Information on EC 1.3.8.7 - medium-chain acyl-CoA dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.3.8.7
-
RECOMMENDED NAME
GeneOntology No.
medium-chain acyl-CoA dehydrogenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a medium-chain acyl-CoA + electron-transfer flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenation
-
-
-
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oxidation
redox reaction
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-
-
-
reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
beta-Alanine metabolism
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Biosynthesis of antibiotics
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Biosynthesis of secondary metabolites
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Fatty acid degradation
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fatty acid salvage
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lipid metabolism
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Metabolic pathways
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Propanoate metabolism
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Valine, leucine and isoleucine degradation
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SYSTEMATIC NAME
IUBMB Comments
medium-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 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.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-65-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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-
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Manually annotated by BRENDA team
wild-type strain CB13 and proline auxotrophic strain CB15
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Manually annotated by BRENDA team
algae
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Mougeotia sp.
algae
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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involved in fatty acid oxidation, essential energy generation
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
-
-
-
-
(5Z,8Z,11Z,14Z,17Z) -5,8,11,14,17-icosapentaenoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
2,6-dimethylheptanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
4,8,12-trimethyltridecanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
4-cis,7-cis-decadienoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans,4-cis,7cis-decatrienoyl-CoA + reduced acceptor
show the reaction diagram
-
cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
-
?
4-cis-decenoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans,4-cis-decadienoyl-CoA + reduced acceptor
show the reaction diagram
-
cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
-
?
4-decynoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
trans-2-ene-4-decynoyl-CoA + reduced acceptor
show the reaction diagram
-
cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
-
?
4-oxaoctanoyl-CoA + phenazine methosulfate + 2,6-dichlorophenolindophenol
4-thia-trans-2-octenoyl-CoA + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
poor substrate, oxidized at about 10% of the rate of octanoyl-CoA
-
?
4-thiaoctanoyl-CoA + phenazine methosulfate + 2,6-dichlorophenolindophenol
4-thia-trans-2-octenoyl-CoA + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
oxidized 1.5fold faster than octanoyl-CoA
-
?
5-cis-decenoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans,5-cis-decadienoyl-CoA + reduced acceptor
show the reaction diagram
-
cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
-
?
6-cis-decenoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans,6-cis-decadienoyl-CoA + reduced acceptor
show the reaction diagram
-
cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
acyl-CoA + electron transfer flavoprotein
2,3-dehydroacyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
all-cis-4,7,10,13-hexadecatetraenoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans-all-cis-4,7,10,13-hexadecapentaenoyl-CoA + reduced acceptor
show the reaction diagram
-
cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
-
?
arachidonoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
arachidoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
beta-(2-furyl)propionyl-CoA + electron transfer flavoprotein + 2,6-dichloroindophenol
trans-beta-(2-furyl)acryloyl-CoA + reduced acceptor
show the reaction diagram
beta-(2-furyl)propionyl-CoA + O2
trans-beta-(2-furyl)acryloyl-CoA + H2O2
show the reaction diagram
-
slow oxidase activity
-
?
beta-(2-furyl)propionyl-CoA + pyocyanine
trans-beta-(2-furyl)acryloyl-CoA + reduced pyocanine
show the reaction diagram
-
-
-
?
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
crotonyl-CoA + H2O
L-3-hydroxy-butyryl-CoA
show the reaction diagram
-
enoyl-CoA hydratase activity
-
?
decanoyl-CoA + acceptor
2-decenoyl-CoA + reduced acceptor
show the reaction diagram
decanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
decanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-trans-decenoyl-CoA + reduced acceptor
show the reaction diagram
docosanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
dodecanoyl-CoA + acceptor
2-dodecenoyl-CoA + reduced acceptor
show the reaction diagram
elaidoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
furylpropionyl-CoA + ferricenium hexafluorophosphate
furylacryloyl-CoA + ferrocenium hexafluorophosphate
show the reaction diagram
heptadecan-2-onyl-dethio-CoA + phenazine methosulfate + 2,6-dichloroindophenol
?
show the reaction diagram
heptadecanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
hexadecanoyl-CoA + acceptor
2-hexadecenoyl-CoA + reduced acceptor
show the reaction diagram
hexadecanoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans-hexadecenoyl-CoA + reduced acceptor
show the reaction diagram
hexanoyl-CoA + 2,6-dichloroindophenol
2-hexenoyl-CoA + reduced 2,6-dichloroindophenol
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
hexanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
hexanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-trans-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
indolepropionyl-CoA + ferricenium hexafluorophosphate
indoleacryloyl-CoA + ferrocenium hexafluorophosphate
show the reaction diagram
indolepropionyl-CoA + O2
indoleacryloyl-CoA + H2O2
show the reaction diagram
lauroyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
lauryl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-trans-dodecenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
linoleoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
myristoleoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
myristoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
n-octanoyl-CoA + acceptor
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
n-tetradecanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-tetradecenoyl-CoA + reduced acceptor
show the reaction diagram
nonanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
octadecanoyl-CoA + acceptor
2-octadecenoyl-CoA + reduced acceptor
show the reaction diagram
octanoyl 3'-dephospho-CoA + 2,6-dichloroindophenol
?
show the reaction diagram
-
-
-
-
?
octanoyl pantetheine + 2,6-dichloroindophenol
?
show the reaction diagram
-
-
-
-
?
octanoyl-1,N6-etheno-CoA + 2,6-dichloroindophenol
?
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced 2,6-dichloroindophenol
show the reaction diagram
-
optimal substrate for wild type enzyme
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-
?
octanoyl-CoA + acceptor
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
octanoyl-CoA + electron transferring flavoprotein
2-octenoyl-CoA + reduced electron transferring flavoprotein
show the reaction diagram
octanoyl-CoA + ferricenium
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
octanoyl-CoA + ferricenium hexafluorophosphate
2-octenoyl-CoA + ferrocenium hexafluorophosphate
show the reaction diagram
-
medium chain acyl-CoA dehydrogenase from kidney
-
?
octanoyl-CoA + ferriocenium hexfluorophosphate
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
oleoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
palmitoleoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
palmitoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
pentadecanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
pentanoyl-CoA + acceptor
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
phenylpropionyl-CoA + acceptor
? + reduced acceptor
show the reaction diagram
phenylpropionyl-CoA + ferricenium hexafluorophosphate
? + reduced ferricenium hexafluorophosphate
show the reaction diagram
-
-
-
-
?
stearoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
tetradecanoyl-CoA + acceptor
2-tetradecenoyl-CoA + reduced acceptor
show the reaction diagram
undecanoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
[4-(dimethylamino)phenyl]propionyl-CoA + ferricenium hexafluorophosphate
4-(dimethylamino)cinnamoyl-CoA + ferrocenium hexafluorophosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acyl-CoA + electron transfer flavoprotein
2,3-dehydroacyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
octanoyl-CoA + electron transferring flavoprotein
2-octenoyl-CoA + reduced electron transferring flavoprotein
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Methylenecyclopropyl)acetyl-CoA
(R)-(-)-(Methylenecyclopropyl)acetyl-CoA
(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
2,3-octadienoyl-CoA
-
-
2-decenoyl-CoA
-
medium- and long-chain acyl-CoA dehydrogenase
2-hexadecenoyl-CoA
-
competitive, long-chain acyl-CoA dehdrogenase
2-octenoyl-CoA
-
-
2-octynoyl-CoA
3,4-pentadienoyl-CoA
-
suicide substrate, 0.1 mM almost complete inhibition
3-butynoyl-CoA
-
concentration-dependent, progressive total inactivation, active site inhibitor
3-ketodecanoyl-CoA
-
medium- and long-chain acyl-CoA dehydrogenase
3-ketooctanoyl-CoA
-
76% inhibition
3-oxaoctanoyl-CoA
-
-
3-thiaoctanoyl-CoA
-
-
4-oxaoctanoyl-CoA
-
-
4-thiaoctanoyl-CoA
-
-
acetoacetyl-CoA
-
-
crotonyl-CoA
-
-
diethyldicarbonate
-
rapid inactivation
DL-3-hydroxydecenoyl-CoA
-
-
iodoacetamide
-
2 mM, 73% inhibition
iodoacetic acid
L-3-hydroxyoctanoyl-CoA
-
0.03 mM, 7% inhibition
Methylmercury chloride
-
0.1 mM, strong inhibition
Methylmercury iodide
N-ethylmaleimide
oct-2-yn-4-enoyl-CoA
-
pH-dependent inactivation
oct-4-en-2-ynoyl-CoA
-
irreversible inhibitor, active-site directed, enzyme protected by 2-octenoyl-CoA
Octanoyl-CoA
-
0.0045 mM, 98% inhibition of enoyl-CoA hydratase activity
octenoyl-CoA
-
competitive, medium-chain acyl-CoA dehydrogenase
Octyl-CoA
-
-
p-chloromercuribenzoate
p-hydroxymercuribenzoate
-
0.1 mM, almost complete inhibition of the apo-enzyme
S-Heptadecyl-CoA
-
competitive inhibition
semiquinone electron transfer flavoprotein
-
-
-
trans-2-octenoyl-CoA
-
0.03 mM, 62% inhibition
trans-3-octenoyl-CoA
-
0.03 mM, 67% inhibition
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
0.0023
4-cis,7-cis-decadienoyl-CoA
-
-
0.004
4-cis-Decenoyl-CoA
-
-
0.0029
4-decynoyl-CoA
-
-
0.003
5-cis-decenoyl-CoA
-
-
0.0021
6-cis-decenoyl-CoA
-
-
0.002
all-cis-4,7,10,13-hexadecatetraenoyl-CoA
-
-
0.001 - 0.007
beta(2-furyl)propionyl-CoA
0.0091
beta-(2-Furyl)propionyl-CoA
-
-
0.0084 - 0.45
Butanoyl-CoA
0.00714
Butyryl-CoA
-
-
0.016 - 0.038
crotonyl-CoA
-
hydratase reaction, value depending on pH
0.0007 - 0.05
decanoyl-CoA
0.0025 - 0.05
Dodecanoyl-CoA
0.0034 - 0.0045
electron transfer flavoprotein
0.0003 - 0.01
electron transferring flavoprotein
0.0024
FAD
-
-
0.055
ferricenium hexafluorophosphate
-
-
0.0099 - 0.069
ferrocenium hexafluorophosphate
0.014 - 0.0144
furylpropionyl-CoA
0.001 - 0.002
hexadecanoyl-CoA
0.0014 - 0.0216
Hexanoyl-CoA
0.00049 - 0.01
indolepropionyl-CoA
0.00021
linoleoyl-CoA
-
-
0.0011
Octanoyl 3'-dephospho-CoA
-
-
0.00928
Octanoyl-1,N6-etheno-CoA
-
-
0.00084 - 1.47
Octanoyl-CoA
0.107
octanoyl-pantetheine
-
-
0.00007
palmitoleoyl-CoA
-
-
0.0008 - 0.023
palmitoyl-CoA
0.0396
pentanoyl-CoA
-
-
1.67
phenazine methosulfate
-
-
0.0023 - 0.0057
tetradecanoyl-CoA
0.01
tetradecenoyl-CoA
-
-
-
0.0563
valeryl-CoA
-
-
0.0426 - 0.061
[4-(dimethylamino)phenyl]propionyl-CoA
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.2 - 11.5
Butanoyl-CoA
0.00233 - 0.00783
crotonyl-CoA
Sus scrofa
-
hydratase activity, value depending on pH
0.233 - 11.7
decanoyl-CoA
7
dodecadecanoyl-coA
Homo sapiens
-
-
3.33 - 9.5
Dodecanoyl-CoA
11.6
electron transfer flavoprotein
Sus scrofa
-
-
1.17 - 2.33
electron transferring flavoprotein
12
electron transferring protein
Sus scrofa
-
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
Sus scrofa
-
medium chain acyl-CoA dehydrogenase from kidney
13.2 - 13.6
furylpropionyl-CoA
0.617 - 2.92
hexadecanoyl-CoA
2.83 - 31.2
Hexanoyl-CoA
0.016 - 3.4
indolepropionyl-CoA
0.1
meldola's blue
Sus scrofa
-
medium chain acyl-CoA dehydrogenase from kidney, terminal acceptor iodonitrotetrazolium
0.667
Octadecanoyl-CoA
Homo sapiens
-
K304E mutant enzyme, ferricenium assay
0.0024 - 35.7
Octanoyl-CoA
0.235
octanoyl-pantetheine
Sus scrofa
-
general acyl-CoA dehydrogenase
0.75
phenazine ethosulfate
Sus scrofa
-
medium chain acyl-CoA dehydrogenase from kidney, terminal acceptor 2,6-dichlorphenol-indophenol
3
phenazine methosulfate
Sus scrofa
-
medium chain acyl-CoA dehydrogenase from kidney, terminal acceptor 2,6-dichlorphenol-indophenol
1.67 - 18.3
recombinant beta-Y16L electron transferring flavoprotein
1 - 14.7
recombinant electron transferring flavoprotein
2.67 - 8.33
tetradecanoyl-CoA
0.61 - 4.6
[4-(dimethylamino)phenyl]propionyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00073
2,3-octadienoyl-CoA
-
-
0.0034
2-octenoyl-CoA
-
-
0.00036 - 0.0065
2-octynoyl-CoA
0.0134
3-butynoyl-CoA
-
-
0.0007
3-oxodecanoyl-CoA
-
-
0.00567 - 0.0074
acetoacetyl-CoA
0.0144 - 0.0184
crotonyl-CoA
0.00028
electron transfer flavoprotein semiquinone
-
-
-
0.011
oct-4-en-2-ynoyl-CoA
-
-
0.00004
S-Heptadecyl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
-
activity in extracts of strain CB13 grown on oleic acid as carbon source
0.043
-
; activity in extracts of strain CB15 grown on oleic acid as carbon source
0.076
-
substrate butanoyl-CoA
0.08
-
activity in cells grown on triolein, barely detectable activity in glucose-grown cells
0.168
-
substrate hexadecanoyl-CoA
0.272
-
substrate octanoyl-CoA
1.96
-
long-chain acyl-CoA dehydrogenase
4.46
-
substrate indolepropionyl-CoA, ferrocenium hexafluorophosphate as electron carrier
6.75
-
-
10 - 10.2
-
-
10.6
-
assessed by measuring the amount of product formed in the first 5 min by gas chromatographic analysis
10.7
-
dye reduction assay with 2,6-dichlorophenolindophenol
11.9
-
medium-chain acyl-CoA dehydrogenase
17.5
-
recombinant K304E mutant enzyme, measured with ferricenium assay
24.9
-
recombinant wild-type enzyme, measured with ferricenium assay
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
-
9 - 10
-
T168A mutant
9
-
enoyl-CoA hydratase activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
6 - 9.5
-
-
6.5 - 8.5
-
increasing activity with increasing pH
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
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
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
SDS-PAGE
119000
-
gel filtration
155000
-
enzyme from heart, SDS-PAGE after cross-linkage with dimethylsuberimidate
160000
178000
180000
-
gel filtration
182000
-
gel filtration
183000
-
gel filtration
205000
-
native gel electrophoresis in polyacrylamide gradient
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 43000, SDS-PAGE
dimer
-
gel filtration, 64800, predicted by 37-amino acid leader peptide cleaved sequentially by two mitochondrial peptidases
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and E376G/T255E double mutant enzyme and enzyme substrate complexes, vapor diffusion method at 4C 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
-
5-10 mg/ml enzyme in 50 mM potassium phosphate, pH 7.5, 0.1 mM EDTA, 2% polyethylene glycol 6000, 4C, after 7 days 5% polyethylene glycol, crystals emerge 2-3 days later
-
dialysis against distilled water at 4C
-
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
-
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
-
x-ray structure, 3.0 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.7
-
-
391272
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 37
-
biphasic inactivation, half-lives: 3 h, fast phase, and more than 700 h, slow phase, at 28C and 2 h, fast phase, and approx. 230 h, slow phase, at 37C for the wild-type enzyme, the corresponding values for the K304E mutant enzyme are 1.7 h, 100 h at 28C and 1.25 h and 55 h at 37C
25
-
mutant enzyme E376Q is instable at 25C
41
-
wild-type enzyme: almost no loss of activity after 1 h at 41C, T168A mutant enzyme: complete inactivation after 20 min at 41C
42
-
decreased stability of mutant enzymes Y42H and K304E above 42C compared to wild-type enzyme
60
-
11 min, reduced enzyme stable, oxidized enzyme unstable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enoyl-CoA compounds and acyl-CoA compounds stabilize the semiquinone form of enzyme
-
no inactivation by freezing/thawing
-
urea, 7.3 M, 25C, half-life: 22 min, inactivation of the oxidized enzyme after 230 min, reduced enzyme remains active
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 100 mM phosphate buffer, pH 7.6
-
-20C, at least 1 month
-
-70C, concentrated form, more than 1 year, no loss of activity
-80C, 6 months, remains stable
-
-80C, stable for at least 3 months, wild-type enzyme, mutant enzymes R256A, R256K, R256Q and R256E
-
4C, 1 week without significant change of activity, His-tagged protein
-
4C, ammonium sulfate suspension
-
frozen, 50 mM phosphate buffer, pH 7.6
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity-purified, ca. 95% pure
-
apoprotein
-
HiTrap chelating nickel affinity chromatography
-
recombinant enzyme
-
recombinant liver enzyme, DEAE-Sephacel, hydroxyapatite, tandem column-chromatography
-
recombinant T168A mutant enzyme
-
recombinant wild-type and K304E mutant enzyme
-
recombinant wild-type, T255E, T255E/E367G and T255E/E367T mutant enzymes
-
wild-type and E376G/T255E double mutant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned on plasmid pEHEX2 and heterologous expression in Streptomyces lividans T7
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
expression of recombinant wild-type and K304E mutant enzyme in Escherichia coli
expression of T168A mutant enzyme in Escherichia coli
-
gene ACADM, DNA and amino acid sequence determination and analysis
-
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
-
in vitro translation in rabbit reticulocyte lysate
-
overexpression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A1010C
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency
A151T
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
A533C
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency
D79X
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
E18K
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
E376G
-
the rate of dehydrogenation is lowered by approximately 5 orders of magnitude
E376Q/E99G
-
the rate of dehydrogenation is lowered by 4-5 orders of magnitude
G127A
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency, not clearly associated with a clinical phenotype
G170R
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
G285R
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
G799A
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency
K304E
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
K329E
-
reported to be responsible for medium-chain CoA dehydrogenase deficiency
L59F
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
L73DELTA
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
N169D
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
N396Y
-
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
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
Q20R
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
R123K
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
R256S
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
T1229G
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency
T168A
-
thermostability is markedly decreased, 80% lowered activity in ferricinum assay
T199C
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency, not clearly associated with a clinical phenotype
T255E
-
same activity with octanoyl-CoA as wild-type, activity/chain length profile is, however, narrower
T255E/E376G
-
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
-
shifts the chain length activity profile to higher values, drastic reduction of maximal velocity
T92T
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
T96I
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
V362V
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
Y42H
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
K304E
-
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 42C compared to wild-type enzyme
R256K
-
3.6fold increase in Km-value for octanoyl-CoA, 45fold decrease in turnovernumber with octanoyl-CoA compared to wild-type enzyme
Y375A
-
very low acyl-CoA dehydrogenase activity
Y375E
-
inactive
Y375F
-
very low acyl-CoA dehydrogenase activity
Y375K
-
very low acyl-CoA dehydrogenase activity, mutant exhibits acyl-CoA oxidase activity
Y42H
-
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 42C compared to wild-type enzyme
E276Q
-
no detectable activity in ferricenium assay
E376P
-
no detectable activity in ferricenium assay
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
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
Show AA Sequence (427 entries)
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