Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(3,3-difluorobutyryl)pantetheine + phenazine methosulfate + dichlorophenolindophenol
3-fluoro-2-butenoylpantetheine + HF
-
-
-
?
(E)-2-butenoyl-CoA + reduced methylviologen
? + oxidized methylviologen
-
-
-
-
?
(S)-2-methylbutyryl-CoA + phenazine methosulfate + dichloroindophenol
(S)-2-methyl-2-butenoyl-CoA + reduced acceptor
-
6.0% of activity with butyryl-CoA
-
?
2-azabutyryl-CoA + ?
?
-
substrate may be converted by intrinsic hydratase activity of the enzyme to 2-azaacetyl-CoA
-
-
?
2-butenoyl-CoA + reduced acceptor
butanoyl-CoA + acceptor
-
reduction in vivo
-
-
r
2-butenoyl-CoA + reduced acceptor
butyryl-CoA + acceptor
-
trans-addition of hydrogen
-
?
2-butenoyl-CoA + reduced electron transfer flavoprotein
butanoyl-CoA + electron transfer protein
-
enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro
-
r
2-hexenoyl-CoA + reduced electron transfer flavoprotein
hexanoyl-CoA + electron transfer protein
-
enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro
-
r
2-methylbutanoyl-CoA + acceptor
2-methyl-2-butenoyl-CoA + reduced acceptor
-
-
-
-
r
2-methylbutyryl-CoA + electron acceptor
2-methyl-2-butenoyl-CoA + reduced acceptor
-
highest activity
-
-
?
2-methylpropionyl-CoA + phenazine methosulfate + dichloroindophenol
2-methylpropenoyl-CoA + reduced acceptor
-
1.5% of activity with butyryl-CoA
-
?
2-pentenoyl-CoA + reduced electron transfer flavoprotein
pentanoyl-CoA + electron transfer protein
-
enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro
-
r
2-propenoyl-CoA + reduced electron transfer flavoprotein
propanoyl-CoA + electron transfer protein
3-fluoropropionyl-CoA + phenazine methosulfate + dichlorophenolindophenol
2-propenoyl-CoA + HF
-
-
-
?
3-hydroxybutyryl-CoA + acceptor
acetoacetyl-CoA + reduced acceptor
4-methylpentanoyl-CoA + phenazine methosulfate + dichloroindophenol
4-methyl-2-pentenoyl-CoA + reduced acceptor
-
18.0% of activity with butyryl-CoA
-
?
acrolein + reduced methylviologen
? + oxidized methylviologen
-
-
-
-
?
acryloyl-CoA + benzyl viologen
propanoyl-CoA + reduced benzyl viologen
acryloyl-CoA + reduced methylviologen
propanoyl-CoA + oxidized methylviologen
-
-
-
-
?
butanoyl-CoA + acceptor
2-butenoyl-CoA + reduced acceptor
butanoyl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
butanoyl-CoA + FAD
2-butenoyl-CoA + FADH2
butanoyl-CoA + FAD
but-2-enoyl-CoA + FADH2
-
-
-
?
butanoyl-CoA + FAD
trans-2,3-dehydrobutanoyl-CoA + FADH2
-
-
-
-
?
butanoyl-CoA + oxidized acceptor
crotonyl-CoA + reduced acceptor
-
-
-
-
r
butyryl-CoA + 2,6-dichloro-phenolindophenol
but-2-enoyl-CoA + reduced 2,6-dichloro-phenolindophenol
-
-
-
-
r
butyryl-CoA + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
2-butenoyl-CoA + reduced acceptor
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
butyryl-CoA + electron transfer flavoprotein
2-butenoyl-CoA + reduced electron transfer flavoprotein
-
-
-
-
?
butyryl-CoA + electron transfer flavoprotein
crotonyl-CoA + reduced electron transfer flavoprotein
-
-
-
-
?
butyryl-CoA + electron-transferring flavoprotein
2-butenoyl-CoA + reduced electron-transferring flavoprotein
-
-
-
-
?
butyryl-CoA + ferricenium
2-butenoyl-CoA + ferrocene
-
-
-
-
?
butyryl-CoA + ferricytochrome c
butenoyl-CoA + reduced acceptor
-
-
-
r
butyryl-CoA + ferrocenium
2-butenoyl-CoA + ferrocene
-
-
-
-
?
butyryl-CoA + O2
2-butenoyl-CoA + H2O2
butyryl-CoA + oxidized acceptor
crotonyl-CoA + reduced acceptor
-
-
-
-
?
butyryl-CoA + pyocyanine + triphenyltetrazolium chloride
2-butenoyl-CoA + reduced acceptor
-
-
-
r
crotonyl-CoA + 2 NADH + 2 Fd-
butyryl-CoA + 2 NAD+ + 2 Fd2-
crotonyl-CoA + electron acceptor
butyryl-CoA + reduced acceptor
-
-
-
-
?
crotonyl-CoA + electron transfer flavoprotein
butyryl-CoA + ?
-
-
-
?
crotonyl-CoA + O2 + 2 NADH + 2 H+
butanoyl-CoA + H2O2 + 2 NAD+
crotonyl-CoA + reduced acceptor
butyryl-CoA + oxidized acceptor
-
-
-
-
?
crotonyl-CoA + reduced ferredoxin
butanoyl-CoA + oxidized ferredoxin
cyclobutanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-butenecarboxyl-CoA + reduced acceptor
cycloheptanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-heptenecarboxyl-CoA + reduced acceptor
-
3.2% of activity with butyryl-CoA
-
?
cyclohexanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-hexenecarboxyl-CoA + reduced acceptor
-
6.7% of activity with butyryl-CoA
-
?
cyclopentanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-pentenecarboxyl-CoA + reduced acceptor
ethyl vinyl ketone + reduced methylviologen
? + oxidized methylviologen
-
-
-
-
?
heptanoyl-CoA + electron acceptor
2-heptenoyl-CoA + reduced acceptor
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
-
-
-
-
r
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
-
-
-
?
hexanoyl-CoA + electron acceptor
2-hexenoyl-CoA + reduced acceptor
hexanoyl-CoA + electron transfer flavoprotein
2-hexenoyl-CoA + reduced acceptor
hexanoyl-CoA + FAD
hex-2-enoyl-CoA + FADH2
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
N-acetyl-S-acryloyl-cysteamine + reduced methylviologen
? + oxidized methylviologen
-
-
-
-
?
octanoyl-CoA + electron acceptor
2-octenoyl-CoA + reduced acceptor
octanoyl-CoA + electron transfer flavoprotein
octenoyl-CoA + reduced acceptor
-
-
-
-
?
octanoyl-CoA + electron transfer protein
2-octenoyl-CoA + reduced acceptor
-
-
-
?
octanoyl-CoA + Meldola's Blue + iodonitrotetrazolium chloride
2-octenoyl-CoA + reduced acceptor
pentanoyl-CoA + 2,6-dichlorophenolindophenol + phenazine ethosulfate
2-pentenoyl-CoA + reduced acceptor
pentanoyl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
-
-
-
?
pentanoyl-CoA + electron transfer flavoprotein
2-pentenoyl-CoA + reduced acceptor
-
-
-
?
pentanoyl-CoA + FAD
pent-2-enoyl-CoA + FADH2
-
-
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
pentenoyl-CoA + oxidized electron transfer flavoprotein
valeryl-CoA + reduced electron transfer flavoprotein
-
-
-
-
?
propionyl-CoA + 2,6-dichlorophenolindophenol
2-propenoyl-CoA + reduced acceptor
propionyl-CoA + electron transfer flavoprotein
2-propenoyl-CoA + reduced acceptor
-
-
-
?
propionyl-CoA + phenazine methosulfate
2-propenoyl-CoA + reduced acceptor
-
-
-
?
reduced ferredoxin + NAD+ + H+
oxidized ferredoxin + NADH
S-butyrylpantetheine + phenazine ethosulfate + dichloroindophenol
S-but-2-eneoylpantetheine + reduced acceptor
-
51.0% of activity with butyryl-CoA
-
?
valeryl-CoA + electron acceptor
2-pentenoyl-CoA + reduced acceptor
-
-
-
-
?
additional information
?
-
2-propenoyl-CoA + reduced electron transfer flavoprotein
propanoyl-CoA + electron transfer protein
-
-
-
-
?
2-propenoyl-CoA + reduced electron transfer flavoprotein
propanoyl-CoA + electron transfer protein
-
enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro
-
r
3-hydroxybutyryl-CoA + acceptor
acetoacetyl-CoA + reduced acceptor
-
-
-
?
3-hydroxybutyryl-CoA + acceptor
acetoacetyl-CoA + reduced acceptor
-
-
-
?
acryloyl-CoA + benzyl viologen
propanoyl-CoA + reduced benzyl viologen
-
-
-
-
?
acryloyl-CoA + benzyl viologen
propanoyl-CoA + reduced benzyl viologen
-
-
-
-
?
butanoyl-CoA + acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
-
r
butanoyl-CoA + acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
-
r
butanoyl-CoA + acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
-
r
butanoyl-CoA + acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
r
butanoyl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
-
-
-
-
?
butanoyl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
-
-
-
?
butanoyl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
-
-
-
-
?
butanoyl-CoA + FAD
2-butenoyl-CoA + FADH2
-
-
-
?
butanoyl-CoA + FAD
2-butenoyl-CoA + FADH2
-
-
-
-
?
butyryl-CoA + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
2-butenoyl-CoA + reduced acceptor
-
-
-
?
butyryl-CoA + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
2-butenoyl-CoA + reduced acceptor
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
r
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptors phenazine methosulfate or phenazine ethosulfate
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptors phenazine methosulfate or Meldola' s Blue (i.e. 8-dimethylamino-2,3-benzophenoxazinium chloride)
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor iodonitrotetrazolium chloride
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptor phenazine methosulfate
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptors phenazine methosulfate or electron transfer flavoprotein
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptor phenazine methosulfate
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
r
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptors phenazine methosulfate or phenazine ethosulfate
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptors phenazine methosulfate or Meldola' s Blue (i.e. 8-dimethylamino-2,3-benzophenoxazinium chloride)
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
enzyme may also have an intrinsic crotonase activity
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor iodonitrotetrazolium chloride
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor iodonitrotetrazolium chloride
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptor phenazine methosulfate
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptor phenazine methosulfate
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptors phenazine methosulfate or electron transfer flavoprotein
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptors phenazine methosulfate or electron transfer flavoprotein
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
no activity towards dicarboxylic-CoAs
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptor phenazine methosulfate
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptor phenazine methosulfate
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptor phenazine methosulfate
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
intermediate electron acceptor phenazine methosulfate
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
-
-
-
?
butyryl-CoA + O2
2-butenoyl-CoA + H2O2
-
-
-
?
butyryl-CoA + O2
2-butenoyl-CoA + H2O2
-
-
-
?
crotonyl-CoA + 2 NADH + 2 Fd-
butyryl-CoA + 2 NAD+ + 2 Fd2-
-
-
-
?
crotonyl-CoA + 2 NADH + 2 Fd-
butyryl-CoA + 2 NAD+ + 2 Fd2-
-
-
-
?
crotonyl-CoA + O2 + 2 NADH + 2 H+
butanoyl-CoA + H2O2 + 2 NAD+
the crotonyl-CoA reduction mediated by the Clostridium difficile enzyme appears to be decoupled from ferredoxin reduction in the presence of air. Here, molecular oxygen apparently serves as an electron acceptor and hydrogen peroxide is formed as a second product
-
-
?
crotonyl-CoA + O2 + 2 NADH + 2 H+
butanoyl-CoA + H2O2 + 2 NAD+
-
the crotonyl-CoA reduction mediated by the Clostridium difficile enzyme appears to be decoupled from ferredoxin reduction in the presence of air. Here, molecular oxygen apparently serves as an electron acceptor and hydrogen peroxide is formed as a second product
-
-
?
crotonyl-CoA + reduced ferredoxin
butanoyl-CoA + oxidized ferredoxin
-
-
-
?
crotonyl-CoA + reduced ferredoxin
butanoyl-CoA + oxidized ferredoxin
-
-
-
?
crotonyl-CoA + reduced ferredoxin
butanoyl-CoA + oxidized ferredoxin
-
-
-
?
crotonyl-CoA + reduced ferredoxin
butanoyl-CoA + oxidized ferredoxin
-
-
-
-
?
cyclobutanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-butenecarboxyl-CoA + reduced acceptor
-
-
-
-
?
cyclobutanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-butenecarboxyl-CoA + reduced acceptor
-
1.0% of activity with butyryl-CoA
-
?
cyclopentanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-pentenecarboxyl-CoA + reduced acceptor
-
-
-
-
?
cyclopentanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-pentenecarboxyl-CoA + reduced acceptor
-
2.1% of activity with butyryl-CoA
-
?
heptanoyl-CoA + electron acceptor
2-heptenoyl-CoA + reduced acceptor
-
-
-
-
?
heptanoyl-CoA + electron acceptor
2-heptenoyl-CoA + reduced acceptor
-
low activity
-
-
?
heptanoyl-CoA + electron acceptor
2-heptenoyl-CoA + reduced acceptor
-
low activity
-
-
?
hexanoyl-CoA + electron acceptor
2-hexenoyl-CoA + reduced acceptor
-
-
-
-
?
hexanoyl-CoA + electron acceptor
2-hexenoyl-CoA + reduced acceptor
-
-
-
-
?
hexanoyl-CoA + electron acceptor
2-hexenoyl-CoA + reduced acceptor
-
-
-
-
?
hexanoyl-CoA + electron transfer flavoprotein
2-hexenoyl-CoA + reduced acceptor
-
-
-
?
hexanoyl-CoA + electron transfer flavoprotein
2-hexenoyl-CoA + reduced acceptor
-
-
-
-
?
hexanoyl-CoA + electron transfer flavoprotein
2-hexenoyl-CoA + reduced acceptor
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
-
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
-
52% of activity with butyryl-CoA
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
-
40% of activity with butyryl-CoA
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
-
4.2% of activity with butyryl-coA
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
-
acceptor Meldola's Blue and iodonitrotetrazolium chloride
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
-
13% of butyryl-CoA activity
-
?
octanoyl-CoA + electron acceptor
2-octenoyl-CoA + reduced acceptor
-
low activity
-
-
?
octanoyl-CoA + electron acceptor
2-octenoyl-CoA + reduced acceptor
-
low activity
-
-
?
octanoyl-CoA + Meldola's Blue + iodonitrotetrazolium chloride
2-octenoyl-CoA + reduced acceptor
-
-
-
-
?
octanoyl-CoA + Meldola's Blue + iodonitrotetrazolium chloride
2-octenoyl-CoA + reduced acceptor
-
14.4% of activity with butyryl-CoA
-
?
pentanoyl-CoA + 2,6-dichlorophenolindophenol + phenazine ethosulfate
2-pentenoyl-CoA + reduced acceptor
-
-
-
-
?
pentanoyl-CoA + 2,6-dichlorophenolindophenol + phenazine ethosulfate
2-pentenoyl-CoA + reduced acceptor
-
-
-
?
pentanoyl-CoA + 2,6-dichlorophenolindophenol + phenazine ethosulfate
2-pentenoyl-CoA + reduced acceptor
-
-
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
-
pentanoyl-CoA i.e. valeryl-CoA
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
-
45% of activity with butyryl-CoA, 2,6-dichlorophenolindophenol as final electron acceptor
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
-
pentanoyl-CoA i.e. valeryl-CoA
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
-
-
-
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
-
pentanoyl-CoA i.e. valeryl-CoA
-
?
propionyl-CoA + 2,6-dichlorophenolindophenol
2-propenoyl-CoA + reduced acceptor
-
-
-
-
?
propionyl-CoA + 2,6-dichlorophenolindophenol
2-propenoyl-CoA + reduced acceptor
-
30% of activity with butyryl-CoA
-
?
propionyl-CoA + 2,6-dichlorophenolindophenol
2-propenoyl-CoA + reduced acceptor
-
20% of activity with butyryl-CoA
-
?
propionyl-CoA + 2,6-dichlorophenolindophenol
2-propenoyl-CoA + reduced acceptor
-
20% of activity with butyryl-CoA
-
?
reduced ferredoxin + NAD+ + H+
oxidized ferredoxin + NADH
-
-
-
?
reduced ferredoxin + NAD+ + H+
oxidized ferredoxin + NADH
-
-
-
-
?
additional information
?
-
the bifurcating electron transferring flavoprotein Etf and butanoyl-CoA dehydrogenase Bcd couple the exergonic reduction of crotonyl-CoA to butanoyl-CoA to the endergonic reduction of ferredoxin both with NADH. In the Etf-NADH complex, beta-FAD is acceptor of the hydride of NADH. The formed beta-FADH- is the bifurcating electron donor. As a result of a domain movement, alpha-FAD- takes up one electron yielding a stable anionic semiquinone, which donates this electron further to dehydrogenase-FAD of Bcd. The remaining nonstabilized neutral semiquinone, immediately reduces ferredoxin
-
-
?
additional information
?
-
the bifurcating electron transferring flavoprotein Etf and butanoyl-CoA dehydrogenase Bcd couple the exergonic reduction of crotonyl-CoA to butanoyl-CoA to the endergonic reduction of ferredoxin both with NADH. In the Etf-NADH complex, beta-FAD is acceptor of the hydride of NADH. The formed beta-FADH- is the bifurcating electron donor. As a result of a domain movement, alpha-FAD- takes up one electron yielding a stable anionic semiquinone, which donates this electron further to dehydrogenase-FAD of Bcd. The remaining nonstabilized neutral semiquinone, immediately reduces ferredoxin
-
-
?
additional information
?
-
-
the bifurcating electron transferring flavoprotein Etf and butanoyl-CoA dehydrogenase Bcd couple the exergonic reduction of crotonyl-CoA to butanoyl-CoA to the endergonic reduction of ferredoxin both with NADH. In the Etf-NADH complex, beta-FAD is acceptor of the hydride of NADH. The formed beta-FADH- is the bifurcating electron donor. As a result of a domain movement, alpha-FAD- takes up one electron yielding a stable anionic semiquinone, which donates this electron further to dehydrogenase-FAD of Bcd. The remaining nonstabilized neutral semiquinone, immediately reduces ferredoxin
-
-
?
additional information
?
-
the bifurcating electron transferring flavoprotein Etf and butanoyl-CoA dehydrogenase Bcd couple the exergonic reduction of crotonyl-CoA to butanoyl-CoA to the endergonic reduction of ferredoxin both with NADH. In the Etf-NADH complex, beta-FAD is acceptor of the hydride of NADH. The formed beta-FADH- is the bifurcating electron donor. As a result of a domain movement, alpha-FAD- takes up one electron yielding a stable anionic semiquinone, which donates this electron further to dehydrogenase-FAD of Bcd. The remaining nonstabilized neutral semiquinone, immediately reduces ferredoxin
-
-
?
additional information
?
-
-
enzyme is a a bifurcating butyryl-CoA dehydrogenase which catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH. Since the reoxidation of ferredoxin by a membrane-bound ferredoxin:NAD+-oxidoreductase enables electron transport phosphorylation, additional ATP is formed. The butyryl-CoA dehydrogenase from Clostridium difficile is oxygen stable and apparently uses oxygen as a cooxidant of NADH in the presence of air
-
-
?
additional information
?
-
enzyme is a a bifurcating butyryl-CoA dehydrogenase which catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH. Since the reoxidation of ferredoxin by a membrane-bound ferredoxin:NAD+-oxidoreductase enables electron transport phosphorylation, additional ATP is formed. The butyryl-CoA dehydrogenase from Clostridium difficile is oxygen stable and apparently uses oxygen as a cooxidant of NADH in the presence of air
-
-
?
additional information
?
-
-
enzyme is a a bifurcating butyryl-CoA dehydrogenase which catalyzes the NADH-dependent reduction of ferredoxin coupled to the reduction of crotonyl-CoA also by NADH. Since the reoxidation of ferredoxin by a membrane-bound ferredoxin:NAD+-oxidoreductase enables electron transport phosphorylation, additional ATP is formed. The butyryl-CoA dehydrogenase from Clostridium difficile is oxygen stable and apparently uses oxygen as a cooxidant of NADH in the presence of air
-
-
?
additional information
?
-
-
catalyzes the first step in the beta-oxidation cycle with substrate optima of 4 carbon chains
-
-
?
additional information
?
-
-
fails to oxidize propionyl-CoA, inactive with the CoA derivatives of all phenylalkanoates, the enzyme is not involved in the beta-oxidation of aromatic compounds
-
-
?
additional information
?
-
-
fails to oxidize propionyl-CoA, inactive with the CoA derivatives of all phenylalkanoates, the enzyme is not involved in the beta-oxidation of aromatic compounds
-
-
?
additional information
?
-
-
no activity with octanoyl-CoA and acetyl-CoA
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Krumholz, L.R.; Crawford, R.L.; Hemling, M.E.; Bryant, M.P.
Metabolism of gallate and phloroglucinol in Eubacterium oxidoreducens via 3-hydroxy-5-oxohexanoate
J. Bacteriol.
169
1886-1890
1987
Eubacterium oxidoreducens
brenda
Yarlett, N.; Lloyd, D.; Williams, A.G.
Butyrate formation from glucose by the rumen protozoon Dasytricha ruminantium
Biochem. J.
228
187-192
1985
Dasytricha ruminantium
brenda
Boynton, Z.L.; Bennett, G.N.; Rudolph, F.B.
Cloning, sequencing, and expression of clustered genes encoding beta-hydroxybutyryl-coenzyme A (CoA) dehydrogenase, crotonase, and butyryl-CoA dehydrogenase from Clostridium acetobutylicum ATCC 824
J. Bacteriol.
178
3015-3024
1996
Clostridium acetobutylicum
brenda
Suzuki, H.; Yamada, J.; Watanabe, T.; Suga, T.
Compartmentation of dicarboxylic acid beta-oxidation in rat liver: importance of peroxisomes in the metabolism of dicarboxylic acids
Biochim. Biophys. Acta
990
25-30
1989
Rattus norvegicus
brenda
Matsubara, Y.; Indo, Y.; Naito, E.; Ozasa, H.; Glassberg, R.; Vockley, J.; Ikeda, Y.; Kraus, J.; Tanaka, K.
Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family
J. Biol. Chem.
264
16321-16331
1989
Rattus norvegicus
brenda
Finocchiaro, G.; Ito, M.; Tanaka, K.
Purification and properties of short chain acyl-CoA, medium chain acyl-CoA, and isovaleryl-CoA dehydrogenases from human liver
J. Biol. Chem.
262
7982-7989
1987
Homo sapiens
brenda
Ikeda, Y.; Dabrowski, C.; Tanaka, K.
Separation and properties of five distinct acyl-CoA dehydrogenases from rat liver mitochondria. Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase
J. Biol. Chem.
258
1066-1076
1983
Rattus norvegicus
brenda
Ikeda, Y.; Tanaka, K.
Selective inactivation of various acyl-CoA dehydrogenases by (methylenecyclopropyl)acetyl-CoA
Biochim. Biophys. Acta
1038
216-221
1990
Rattus norvegicus
brenda
Stantom, T.B.
Glucose metabolism and NADH recycling by Treponema hyodysenteriae, the agent of swine dysentery
Appl. Environ. Microbiol.
55
2365-2371
1989
Brachyspira hyodysenteriae
brenda
Van Berkel, W.J.H.; Van den Berg, W.A.M.; Muller, F.
Large-scale preparation and reconstitution of apo-flavoproteins with special reference to butyryl-CoA dehydrogenase from Megasphaera elsdenii. Hydrophobic-interaction chromatography [published erratum appears in Eur J Biochem 1989 Apr 1;180(3):603]
Eur. J. Biochem.
178
197-207
1988
Megasphaera elsdenii
brenda
Shaw, L.; Engel, P.C.
CoA-persulphide: a possible in vivo inhibitor of mammalian short-chain acyl-CoA dehydrogenase
Biochim. Biophys. Acta
919
171-174
1987
Bos taurus
brenda
Stankovich, M.T.; Soltysik, S.
Regulation of the butyryl-CoA dehydrogenase by substrate and product binding
Biochemistry
26
2627-2632
1987
Megasphaera elsdenii
brenda
Ikeda, Y.; Keese, S.M.; Fenton, W.A.; Tanaka, K.
Biosynthesis of four rat liver mitochondrial acyl-CoA dehydrogenases: in vitro synthesis, import into mitochondria, and processing of their precursors in a cell-free system and in cultured cells
Arch. Biochem. Biophys.
252
662-674
1987
Rattus norvegicus
brenda
Fink, C.W.; Stankovich, M.T.; Soltysik, S.
Oxidation-reduction potentials of butyryl-CoA dehydrogenase
Biochemistry
25
6637-6643
1986
Megasphaera elsdenii
brenda
Waters, B.W.; Engel, P.C.; Williamson, G.
Photoinactivation of butyryl-CoA dehydrogenase
Biochem. Soc. Trans.
14
138-139
1985
Megasphaera elsdenii
-
brenda
Ikeda, Y.; Okamura-Ikeda, K.; Tanaka, K.
Spectroscopic analysis of the interaction of rat liver short-chain, medium-chain, and long-chain acyl coenzyme A dehydrogenases with acyl coenzyme A substrates
Biochemistry
24
7192-7199
1985
Rattus norvegicus
brenda
Shaw, L.; Engel, P.C.
The suicide inactivation of ox liver short-chain acyl-CoA dehydrogenase by propionyl-CoA. Formation of an FAD adduct
Biochem. J.
230
723-731
1985
Bos taurus
brenda
Okamura-Ikeda, K.; Ikeda, Y.; Tanaka, K.
An essential cysteine residue located in the vicinity of the FAD-binding site in short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria
J. Biol. Chem.
260
1338-1345
1985
Rattus norvegicus
brenda
Ikeda, Y.; Hine, D.G.; Okamura-Ikeda, K.; Tanaka, K.
Mechanism of action of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases. Direct evidence for carbanion formation as an intermediate step using enzyme-catalyzed C-2 proton/deuteron exchange in the absence of C-3 exchange
J. Biol. Chem.
260
1326-1337
1985
Rattus norvegicus
brenda
Ikeda, Y.; Okamura-Ikeda, K.; Tanaka, K.
Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme
J. Biol. Chem.
260
1311-1325
1985
Rattus norvegicus
brenda
Ghisla, S.; Thorpe, C.; Massey, V.
Mechanistic studies with general acyl-CoA dehydrogenase and butyryl-CoA dehydrogenase: evidence for the transfer of the beta-hydrogen to the flavin N(5)-position as a hydride
Biochemistry
23
3154-3161
1984
Megasphaera elsdenii
brenda
Williamson, G.; Engel, P.C.
Butyryl-CoA dehydrogenase from Megasphaera elsdenii. Specificity of the catalytic reaction
Biochem. J.
218
521-529
1984
Megasphaera elsdenii
brenda
Dommes, V.; Kunau, W.H.
Purification and properties of acyl coenzyme A dehydrogenases from bovine liver. Formation of 2-trans,4-cis-decadienoyl coenzyme A
J. Biol. Chem.
259
1789-1797
1984
Bos taurus
brenda
Shaw, L.; Engel, P.C.
The purification and properties of ox liver short-chain acyl-CoA dehydrogenase
Biochem. J.
218
511-520
1984
Bos taurus
brenda
Williamson, G.; Engel, P.C.
The effect on butyryl-CoA dehydrogenase of reagents specific for nucleophilic sulphur
Biochem. J.
211
559-566
1983
Megasphaera elsdenii
brenda
Fendrich, G.; Abeles, R.H.
Mechanism of action of butyryl-CoA dehydrogenase: reactions with acetylenic, olefinic, and fluorinated substrate analogues
Biochemistry
21
6685-6695
1982
Megasphaera elsdenii
brenda
Williamson, G.; Engel, P.C.
A convenient and rapid method for the complete removal of CoA from butyryl-CoA dehydrogenase
Biochim. Biophys. Acta
706
245-248
1982
Megasphaera elsdenii
brenda
Williamson, G.; Engel, P.C.; Mizzer, J.P.; Thorpe, C.; Massey, V.
Evidence that the greening ligand in native butyryl-CoA dehydrogenase is a CoA persulfide
J. Biol. Chem.
257
4314-4320
1982
Megasphaera elsdenii
brenda
Furuta, S.; Miyazawa, S.; Hashimoto, T.
Purification and properties of rat liver acyl-CoA dehydrogenases and electron transfer flavoprotein
J. Biochem.
90
1739-1750
1981
Rattus norvegicus
brenda
Davidson, B.; Schulz, H.
Separation, properties, and regulation of acyl coenzyme A dehydrogenases from bovine heart and liver
Arch. Biochem. Biophys.
213
155-162
1982
Bos taurus
brenda
Engel, P.C.
Butyryl-CoA dehydrogenase from Megasphaera elsdenii
Methods Enzymol.
71
359-366
1981
Megasphaera elsdenii
-
brenda
Kean, E.A.
Selective inhibition of acyl-CoA dehydrogenases by a metabolite of hypoglycin
Biochim. Biophys. Acta
422
8-14
1976
Oryctolagus cuniculus, Rattus norvegicus
brenda
Engel, P.C.; Massey, V.
The purification and properties of butyryl-coenzyme A dehydrogenase from Peptostreptococcus elsdenii
Biochem. J.
125
879-887
1971
Megasphaera elsdenii
brenda
Beinert, H.
Acyl Coenzyme A dehydrogenase
The Enzymes, 2nd Ed (Boyer, P. D. , Lardy, H. , Myrbck, K. , eds. )
7
447-466
1963
Sus scrofa
-
brenda
Ross, N.S.; Hoppel, C.L
Acyl-CoA dehydrogenase activity in the riboflavin-deficient rat
Biochem. J.
244
387-391
1987
Rattus norvegicus
brenda
La Roche, H.J.; Kellner, M.; Gunther, H.; Simon, H.
Stereochemie der Butyryl-CoA-Dehydrogenase in Clostridium kluyveri
Hoppe-Seyler's Z. Physiol. Chem.
352
399-402
1971
Clostridium kluyveri
brenda
Engel, P.C.; Massey, V.
Green butyryl-coenzyme A dehydrogenase
Biochem. J.
125
889-902
1971
Megasphaera elsdenii
brenda
Gomes, B.; Fendrich, G.; Abeles, R.H.
Mechanism of action of glutaryl-CoA and butyryl-CoA dehydrogenases. Purification of glutaryl-CoA dehydrogenase
Biochemistry
20
1481-1490
1981
Megasphaera elsdenii
brenda
Shaw, L.; Engel, P.C.
A new purification for ox liver short-chain-CoA dehydrogenase
Biochem. Soc. Trans.
11
176-177
1983
Bos taurus
-
brenda
Williamson, G.; Engel, P.C.; Nishina, Y.; Shiga, K.
A resonance raman study on the nature of charge-transfer interactions in butyryl CoA dehydrogenase
FEBS Lett.
138
29-32
1982
Megasphaera elsdenii
brenda
Ozasa, H.; Furuta, S.; Miyazawa, S.; Osumi, T.; Hashimoto, T.; Mori, M.; Miura, S.; Tatibana, M.
Biosynthesis of enzymes of rat-liver mitochondria beta-oxidation
Eur. J. Biochem.
144
453-458
1984
Rattus norvegicus
brenda
Ellison, P.A.; Engel, P.C.
Crotonase activity in preparations of butyryl-CoA dehydrogenase from Megasphaera elsdenii
Biochem. Soc. Trans.
14
158-159
1986
Megasphaera elsdenii
-
brenda
Veitch, K.; Draye, J.P.; van Hoof, F.; Stanley, H.; Sherratt, H.S.
Effects of riboflavin deficiency and clofibrate treatment on the five acyl-CoA dehydrogenases in rat liver mitochondria
Biochem. J.
254
477-481
1988
Rattus norvegicus
brenda
Green, D.E.; Mahler, H.R.
Studies on the fatty acid oxidization system of animal tissues. III. Butyryl coenzyme A dehydrogenase
J. Biol. Chem.
206
1-12
1954
Bos taurus
brenda
Mahler, H.R.
Studies on the fatty acid oxidization system of animal tissues. IV. The prosthetic group of butyryl coenzyme A dehydrogenase
J. Biol. Chem.
206
13-26
1954
Bos taurus, Sus scrofa
brenda
Becker, D.F.; Fuchs, J.A.; Banfield, D.K.; Funk, W.D.; MacGillivray, R.T.; Stankovich, M.T.
Characterization of wild-type and an active-site mutant in Escherichia coli of short-chain acyl-CoA dehydrogenase from Megasphaera elsdenii
Biochemistry
32
10736-10742
1993
Megasphaera elsdenii
brenda
Wallrabenstein, C.; Schink, B.
Evidence of reversed electron transport in syntrophic butyrate or benzoate oxidation by Syntrophomonas wolfei and Syntrophus buswellii
Arch. Microbiol.
162
136-142
1994
Syntrophomonas wolfei
-
brenda
Pace, C.P.; Stankovich, M.T.
Oxidation-reduction properties of short-chain acyl-CoA dehydrogenase: effects of substrate analogs
Arch. Biochem. Biophys.
313
261-266
1994
Megasphaera elsdenii
brenda
Djordjevic, S.; Pace, C.P.; Stankovich, M.T.; Kim, J.J.P.
Three-dimensional structure of butyryl-CoA dehydrogenase from Megasphaera elsdenii
Biochemistry
34
2163-2171
1995
Megasphaera elsdenii
brenda
Battaile, K.P.; Mohsen, A.W.A.; Vockley, J.
Functional role of the active site glutamate-368 in rat short chain Acyl-CoA dehydrogenase
Biochemistry
35
15356-15363
1996
Rattus norvegicus
brenda
Diez-Gonzalez, F.; Russell, J.B.; Hunter, J.B.
NAD-independent lactate and butyryl-CoA dehydrogenases of Clostridium acetobutylicum P262
Curr. Microbiol.
34
162-166
1997
Clostridium acetobutylicum, Clostridium acetobutylicum P262
brenda
Dakoji, S.; Shin, I.; Battaile, K.P.; Vockley, J.; Liu, H.W.
Redesigning the active-site of an acyl-CoA dehydrogenase: new evidence supporting a one-base mechanism
Bioorg. Med. Chem.
5
2157-2164
1997
Megasphaera elsdenii, Rattus norvegicus
brenda
DuPlessis, E.R.; Pellett, J.; Stankovich, M.T.; Thorpe, C.
Oxidase activity of the acyl-CoA dehydrogenases
Biochemistry
37
10469-10477
1998
Megasphaera elsdenii
brenda
Veitch, K.; Draye, J.P.; Vamecq, J.; Causey, A.G.; Barlett, K.; Sherratt, H.S.A; Van Hoof,F.
Altered acyl-CoA metabolism in riboflavin deficiency
Biochim. Biophys. Acta
1006
335-343
1989
Rattus norvegicus
brenda
Lamm, T.R.; Kohls, T.D.; Saenger, A.K.; Stankovich, M.T.
Comparison of ligand polarization and enzyme activation in medium- and short-chain acyl-coenzyme A dehydrogenase-novel analog complexes
Arch. Biochem. Biophys.
409
251-261
2003
Megasphaera elsdenii
brenda
Nguyen, T.V.; Riggs, C.; Babovic-Vuksanovic, D.; Kim, Y.S.; Carpenter, J.F.; Burghardt, T.P.; Gregersen, N.; Vockley, J.
Purification and characterization of two polymorphic variants of short chain acyl-CoA dehydrogenase reveal reduction of catalytic activity and stability of the Gly185Ser enzyme
Biochemistry
41
11126-11133
2002
Homo sapiens
brenda
Sato, K.; Nishina, Y.; Shiga, K.
Purification of electron-transferring flavoprotein from Megasphaera elsdenii and binding of additional FAD with an unusual absorption spectrum
J. Biochem.
134
719-729
2003
Megasphaera elsdenii
brenda
Battaile, K.P.; Molin-Case, J.; Paschke, R.; Wang, M.; Bennett, D.; Vockley, J.; Kim, J.J.
Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases
J. Biol. Chem.
277
12200-12207
2002
Rattus norvegicus (P15651)
brenda
Katagiri, H.; Asano, T.; Yamada, T.; Aoyama, T.; Fukushima, Y.; Kikuchi, M.; Kodama, T.; Oka, Y.
Acyl-coenzyme A dehydrogenases are localized on GLUT4-containing vesicles via association with insulin-regulated aminopeptidase in a manner dependent on its dileucine motif
Mol. Endocrinol.
16
1049-1059
2002
Mus musculus
brenda
Holm, D.A.; Dagnaes-Hansen, F.; Simonsen, H.; Gregersen, N.; Bolund, L.; Jensen, T.G.; Corydon, T.J.
Expression of short-chain acyl-CoA dehydrogenase (SCAD) proteins in the liver of SCAD deficient mice after hydrodynamic gene transfer
Mol. Genet. Metab.
78
250-258
2003
Homo sapiens
brenda
Asanuma, N.; Ishiwata, M.; Yoshii, T.; Kikuchi, M.; Nishina, Y.; Hino, T.
Characterization and transcription of the genes involved in butyrate production in Butyrivibrio fibrisolvens type I and II strains
Curr. Microbiol.
51
91-94
2005
Butyrivibrio fibrisolvens (Q65Y10)
brenda
Saenger, A.K.; Nguyen, T.V.; Vockley, J.; Stankovich, M.T.
Biochemical and electrochemical characterization of two variant human short-chain acyl-CoA dehydrogenases
Biochemistry
44
16035-16042
2005
Homo sapiens
brenda
Saenger, A.K.; Nguyen, T.V.; Vockley, J.; Stankovich, M.T.
Thermodynamic regulation of human short-chain acyl-CoA dehydrogenase by substrate and product binding
Biochemistry
44
16043-16053
2005
Homo sapiens
brenda
McMahon, B.; Gallagher, M.E.; Mayhew, S.G.
The protein coded by the PP2216 gene of Pseudomonas putida KT2440 is an acyl-CoA dehydrogenase that oxidises only short-chain aliphatic substrates
FEMS Microbiol. Lett.
250
121-127
2005
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Goetzman, E.S.; He, M.; Nguyen, T.V.; Vockley, J
Functional analysis of acyl-CoA dehydrogenase catalytic residue mutants using surface plasmon resonance and circular dichroism
Mol. Genet. Metab.
87
233-242
2006
Homo sapiens
brenda
Maggio-Hall, L.A.; Lyne, P.; Wolff, J.A.; Keller, N.P.
A single acyl-CoA dehydrogenase is required for catabolism of isoleucine, valine and short-chain fatty acids in Aspergillus nidulans
Fungal Genet. Biol.
45
180-189
2008
Aspergillus nidulans
brenda
Beattie, S.G.; Goetzman, E.; Conlon, T.; Germain, S.; Walter, G.; Campbell-Thompson, M.; Matern, D.; Vockley, J.; Flotte, T.R.
Biochemical correction of short-chain acyl-coenzyme A dehydrogenase deficiency after portal vein injection of rAAV8-SCAD
Hum. Gene Ther.
19
579-588
2008
Mus musculus
brenda
Pedersen, C.B.; Kolvraa, S.; Kolvraa, A.; Stenbroen, V.; Kjeldsen, M.; Ensenauer, R.; Tein, I.; Matern, D.; Rinaldo, P.; Vianey-Saban, C.; Ribes, A.; Lehnert, W.; Christensen, E.; Corydon, T.J.; Andresen, B.S.; Vang, S.; Bolund, L.; Vockley, J.; Bross, P.; Gregersen, N.
The ACADS gene variation spectrum in 114 patients with short-chain acyl-CoA dehydrogenase (SCAD) deficiency is dominated by missense variations leading to protein misfolding at the cellular level
Hum. Genet.
124
43-56
2008
Homo sapiens
brenda
Li, F.; Hinderberger, J.; Seedorf, H.; Zhang, J.; Buckel, W.; Thauer, R.K.
Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri
J. Bacteriol.
190
843-850
2008
Clostridium kluyveri
brenda
Martens, G.A.; Vervoort, A.; Van de Casteele, M.; Stange, G.; Hellemans, K.; Van Thi, H.V.; Schuit, F.; Pipeleers, D.
Specificity in beta cell expression of L-3-hydroxyacyl-CoA dehydrogenase, short chain, and potential role in down-regulating insulin release
J. Biol. Chem.
282
21134-21144
2007
Rattus norvegicus
brenda
Giurgiutiu, D.V.; Espinoza, L.M.; Wood, T.C.; DuPont, B.R.; Holden, K.R.
Persistent growth failure in Prader-Willi syndrome associated with short-chain acyl-CoA dehydrogenase gene variant
J. Child Neurol.
23
112-117
2008
Homo sapiens
brenda
Kragh, P.M.; Pedersen, C.B.; Schmidt, S.P.; Winter, V.S.; Vajta, G.; Gregersen, N.; Bolund, L.; Corydon, T.J.
Handling of human short-chain acyl-CoA dehydrogenase (SCAD) variant proteins in transgenic mice
Mol. Genet. Metab.
91
128-137
2007
Homo sapiens
brenda
Tein, I.; Elpeleg, O.; Ben-Zeev, B.; Korman, S.H.; Lossos, A.; Lev, D.; Lerman-Sagie, T.; Leshinsky-Silver, E.; Vockley, J.; Berry, G.T.; Lamhonwah, A.M.; Matern, D.; Roe, C.R.; Gregersen, N.
Short-chain acyl-CoA dehydrogenase gene mutation (c.319C>T) presents with clinical heterogeneity and is candidate founder mutation in individuals of Ashkenazi Jewish origin
Mol. Genet. Metab.
93
179-189
2008
Homo sapiens
brenda
Waisbren, S.E.; Levy, H.L.; Noble, M.; Matern, D.; Gregersen, N.; Pasley, K.; Marsden, D.
Short-chain acyl-CoA dehydrogenase (SCAD) deficiency: An examination of the medical and neurodevelopmental characteristics of 14 cases identified through newborn screening or clinical symptoms
Mol. Genet. Metab.
95
39-45
2008
Homo sapiens
brenda
Battisti, C.; Forte, F.; Molinelli, M.; Funghini, S.; Pasquini, E.; Tassini, M.; Dotti, M.T.; Federico, A.
A new case of short-chain acyl-CoA dehydrogenase deficiency: clinical, biochemical, genetic and (1)H-NMR spectroscopic studies
Neurol. Sci.
28
328-330
2007
Homo sapiens
brenda
Sedlmeier, H.; Simon, H.
Purification and some properties of an acryloyl-CoA reductase of Clostridium kluyveri
Biol. Chem. Hoppe-Seyler
366
953-961
1985
Clostridium kluyveri
brenda
Seeliger, S.; Janssen, P.; Schink, B.
Energetics and kinetics of lactate fermentation to acetate and propionate via methylmalonyl-CoA or acrylyl-CoA
FEMS Microbiol. Lett.
211
65-70
2002
Clostridium homopropionicum, Anaerotignum neopropionicum
brenda
Jethva, R.; Bennett, M.J.; Vockley, J.
Short-chain acyl-coenzyme A dehydrogenase deficiency
Mol. Genet. Metab.
95
195-200
2008
Homo sapiens
brenda
Skilling, H.; Coen, P.M.; Fairfull, L.; Ferrell, R.E.; Goodpaster, B.H.; Vockley, J.; Goetzman, E.S.
Brown adipose tissue function in short-chain acyl-CoA dehydrogenase deficient mice
Biochem. Biophys. Res. Commun.
400
318-322
2010
Mus musculus
brenda
Stagi, S.; Gasperini, S.; Manoni, C.; Greco, A.; Funghini, S.; Donati, A.
Autoimmune Thyroiditis, Pernicious Anaemia, Vitiligo and Scleroatrophic Lichen in a boy with short-chain acylCoA dehydrogenase deficiency
Horm. Res. Paediatr.
73
409-413
2010
Homo sapiens
brenda
Shirao, K.; Okada, S.; Tajima, G.; Tsumura, M.; Hara, K.; Yasunaga, S.; Ohtsubo, M.; Hata, I.; Sakura, N.; Shigematsu, Y.; Takihara, Y.; Kobayashi, M.
Molecular pathogenesis of a novel mutation, G108D, in short-chain acyl-CoA dehydrogenase identified in subjects with short-chain acyl-CoA dehydrogenase deficiency
Hum. Genet.
127
619-628
2010
Homo sapiens (D4QEZ8)
brenda
van Maldegem, B.T.; Wanders, R.J.; Wijburg, F.A.
Clinical aspects of short-chain acyl-CoA dehydrogenase deficiency
J. Inherit. Metab. Dis.
33
507-511
2010
Homo sapiens
brenda
Schmidt, S.P.; Corydon, T.J.; Pedersen, C.B.; Bross, P.; Gregersen, N.
Misfolding of short-chain acyl-CoA dehydrogenase leads to mitochondrial fission and oxidative stress
Mol. Genet. Metab.
100
155-162
2010
Homo sapiens
brenda
Pena, L.; Angle, B.; Burton, B.; Charrow, J.
Follow-up of patients with short-chain acyl-CoA dehydrogenase and isobutyryl-CoA dehydrogenase deficiencies identified through newborn screening: one centers experience
Genet. Med.
14
342-347
2012
Homo sapiens
brenda
Aboulnaga, e.l.-.H.; Pinkenburg, O.; Schiffels, J.; El-Refai, A.; Buckel, W.; Selmer, T.
Effect of an Oxygen-Tolerant Bifurcating Butyryl Coenzyme A Dehydrogenase/Electron-Transferring Flavoprotein Complex from Clostridium difficile on Butyrate Production in Escherichia coli
J. Bacteriol.
195
3704-3713
2013
Clostridioides difficile, Clostridioides difficile (Q18AQ1), Clostridioides difficile DSM 1296
brenda
Pepin, E.; Guay, C.; Delghingaro-Augusto, V.; Joly, E.; Madiraju, S.R.; Prentki, M.
Short-chain 3-hydroxyacyl-CoA dehydrogenase is a negative regulator of insulin secretion in response to fuel and non-fuel stimuli in INS832/13 beta-cells
J. Diabetes
2
157-167
2010
Homo sapiens
brenda
Schmidt, S.P.; Corydon, T.J.; Pedersen, C.B.; Vang, S.; Palmfeldt, J.; Stenbroen, V.; Wanders, R.J.; Ruiter, J.P.; Gregersen, N.
Toxic response caused by a misfolding variant of the mitochondrial protein short-chain acyl-CoA dehydrogenase
J. Inherit. Metab. Dis.
34
465-475
2011
Homo sapiens
brenda
Berzin, V.; Tyurin, M.; Kiriukhin, M.
Selective n-Butanol production by Clostridium sp. MTButOH1365 during continuous synthesis gas fermentation due to expression of synthetic thiolase, 3-hydroxy butyryl-CoA dehydrogenase, crotonase, butyryl-CoA dehydrogenase, butyraldehyde dehydrogenase, and NAD-dependent butanol dehydrogenase
Appl. Biochem. Biotechnol.
169
950-959
2013
Clostridium ljungdahlii, Clostridium ljungdahlii DSM 13528
brenda
Chowdhury, N.P.; Mowafy, A.M.; Demmer, J.K.; Upadhyay, V.; Koelzer, S.; Jayamani, E.; Kahnt, J.; Hornung, M.; Demmer, U.; Ermler, U.; Buckel, W.
Studies on the mechanism of electron bifurcation catalyzed by electron transferring flavoprotein (Etf) and butyryl-CoA dehydrogenase (Bcd) of Acidaminococcus fermentans
J. Biol. Chem.
289
5145-5157
2014
Acidaminococcus fermentans (D2RIQ3), Acidaminococcus fermentans (D2RIQ3 and D2RL84), Acidaminococcus fermentans, Acidaminococcus fermentans VR4 (D2RIQ3), Acidaminococcus fermentans ATCC 25085 (D2RIQ3 and D2RL84)
brenda
Ma, Z.; Qin, X.; Zhong, X.; Liao, Y.; Su, Y.; Liu, X.; Liu, P.; Lu, J.; Zhou, S.
Flavine adenine dinucleotide inhibits pathological cardiac hypertrophy and fibrosis through activating short chain acyl-CoA dehydrogenase
Biochem. Pharmacol.
178
114100
2020
Rattus norvegicus (P15651), Rattus norvegicus Sprague-Dawley (P15651)
brenda