydrogenases. A mutant with insertionally inactivated isoform PP_1893 grows and accumulates medium chain length polyhydroxyalkanoate on a range of fatty acids as the sole source of carbon and energy
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physiological function
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genome sequence reveals 21 putative acyl-CoA dehydrogenases. A mutant with insertionally inactivated isoform PP_2039 grows and accumulates medium chain length polyhydroxyalkanoate on a range of fatty acids as the sole source of carbon and energy
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physiological function
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genome sequence reveals 21 putative acyl-CoA dehydrogenases. A mutant with insertionally inactivated isoform PP_2048 grows and accumulates medium chain length polyhydroxyalkanoate on a range of fatty acids as the sole source of carbon and energy
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Show AA Sequence and Transmembrane Helices (9522 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
155000
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enzyme from heart, SDS-PAGE after cross-linkage with dimethylsuberimidate
160000
178000
43000
43685
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4 * 43685, mature enzyme, calculation from nucleotide sequence
45000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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gel filtration, 64800, predicted by 37-amino acid leader peptide cleaved sequentially by two mitochondrial peptidases
tetramer
tetramer
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4 * 43685, mature enzyme, calculation from nucleotide sequence
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular dynamics simulation and comparison between the porcine MCAD and human MCAD structures. Both proteins are essentially similar
wild-type and E376G/T255E double mutant enzyme and enzyme substrate complexes, vapor diffusion method at 4°C using the sitting drop technique, 0.027 mg enzyme in 140 mM Tris-acetate, pH 7.0, 8% w/v polyethylene glycol 4000, the human enzyme structure is essentially the same as that of the pig enzyme
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5-10 mg/ml enzyme in 50 mM potassium phosphate, pH 7.5, 0.1 mM EDTA, 2% polyethylene glycol 6000, 4°C, after 7 days 5% polyethylene glycol, crystals emerge 2-3 days later
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FT-IR spectroscopic studies. The hydrogen-bond enthalpy change responsible for the polarization on the transfer of the substrate from aqueous solution to the active site of enzyme is estimated to be 15 kcal/mol. The 1626 per cm band is noticeably weakened in the case of acyl-CoA with acyl chains longer than C12 which are poor substrates, suggesting that C(1) =O is likely to exist in multiple orientations in the active-site cavity, whence the band becomes obscured. A band identical to that of bound C8-CoA is observed in the case of C4-CoA which is a poor substrate, indicating the strong hydrogen bond at C(1)-O
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molecular dynamics simulation and comparison between the porcine MCAD and human MCAD structures. Both proteins are essentially similar
sitting-drop method, native enzyme and enzyme-substrate complex, x-ray structure, 2.4 A resolution, monomer is folded into 3 domains of approx. equal size, the flavin ring is located in a crevice between the beta-domain and the C-terminal domain
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A1010C
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genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency
A151T
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
A31P
A52V
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
A533C
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genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency
A985G
D266G
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
D79X
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
E18K
E376G
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the rate of dehydrogenation is lowered by approximately 5 orders of magnitude
E376Q
G127A
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genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency, not clearly associated with a clinical phenotype
G170R
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
G285R
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
G799A
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genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency
K304E
K329E
L59F
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
L73DELTA
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
N169D
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
N396Y
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involved in MCAD deficiency with a MCAD activity of 11.2% compared to the wild type enzyme, in combination with the deletion mutation DELTA449-CTGA-452
P128X
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
Q20R
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
R123K
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
R206C
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
R256S
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
R334K
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
R413S
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
T1229G
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genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency
T168A
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thermostability is markedly decreased, 80% lowered activity in ferricinum assay
T199C
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genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency, not clearly associated with a clinical phenotype
T255E
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same activity with octanoyl-CoA as wild-type, activity/chain length profile is, however, narrower
T255E/E376G
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chimeric medium-long chain acyl-CoA dehydrogenase, has 20% of the activity of medium-chain acyl-CoA dehydrogenase and 25% that of long-chain acyl-CoA dehydrogenase activity with its best substrates octanoyl-CoA and dodecanoyl-CoA respectively, activity maximum is shifted to C12 and C14-CoA, enzyme shows an enhanced rate of reoxidation with oxygen
T255E/E376T
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shifts the chain length activity profile to higher values, drastic reduction of maximal velocity
T92T
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
T96I
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
V362V
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
Y158H
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
Y42H
Y67H
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
K304E
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maximal velocity of the mutant protein is only one third of the wild-type value. 16% higher activity with the natural electron acceptor, electron transferring flavoprotein, than the wild-type enzyme. Decreased stability at temperatures above 42°C compared to wild-type enzyme
R256K
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3.6fold increase in Km-value for octanoyl-CoA, 45fold decrease in turnovernumber with octanoyl-CoA compared to wild-type enzyme
Y375K
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very low acyl-CoA dehydrogenase activity, mutant exhibits acyl-CoA oxidase activity
Y42H
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mutant enzyme has approximately the same maximal velocity as the wild-type enzyme, the KM-value for octanoyl-CoA is 1.6fold higher than the wild-type value. 7% higher activity with the natural electron acceptor, electron transferring flavoprotein, than the wild-type enzyme. Decreased stability at temperatures above 42°C compared to wild-type enzyme
additional information
A31P
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
A985G
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in the Brazilian population, about 0.41% of individuals are heterozygous for the A985G mutation. The mutant homozygous genotype was not found
A985G
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genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency, phenotype, overview
E18K
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
E376Q
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mutation slows down the octanoyl-CoA-dependent reductive half-reaction of the enzyme by about 5 orders of magnitude due to impairment in the proton transfer step, also impairs the association and dissociation rates for the binding of the reaction product octenoyl-CoA. Km-value for octanoyl-CoA is 1.6fold reduced, turnover number for octenoyl-CoA is 7083fold reduced compared to wild-type enzyme
K304E
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
K329E
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reported to be responsible for medium-chain CoA dehydrogenase deficiency
K329E
mutation identified in a newborn. Mutatio lowers the temperature threshold at which loss-of-function occurs
Y42H
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the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
additional information
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lipB insertion mutant, zone of growth inhibition around mutant is only ca. 62% of the wild-type inhibition zone indicating a reduced friulimicin production or a modified, less biologically active friulimicin production
additional information
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AF-toxin I is 55.5% and 97.9% lower in mutant strains 24.1 and 24.1.8, respectively, than in the wild type, AF-toxin II production decreases to almost 70% in strain 24.1 and up to 90% in strain 24.1.8
additional information
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among 11 Japanese patients with medium-chain acyl-CoA dehydrogenase deficiency, mutation c.449-452delCTGA accounts for 45%. Seven of 10 independent patients carried at least one copy of the mutation. Phenotypes of homozygous patients with the c.449-452delCTGA mutation varied from asymtomatic to life-threatening metabolic decompensations
additional information
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mutant strain deleted in the pim gene cluster, grows at about half the rate of the wild-type parent when benzoate or pimelate is supplied as the sole carbon source, grows five times more slowly than the wild-type on the C14 dicarboxylic acid tetradecanedioate, but is unimpaired in growth on the C8-fatty acid caprylate
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 37
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biphasic inactivation, half-lives: 3 h, fast phase, and more than 700 h, slow phase, at 28°C and 2 h, fast phase, and approx. 230 h, slow phase, at 37°C for the wild-type enzyme, the corresponding values for the K304E mutant enzyme are 1.7 h, 100 h at 28°C and 1.25 h and 55 h at 37°C
41
42
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decreased stability of mutant enzymes Y42H and K304E above 42°C compared to wild-type enzyme
52
53.5
41
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wild-type enzyme: almost no loss of activity after 1 h at 41°C, T168A mutant enzyme: complete inactivation after 20 min at 41°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enoyl-CoA compounds and acyl-CoA compounds stabilize the semiquinone form of enzyme
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urea, 7.3 M, 25°C, half-life: 22 min, inactivation of the oxidized enzyme after 230 min, reduced enzyme remains active
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, concentrated form, more than 1 year, no loss of activity
-80°C, stable for at least 3 months, wild-type enzyme, mutant enzymes R256A, R256K, R256Q and R256E
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant liver enzyme, DEAE-Sephacel, hydroxyapatite, tandem column-chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned on plasmid pEHEX2 and heterologous expression in Streptomyces lividans T7
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expression in Escherichia coli
expression of recombinant wild-type and K304E mutant enzyme in Escherichia coli
heterologous expression of wild-type, K304E and R28C mutant enzymes from patients with medium chain acyl-CoA dehydrogenase deficiency, in Escherichia coli and COS-7 cells
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expression of recombinant wild-type and K304E mutant enzyme in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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application of single exon and multiplex PCR protocol for sequencing based mutation screening of medium-chain acyl-CoA dehydrogenase and ornithine transcarbamylase genes. Both protocols give comparable resultswithout any re-design of the PCR primers or other optimization steps
medicine
additional information
medicine
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inhibitor may become a lead for further development for treating non-insulin-dependent diabetes mellitus
medicine
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in medium-chain acyl-CoA dehydrogenase deficiency, the affected patients predominantly present high levels of octanoic and decanoic acids and their glycine and carnitine by-products in tissues and body fluids. Treatment of healthy brain mitochondrial preparations with octanoic and decanoic acid markedly increases state 4 respiration and diminishes state 3 respiration as well as the respiratory control ratio, the mitochondrial membrane potential and the matrix NAD(P)H levels. Decanoic acid-elicited increase in oxygen consumption in state 4 respiration is partially prevented by atractyloside. Octanoic and decanoic acid also reduce ADP/O ratio, CCCP-stimulated respiration and the activities of respiratory chain complexes.The major accumulating fatty acids in MCADD may act as uncouplers of oxidative phosphorylation and as metabolic inhibitors. Decanoic acid, but not octanoic acid, provokes a marked mitochondrial swelling and cytochrome c release from mitochondria, reflecting a permeabilization of the inner mitochondrial membrane
medicine
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in the Brazilian population, about 0.41% of individuals are heterozygous for the A985G mutation. The mutant homozygous genotype was not found
medicine
-
among 11 Japanese patients with medium-chain acyl-CoA dehydrogenase deficiency, mutation c.449-452delCTGA accounts for 45%. Seven of 10 independent patients carried at least one copy of the mutation. Phenotypes of homozygous patients with the c.449-452delCTGA mutation varied from asymtomatic to life-threatening metabolic decompensations
medicine
cloning and functional characterization of mutations with unknown clinical relevance identified in asymptomatic newborns. Eighteen of these mutations were separately cloned into the human ACADM and functionally characterized
medicine
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analysis of variant enzymes identified in newborns. Enzyme analyses with hexanoyl-CoA, hexanoyl-CoA + butanoyl-CoA, and phenylpropionyl-CoA show significantly higher residual medium-chain acyl-CoA dehydrogenase activities in subjects with variant ACADM genotypes when compared to patients with classical ACADM genotypes. After prolonged fasting no hypoglycaemia is observed. Increasing concentrations of free fatty acids indicate lipolysis, and ketone body concentrations are sufficient for blood glucose concentrations in 5 out of 6 subjects. Phenylpropionic acid loading demonstrates in vivo residual enzyme activity in all studied subjects
medicine
mutations in the ACADM gene identified in newborn lower the temperature threshold at which loss-of-function occurs. Increased temperature as it occurs during intercurrent infections, significantly increases the risk of further conformational derangement and loss of function of the enzyme, explaining the life-threatening clinical courses observed during fever episodes
additional information
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development of fluorogenic and fluoromorphic probes for the enzyme as indicators for selective and sensetive detection of MCAD activity in tissue homogenates
additional information
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development of fluorogenic and fluoromorphic probes for the enzyme as indicators for selective and sensetive detection of MCAD activity in tissue homogenates
additional information
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highly homologous to human very-long-chain acyl-CoA dehydrogenase
additional information
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acyl-CoA dehydrogenase LipB is involved in the introduction of the unusual Dcis3 double bond into the acyl residue of friulimicin
additional information
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AFT10-1, which encodes an acyl-CoA dehydrogenase, is involved in the formation of the 9,10-epoxy-8-hydroxy-9-methyl-decatrienoic acid moiety of the host-specific AF-toxin molecule
EXTERNAL LINKS (specific for EC-Number 1.3.8.7)
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