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
1.3.8.7
-
RECOMMENDED NAME
GeneOntology No.
medium-chain acyl-CoA dehydrogenase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dehydrogenation
-
-
-
-
oxidation
-
-
-
-
oxidation
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
fatty acid salvage
-
Fatty acid degradation
-
Valine, leucine and isoleucine degradation
-
beta-Alanine metabolism
-
Propanoate metabolism
-
Metabolic pathways
-
Biosynthesis of secondary metabolites
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ACAD-9
-
-
acyl CoA dehydrogenase
-
-
-
-
acyl CoA dehydrogenase
-
-
acyl coenzyme A dehydrogenase
-
-
-
-
acyl dehydrogenase
-
-
-
-
acyl-CoA dehydrogenase
-
-
acyl-CoA dehydrogenase
-
-
acyl-CoA dehydrogenase
-
-
acyl-CoA dehydrogenase-9
-
-
dehydrogenase, acyl coenzyme A
-
-
-
-
EC 1.3.2.2
-
-
formerly
-
fatty acyl coenzyme A dehydrogenase
-
-
-
-
fatty-acyl-CoA dehydrogenase
-
-
-
-
general acyl CoA dehydrogenase
-
-
-
-
LCAD
-
-
MCAD
-
-
-
-
MCADH
-
-
medium chain acyl-CoA dehydrogenase
-
-
medium chain acyl-CoA dehydrogenase
-
-
medium chain acyl-CoA dehydrogenase
-
-
medium chain-specific acyl-CoA oxidase
-
-
medium-chain acyl CoA dehydrogenase
-
-
medium-chain acyl-CoA dehydrogenase
-
-
-
-
medium-chain acyl-CoA dehydrogenase
-
-
medium-chain acyl-CoA dehydrogenase
-
-
medium-chain acyl-CoA dehydrogenase
-
-
medium-chain acyl-coenzyme A dehydrogenase
-
-
-
-
medium-chain acyl-coenzyme A dehydrogenase
-
-
medium-chain acyl-coenzyme A dehydrogenase
-
-
medium-chain coenzyme A dehydrogenase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9027-65-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
wild-type strain CB13 and proline auxotrophic strain CB15
-
-
Manually annotated by BRENDA team
gene ACADM
-
-
Manually annotated by BRENDA team
Japanese patients with medium-chain acyl-CoA dehydrogenase deficiency
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
skin fibroblast cell lines from healthy subjects and from patients with medium-chain, long-chain and with multiple-chain acyl-CoA dehydrogenase deficiency
-
-
Manually annotated by BRENDA team
T168A mutation found in patients with medium-chain acyl-CoA deficiency
-
-
Manually annotated by BRENDA team
Mougeotia sp.
algae
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
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
-
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 ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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 + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
specific for chain lengths C4-C13
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
chain-length specificity depending on electron acceptor: with phenazine methosulfate hexanoyl-CoA, with electron transfer flavoprotein, octanoyl-CoA
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
specific for chain lengths C6-C12
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
2-p-iodophenyl-3-p-nitrophenyl-5-phenyl-2H-tetrazolium chloride as final electron acceptor
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
enzyme-substrate interactions
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
enzyme-substrate interactions
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
intermediary electron acceptor: 2,6-dichloroindophenol
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
intermediary electron acceptor: 2,6-dichloroindophenol
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
intermediary electron acceptor: 2,6-dichloroindophenol
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
intermediary electron acceptor: 2,6-dichloroindophenol
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
intermediary electron acceptor: 2,6-dichloroindophenol
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
intermediary electron acceptor: 2,6-dichloroindophenol
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
intermediary electron acceptor: 2,6-dichloroindophenol
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
intermediary electron acceptor: 2,6-dichloroindophenol
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate or electron transfer flavoprotein
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate or electron transfer flavoprotein
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate or electron transfer flavoprotein
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate or electron transfer flavoprotein
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
electron acceptor: phenazine methosulfate or electron transfer flavoprotein
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
final electron acceptor: 8-dimethylamino-2,3-benzophenoxazinium chloride, trivial name meldola's blue
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
final electron acceptor: 8-dimethylamino-2,3-benzophenoxazinium chloride, trivial name meldola's blue
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
final electron acceptor: 8-dimethylamino-2,3-benzophenoxazinium chloride, trivial name meldola's blue
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
final electron acceptor: 8-dimethylamino-2,3-benzophenoxazinium chloride, trivial name meldola's blue
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
final electron acceptor: 8-dimethylamino-2,3-benzophenoxazinium chloride, trivial name meldola's blue
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
final electron acceptor: 8-dimethylamino-2,3-benzophenoxazinium chloride, trivial name meldola's blue
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
final electron acceptor: 8-dimethylamino-2,3-benzophenoxazinium chloride, trivial name meldola's blue
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
final electron acceptor: 8-dimethylamino-2,3-benzophenoxazinium chloride, trivial name meldola's blue
-
?
acyl-CoA + acceptor
2,3-dehydroacyl-CoA + reduced acceptor
show the reaction diagram
-
specific for chain lengths C6-C8
-
?
acyl-CoA + electron transfer flavoprotein
2,3-dehydroacyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
-
first step in beta-oxidation of fatty acids
-
?
acyl-CoA + electron transfer flavoprotein
2,3-dehydroacyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
-
first step in beta-oxidation of fatty acids
-
?
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 + 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
-
-
-
?
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
-
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
-
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
-
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
r
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
-
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
reduction potential
-
-
butanoyl-CoA + acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
potentiometric measurements
-
-
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 + acceptor
2-decenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
decanoyl-CoA + acceptor
2-decenoyl-CoA + reduced acceptor
show the reaction diagram
-
acceptors: phenazine methosulfate or electron transferring flavoprotein
-
?
decanoyl-CoA + acceptor
2-decenoyl-CoA + reduced acceptor
show the reaction diagram
-
72% of activity with hexanoyl-CoA
-
?
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
-
-
-
-
?
decanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-trans-decenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
-
decanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-trans-decenoyl-CoA + reduced acceptor
show the reaction diagram
-
electron acceptor: Meldola's Blue and iodonitrotetrazoliumchloride, general and long-chain acyl-CoA dehydrogenase
-
?
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
-
-
-
?
dodecanoyl-CoA + acceptor
2-dodecenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
-
dodecanoyl-CoA + acceptor
2-dodecenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
dodecanoyl-CoA + acceptor
2-dodecenoyl-CoA + reduced acceptor
show the reaction diagram
-
acceptors: phenazine methosulfate or electron transferring flavoprotein
-
?
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
-
-
-
-
?
heptadecan-2-onyl-dethio-CoA + phenazine methosulfate + 2,6-dichloroindophenol
?
show the reaction diagram
-
58% of activity with hexadecanoyl-CoA
-
-
?
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 + acceptor
2-hexadecenoyl-CoA + reduced acceptor
show the reaction diagram
-
55% of activity with hexanoyl-CoA
-
-
-
hexadecanoyl-CoA + acceptor
2-hexadecenoyl-CoA + reduced acceptor
show the reaction diagram
-
acceptors: phenazine methosulfate or electron transferring flavoprotein, very low activity
-
?
hexadecanoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans-hexadecenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
-
hexadecanoyl-CoA + Meldola's Blue + iodonitrotetrazoliumchloride
2-trans-hexadecenoyl-CoA + reduced acceptor
show the reaction diagram
-
cis-double bond has almost no effect on velocity of general acyl-CoA dehydrogenase
-
?
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 + acceptor
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
-
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
best substrate
-
-
-
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
acceptors: phenazine methosulfate or electron transferring flavoprotein, best substrate with phenazine methosulfate
-
?
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
100% activity
-
-
?
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 + ferricenium hexafluorophosphate
indoleacryloyl-CoA + ferrocenium hexafluorophosphate
show the reaction diagram
-
chromogenic substrate showing a strong absorption band in the near visible region
-
-
indolepropionyl-CoA + O2
indoleacryloyl-CoA + H2O2
show the reaction diagram
-
very low activity
-
?
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
-
-
-
?
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-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
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
-
best substrate with electron transferring flavoprotein
-
-
-
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
best substrate for medium-chain acyl-CoA dehydrogenase
-
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
no activity with tetradecanoyl-CoA and hexadecanoyl-CoA
-
-
-
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
no activity with tetradecanoyl-CoA and hexadecanoyl-CoA
-
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
82% of activity with hexanoyl-CoA
-
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
phenazine methosulfate substituted by electron transfer flavoprotein
-
?
n-octanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
fibroblast medium-chain acyl-CoA dehydrogenase is specific towards C6-C8 acyl-CoA esters
-
-
?
n-tetradecanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-tetradecenoyl-CoA + reduced acceptor
show the reaction diagram
-
best substrate for long-chain acyl-CoA dehydrogenase
-
?
n-tetradecanoyl-CoA + phenazine methosulfate + 2,6-dichloroindophenol
2-tetradecenoyl-CoA + reduced acceptor
show the reaction diagram
-
best substrate for long-chain acyl-CoA dehydrogenase
-
?
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
-
-
-
-
-
octadecanoyl-CoA + acceptor
2-octadecenoyl-CoA + reduced acceptor
show the reaction diagram
-
acceptors: phenazine methosulfate or electron transferring flavoprotein, extremely low activity
-
?
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
-
-
?
octanoyl-CoA + acceptor
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + acceptor
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
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 + electron transferring flavoprotein
2-octenoyl-CoA + reduced electron transferring flavoprotein
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + electron transferring flavoprotein
2-octenoyl-CoA + reduced electron transferring flavoprotein
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
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
-
-
-
-
-
pentanoyl-CoA + acceptor
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
-
68% of activity with hexanoyl-CoA
-
?
pentanoyl-CoA + acceptor
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
-
acceptors: phenazine methosulfate or electron transferring flavoprotein
-
?
phenylpropionyl-CoA + acceptor
? + reduced acceptor
show the reaction diagram
-
-
-
-
?
phenylpropionyl-CoA + acceptor
? + reduced acceptor
show the reaction diagram
-
110% activity
-
-
?
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
-
-
-
?
tetradecanoyl-CoA + acceptor
2-tetradecenoyl-CoA + reduced acceptor
show the reaction diagram
-
acceptors: phenazine methosulfate or electron transferring flavoprotein, low activity
-
?
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
-
-
-
?
linoleoyl-CoA + oxidized electron transfer flavoprotein
? + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
key enzyme for the beta-oxidation of fatty acids
-
-
-
additional information
?
-
-
substrate/product binding results in ligand polarization and positive flavin potential shifts, which activate the enzyme for electron transfer
-
-
-
additional information
?
-
-
acts on a wide range of chain lengths (C16-C4)
-
-
-
additional information
?
-
-
beta-oxidation enzymes encoded by the pim gene cluster including acyl CoA dehydrogenase are active with medium-chain-length dicarboxylic acids
-
-
-
additional information
?
-
-
involved in the formation of unsaturated fatty acid
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
first step in beta-oxidation of fatty acids
-
?
octanoyl-CoA + electron transferring flavoprotein
2-octenoyl-CoA + reduced electron transferring flavoprotein
show the reaction diagram
-
-
-
-
?
acyl-CoA + electron transfer flavoprotein
2,3-dehydroacyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
-
first step in beta-oxidation of fatty acids
-
?
additional information
?
-
-
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
-
-
-
additional information
?
-
-
key enzyme for the beta-oxidation of fatty acids
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
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
FAD
-
FAD is readily lost upon purification
FAD
-
1 mol per mol of subunit
FAD
-
1 mol per mol of subunit
FAD
-
1 mol per mol of subunit; binding of FAD and FAD anologues; reconstitution of the apoenzyme with 8-chloro-FAD, 8-bromo-FAD or 2-thio-FAD yields an active holoenzyme
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
-
is not the target of the inhibitor
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
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(Methylenecyclopropyl)acetyl-CoA
-
0.01 mM, 95% inhibition
(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
-
-
(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
(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
-
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
2-octynoyl-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
-
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
L-3-hydroxyoctanoyl-CoA
-
0.03 mM, 7% inhibition
Methylmercury chloride
-
0.1 mM, strong inhibition
Methylmercury iodide
-
0.1 mM, strong inhibition, half-time of inactivation: 2 min, octanoyl-CoA protects
N-ethylmaleimide
-
2 mM, 43% inhibition
N-ethylmaleimide
-
inhibitory to apo-enzyme, 2 mM, half-time of inactivation: 4 min, complete inactivation after 20 min
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
-
0.1 mM, 17% inhibition
p-chloromercuribenzoate
-
inhibition of apo-enzyme
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
Methylmercury iodide
-
-
additional information
-
not inhibited by saturated and 2,3-unsaturated branched chain acyl-CoA compounds
-
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 trans-2,trans-4-octadienoyl-CoA and oct-2-en-4-ynoyl-CoA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
beta(2-furyl)propionyl-CoA
-
at pH 6.7
0.007
-
beta(2-furyl)propionyl-CoA
-
at pH 8.5
0.0091
-
beta-(2-Furyl)propionyl-CoA
-
-
0.0084
-
Butanoyl-CoA
-
-
0.04
-
Butanoyl-CoA
-
-
0.07
-
Butanoyl-CoA
-
T255E mutant enzyme
0.09
-
Butanoyl-CoA
-
-
0.12
-
Butanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
0.135
-
Butanoyl-CoA
-
-
0.175
-
Butanoyl-CoA
-
-
0.264
-
Butanoyl-CoA
-
-
0.45
-
Butanoyl-CoA
-
-
0.00714
-
Butyryl-CoA
-
-
0.016
0.038
crotonyl-CoA
-
hydratase reaction, value depending on pH
0.0007
-
Decanoyl-CoA
-
-
0.00094
-
Decanoyl-CoA
-
-
0.0025
-
Decanoyl-CoA
-
-
0.0029
-
Decanoyl-CoA
-
-
0.0029
-
Decanoyl-CoA
-
-
0.0042
-
Decanoyl-CoA
-
T255E/E376G double mutant enzyme
0.0054
-
Decanoyl-CoA
-
-
0.0077
-
Decanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
0.0091
-
Decanoyl-CoA
-
-
0.01
-
Decanoyl-CoA
-
T255E mutant enzyme
0.03
-
Decanoyl-CoA
-
-
0.05
-
Decanoyl-CoA
-
T255E/E376T double mutant enzyme
0.0025
-
Dodecanoyl-CoA
-
-
0.0033
-
Dodecanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
0.0043
-
Dodecanoyl-CoA
-
-
0.0057
-
Dodecanoyl-CoA
-
-
0.0066
-
Dodecanoyl-CoA
-
T255E/E376G double mutant enzyme
0.05
-
Dodecanoyl-CoA
-
T255E/E376T double mutant enzyme
0.0034
-
electron transfer flavoprotein
-
-
0.0045
-
electron transfer flavoprotein
-
-
0.0003
0.001
electron transferring flavoprotein
-
-
0.00035
-
electron transferring flavoprotein
-
-
0.001
-
electron transferring flavoprotein
-
-
0.01
-
electron transferring flavoprotein
-
-
0.0024
-
FAD
-
-
0.055
-
ferricenium hexafluorophosphate
-
-
0.0099
-
ferrocenium hexafluorophosphate
-
substrate indolepropionyl-CoA
0.069
-
ferrocenium hexafluorophosphate
-
substrate octanoyl-CoA
0.014
-
furylpropionyl-CoA
-
-
0.0144
-
furylpropionyl-CoA
-
-
0.001
-
hexadecanoyl-CoA
-
in the presence of bovine serum albumin
0.0013
-
hexadecanoyl-CoA
-
T255E/E376G double mutant enzyme
0.0016
-
hexadecanoyl-CoA
-
-
0.002
-
hexadecanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
0.0014
-
Hexanoyl-CoA
-
T255E mutant enzyme
0.0035
-
Hexanoyl-CoA
-
-
0.0036
-
Hexanoyl-CoA
-
-
0.004
-
Hexanoyl-CoA
-
-
0.005
-
Hexanoyl-CoA
-
-
0.0068
-
Hexanoyl-CoA
-
-
0.0075
-
Hexanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
0.008
-
Hexanoyl-CoA
-
-
0.009
-
Hexanoyl-CoA
-
-
0.0094
-
Hexanoyl-CoA
-
-
0.015
-
Hexanoyl-CoA
-
-
0.0216
-
Hexanoyl-CoA
-
-
0.00049
-
indolepropionyl-CoA
-
oxidase reaction
0.0087
-
indolepropionyl-CoA
-
-
0.01
-
indolepropionyl-CoA
-
-
0.0011
-
Octanoyl 3'-dephospho-CoA
-
-
0.00928
-
Octanoyl-1,N6-etheno-CoA
-
-
0.00084
-
Octanoyl-CoA
-
mutant enzyme Y375K, in 50 mM potassium phosphate buffer, pH 7.6
0.001
-
Octanoyl-CoA
-
-
0.001
-
Octanoyl-CoA
-
T255E/E376G double mutant enzyme
0.002
-
Octanoyl-CoA
-
-
0.0021
-
Octanoyl-CoA
-
pH 7.6, 25C, mutant enzyme E376Q
0.0022
-
Octanoyl-CoA
-
25C, with ferricenium as acceptor, pig enzyme reconstituted with 2'-deoxy-FAD
0.00221
-
Octanoyl-CoA
-
-
0.0023
-
Octanoyl-CoA
-
-
0.0023
-
Octanoyl-CoA
-
25C, with ferricenium as acceptor, native enzyme
0.0023
-
Octanoyl-CoA
-
wild-type enzyme
0.0023
-
Octanoyl-CoA
-
-
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
-
25C, with ferricenium as acceptor, recombinant wild-type enzyme
0.0026
-
Octanoyl-CoA
-
25C, with ferricenium as acceptor, pig enzyme reconstituted with commercial FAD
0.003
-
Octanoyl-CoA
-
-
0.003
-
Octanoyl-CoA
-
pH 7.6, 25C, wild-type enzyme
0.0032
-
Octanoyl-CoA
-
-
0.0034
-
Octanoyl-CoA
-
-
0.0035
-
Octanoyl-CoA
-
-
0.0037
-
Octanoyl-CoA
-
wild-type enzyme
0.004
-
Octanoyl-CoA
-
-
0.0059
-
Octanoyl-CoA
-
mutant enzyme K304E
0.00684
-
Octanoyl-CoA
-
mutant enzyme Y375A, in 50 mM potassium phosphate buffer, pH 7.6
0.008
-
Octanoyl-CoA
-
T255E mutant enzyme
0.0082
-
Octanoyl-CoA
-
mutant enzyme R256K
0.012
-
Octanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
1.47
-
Octanoyl-CoA
-
with phenazine methosulfate
0.107
-
octanoyl-pantetheine
-
-
0.00007
-
palmitoleoyl-CoA
-
-
0.0008
-
palmitoyl-CoA
-
-
0.023
-
palmitoyl-CoA
-
-
0.0396
-
pentanoyl-CoA
-
-
1.67
-
phenazine methosulfate
-
-
0.0023
-
tetradecanoyl-CoA
-
-
0.0052
-
tetradecanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
0.0055
-
tetradecanoyl-CoA
-
T255E/E376G double mutant enzyme
0.0057
-
tetradecanoyl-CoA
-
-
0.01
-
tetradecenoyl-CoA
-
-
-
0.0563
-
valeryl-CoA
-
-
0.0426
-
[4-(dimethylamino)phenyl]propionyl-CoA
-
-
0.061
-
[4-(dimethylamino)phenyl]propionyl-CoA
-
-
0.00021
-
linoleoyl-CoA
-
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6.2
-
Butanoyl-CoA
-
-
6.33
-
Butanoyl-CoA
-
ferricenium assay
8.33
-
Butanoyl-CoA
-
wild-type and T255E mutant enzyme
9
-
Butanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
11.5
-
Butanoyl-CoA
-
-
0.00233
0.00783
crotonyl-CoA
-
hydratase activity, value depending on pH
0.233
-
Decanoyl-CoA
-
T255E/E376T double mutant enzyme
0.333
-
Decanoyl-CoA
-
T255E/E376G double mutant enzyme
7.4
-
Decanoyl-CoA
-
-
8.6
-
Decanoyl-CoA
-
-
8.83
-
Decanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
9.67
-
Decanoyl-CoA
-
-
11.3
-
Decanoyl-CoA
-
T255E mutant enzyme
11.7
-
Decanoyl-CoA
-
-
7
-
dodecadecanoyl-coA
-
-
3.33
-
Dodecanoyl-CoA
-
T255E/E376G double mutant enzyme
9.17
-
Dodecanoyl-CoA
-
-
9.5
-
Dodecanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
11.6
-
electron transfer flavoprotein
-
-
1.17
2
electron transferring flavoprotein
-
-
2.33
-
electron transferring flavoprotein
-
medium chain acyl-CoA dehydrogenase from kidney, terminal acceptor 2,6-dichlorphenol-indophenol
12
-
electron transferring protein
-
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
13.2
-
furylpropionyl-CoA
-
-
13.6
-
furylpropionyl-CoA
-
-
0.617
-
hexadecanoyl-CoA
-
T255E/E376G double mutant enzyme
2.33
-
hexadecanoyl-CoA
-
-
2.92
-
hexadecanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
2.83
-
Hexanoyl-CoA
-
T255E mutant enzyme
12.7
-
Hexanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
14.2
-
Hexanoyl-CoA
-
-
16.8
-
Hexanoyl-CoA
-
-
20.6
-
Hexanoyl-CoA
-
-
20.8
-
Hexanoyl-CoA
-
ferricenium assay
31.2
-
Hexanoyl-CoA
-
medium-chain acyl-CoA dehydrogenase
0.016
-
indolepropionyl-CoA
-
oxidase reaction
0.46
-
indolepropionyl-CoA
-
-
3.4
-
indolepropionyl-CoA
-
-
0.1
-
meldola's blue
-
medium chain acyl-CoA dehydrogenase from kidney, terminal acceptor iodonitrotetrazolium
0.667
-
Octadecanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
0.0024
-
Octanoyl-CoA
-
pH 7.6, 25C, mutant enzyme E376Q
0.038
-
Octanoyl-CoA
-
mutant enzyme Y375K, in 50 mM potassium phosphate buffer, pH 7.6
0.047
-
Octanoyl-CoA
-
25C, with ferricenium as acceptor, pig enzyme reconstituted with 2'-deoxy-FAD
0.071
-
Octanoyl-CoA
-
mutant enzyme R256K
0.167
-
Octanoyl-CoA
-
T255E/E376G double mutant enzyme
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
3.17
-
Octanoyl-CoA
-
-
3.17
-
Octanoyl-CoA
-
phenazine methosulfate as electron carrier
3.2
-
Octanoyl-CoA
-
wild-type enzyme
3.25
-
Octanoyl-CoA
-
phenazine methosulfate and 2,6-dichlorophenolindophenol as electron acceptors
3.3
-
Octanoyl-CoA
-
C-2 proton/deuteron exchange
3.3
-
Octanoyl-CoA
-
wild type enzyme, in 50 mM potassium phosphate buffer, pH 7.6
8.33
-
Octanoyl-CoA
-
with electron transferring flavoprotein as electron carrier
11.2
-
Octanoyl-CoA
-
general acyl-CoA dehydrogenase
13.2
-
Octanoyl-CoA
-
T255E mutant enzyme
16.2
-
Octanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
16.3
-
Octanoyl-CoA
-
-
17
-
Octanoyl-CoA
-
pH 7.6, 25C, wild-type enzyme
18.3
-
Octanoyl-CoA
-
ferricenium assay
18.8
-
Octanoyl-CoA
-
25C, with ferricenium as acceptor, recombinant wild-type enzyme
19.2
-
Octanoyl-CoA
-
-
19.6
-
Octanoyl-CoA
-
-
19.6
-
Octanoyl-CoA
-
25C, with ferricenium as acceptor, native enzyme
19.6
-
Octanoyl-CoA
-
-
20
-
Octanoyl-CoA
-
25C, with ferricenium as acceptor, pig enzyme reconstituted with commercial FAD
27.2
-
Octanoyl-CoA
-
-
33.3
-
Octanoyl-CoA
-
-
35.7
-
Octanoyl-CoA
-
-
0.235
-
octanoyl-pantetheine
-
general acyl-CoA dehydrogenase
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
1.67
-
recombinant beta-Y16L electron transferring flavoprotein
-
T168A mutant enzyme
-
18.3
-
recombinant beta-Y16L electron transferring flavoprotein
-
wild-type enzyme
-
1
-
recombinant electron transferring flavoprotein
-
T168A mutant enzyme
-
14.7
-
recombinant electron transferring flavoprotein
-
wild-type enzyme
-
2.67
-
tetradecanoyl-CoA
-
T255E/E376G double mutant enzyme
4.67
-
tetradecanoyl-CoA
-
-
6
-
tetradecanoyl-CoA
-
long-chain acyl-CoA dehydrogenase
6
-
tetradecanoyl-CoA
-
-
8.33
-
tetradecanoyl-CoA
-
K304E mutant enzyme, ferricenium assay
0.61
-
[4-(dimethylamino)phenyl]propionyl-CoA
-
-
4.6
-
[4-(dimethylamino)phenyl]propionyl-CoA
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00073
-
2,3-octadienoyl-CoA
-
-
0.0034
-
2-octenoyl-CoA
-
-
0.00036
-
2-octynoyl-CoA
-
competitive vs. indolepropionyl-CoA
0.0065
-
2-octynoyl-CoA
-
-
0.0134
-
3-butynoyl-CoA
-
-
0.0007
-
3-oxodecanoyl-CoA
-
-
0.00567
-
acetoacetyl-CoA
-
uncompetitive vs. electron transferring flavoprotein
0.0074
-
acetoacetyl-CoA
-
competitive vs. butanoyl-CoA
0.0144
-
crotonyl-CoA
-
uncompetitive vs. electron transferring flavoprotein
0.015
-
crotonyl-CoA
-
-
0.0165
0.0184
crotonyl-CoA
-
competitive vs. butanoyl-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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
-
-
4.46
-
-
substrate indolepropionyl-CoA, ferrocenium hexafluorophosphate as electron carrier
6.75
-
-
-
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
-
-
-
8.5
-
-
-
9
10
-
T168A mutant
9
-
-
enoyl-CoA hydratase activity
10
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
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 ACCESSION NO.
COMMENTARY
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45000
-
-
SDS-PAGE
119000
-
-
gel filtration
155000
-
-
enzyme from heart, SDS-PAGE after cross-linkage with dimethylsuberimidate
160000
-
-
gel filtration
160000
-
-
SDS-PAGE after cross-linkage with dimethylsuberimidate
160000
-
-
gel filtration
178000
-
-
gel filtration
178000
-
-
gel filtration and empirically determined diffusion constant
180000
-
-
gel filtration
182000
-
-
gel filtration
183000
-
-
gel filtration
205000
-
-
native gel electrophoresis in polyacrylamide gradient
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 43000, SDS-PAGE
dimer
-
gel filtration, 64800, predicted by 37-amino acid leader peptide cleaved sequentially by two mitochondrial peptidases
tetramer
-
4 * 43685, mature enzyme, calculation from nucleotide sequence; values for precursor enzyme and leader peptide
tetramer
-
4 * 44000, SDS-PAGE
tetramer
-
4 * 45000, SDS-PAGE
tetramer
-
4 * 43300, SDS-PAGE
tetramer
-
4 * 45500, SDS-PAGE
tetramer
-
4 * 43685, mature enzyme, calculation from nucleotide sequence
tetramer
-
4 * 45000, SDS-PAGE
tetramer
-
-
tetramer
-
4 * 42000, SDS-PAGE
tetramer
-
4 * 43000, recombinant enzyme, SDS-PAGE
tetramer
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
LITERATURE
no inactivation by freezing/thawing
-
enoyl-CoA compounds and acyl-CoA compounds stabilize the semiquinone form of enzyme
-
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 ACCESSION NO.
LITERATURE
-70C, concentrated form, more than 1 year, no loss of activity
-
-20C, at least 1 month
-
-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
-
-20C, 100 mM phosphate buffer, pH 7.6
-
-70C, concentrated form, more than 1 year, no loss of activity
-
4C, ammonium sulfate suspension
-
frozen, 50 mM phosphate buffer, pH 7.6
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
affinity-purified, ca. 95% pure
-
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
-
HiTrap chelating nickel affinity chromatography
-
recombinant enzyme
-
apoprotein
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloned on plasmid pEHEX2 and heterologous expression in Streptomyces lividans T7
-
expressed in Escherichia coli
-
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
-
expressed in Escherichia coli BL21(DE3) cells
-
overexpression in Escherichia coli
-
expression in Escherichia coli
-
expression of recombinant wild-type and K304E mutant enzyme in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
A31P
-
involved in medium chain acyl-CoA dehydrogenase deficiency
A31P
-
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
A985G
-
mutant is involved in medium chain acyl-CoA dehydrogenase deficiency
A985G
-
involved in MCAD deficiency
A985G
-
in the Brazilian population, about 0.41% of individuals are heterozygous for the A985G mutation. The mutant homozygous genotype was not found
A985G
-
genotype, the naturally occuring mutation is involved in medium-chain acyl-CoA dehydrogenase deficiency, phenotype, overview
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
-
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
E376Q
-
the rate of dehydrogenation is lowered by 4-5 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
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
E276Q
-
no detectable activity in ferricenium assay
E376P
-
no detectable activity in ferricenium assay
additional information
-
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
-
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
L73DELTA
-
the mutation is involved in medium chain acyl-CoA dehydrogenase deficiency
additional information
-
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
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
additional information
-
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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
in the Brazilian population, about 0.41% of individuals are heterozygous for the A985G mutation. The mutant homozygous genotype was not found
medicine
-
inhibitor may become a lead for further development for treating non-insulin-dependent diabetes mellitus
additional information
-
acyl-CoA dehydrogenase LipB is involved in the introduction of the unusual Dcis3 double bond into the acyl residue of friulimicin
additional information
-
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
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
additional information
-
highly homologous to human very-long-chain acyl-CoA dehydrogenase
medicine
-
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
additional information
-
development of fluorogenic and fluoromorphic probes for the enzyme as indicators for selective and sensetive detection of MCAD activity in tissue homogenates