Information on EC 1.3.8.1 - short-chain acyl-CoA dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.3.8.1
-
RECOMMENDED NAME
GeneOntology No.
short-chain acyl-CoA dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-aminobutanoate degradation V
-
-
acetyl-CoA fermentation to butanoate II
-
-
alanine metabolism
-
-
Biosynthesis of secondary metabolites
-
-
butanoate fermentation
-
-
Butanoate metabolism
-
-
Fatty acid degradation
-
-
gallate degradation III (anaerobic)
-
-
glutamate and glutamine metabolism
-
-
L-glutamate degradation V (via hydroxyglutarate)
-
-
L-lysine fermentation to acetate and butanoate
-
-
lipid metabolism
-
-
Metabolic pathways
-
-
pyruvate fermentation to butanoate
-
-
pyruvate fermentation to butanol I
-
-
succinate fermentation to butanoate
-
-
Valine, leucine and isoleucine degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
short-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 catalyses the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms. The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. The highest activity was reported with either butanoyl-CoA [2] or pentanoyl-CoA [4]. The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA [6]. cf. EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-88-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
type I strain ATCC 19171T and type II strain ATCC 51255
SwissProt
Manually annotated by BRENDA team
strain P262
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain KT2440
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3,3-difluorobutyryl)pantetheine + phenazine methosulfate + dichlorophenolindophenol
3-fluoro-2-butenoylpantetheine + HF
show the reaction diagram
-
-
-
?
(E)-2-butenoyl-CoA + reduced methylviologen
? + oxidized methylviologen
show the reaction diagram
-
-
-
-
?
(S)-2-methylbutyryl-CoA + phenazine methosulfate + dichloroindophenol
(S)-2-methyl-2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
6.0% of activity with butyryl-CoA
-
?
2-azabutyryl-CoA + ?
?
show the reaction diagram
-
substrate may be converted by intrinsic hydratase activity of the enzyme to 2-azaacetyl-CoA
-
-
?
2-butenoyl-CoA + reduced acceptor
butanoyl-CoA + acceptor
show the reaction diagram
-
reduction in vivo
-
-
r
2-butenoyl-CoA + reduced acceptor
butyryl-CoA + acceptor
show the reaction diagram
-
trans-addition of hydrogen
-
?
2-butenoyl-CoA + reduced electron transfer flavoprotein
butanoyl-CoA + electron transfer protein
show the reaction diagram
-
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
show the reaction diagram
-
enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro
-
r
2-methyl-3-hydroxybutyryl-CoA
2-methyl-acetoacetyl-CoA
show the reaction diagram
-
among the best substrates
-
-
?
2-methylbutanoyl-CoA + acceptor
2-methyl-2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
r
2-methylbutyryl-CoA + electron acceptor
2-methyl-2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
highest activity
-
-
?
2-methylpropionyl-CoA + phenazine methosulfate + dichloroindophenol
2-methylpropenoyl-CoA + reduced acceptor
show the reaction diagram
-
1.5% of activity with butyryl-CoA
-
?
2-pentenoyl-CoA + reduced electron transfer flavoprotein
pentanoyl-CoA + electron transfer protein
show the reaction diagram
-
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
show the reaction diagram
3-fluoropropionyl-CoA + phenazine methosulfate + dichlorophenolindophenol
2-propenoyl-CoA + HF
show the reaction diagram
-
-
-
?
3-hydroxybutyryl-CoA + acceptor
acetoacetyl-CoA + reduced acceptor
show the reaction diagram
4-methylpentanoyl-CoA + phenazine methosulfate + dichloroindophenol
4-methyl-2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
-
18.0% of activity with butyryl-CoA
-
?
acrolein + reduced methylviologen
? + oxidized methylviologen
show the reaction diagram
-
-
-
-
?
acryloyl-CoA + benzyl viologen
propanoyl-CoA + reduced benzyl viologen
show the reaction diagram
acryloyl-CoA + reduced methylviologen
propanoyl-CoA + oxidized methylviologen
show the reaction diagram
-
-
-
-
?
butanoyl-CoA + acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
butanoyl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
show the reaction diagram
butanoyl-CoA + FAD
2-butenoyl-CoA + FADH2
show the reaction diagram
butanoyl-CoA + FAD
but-2-enoyl-CoA + FADH2
show the reaction diagram
-
-
-
?
butanoyl-CoA + FAD
trans-2,3-dehydrobutanoyl-CoA + FADH2
show the reaction diagram
-
-
-
-
?
butanoyl-CoA + oxidized acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
r
butyryl-CoA + 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
butyryl-CoA + electron transfer flavoprotein
2-butenoyl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
?
butyryl-CoA + electron transfer flavoprotein
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
butyryl-CoA + electron-transferring flavoprotein
2-butenoyl-CoA + reduced electron-transferring flavoprotein
show the reaction diagram
-
-
-
-
?
butyryl-CoA + ferricenium
2-butenoyl-CoA + ferrocene
show the reaction diagram
-
-
-
-
?
butyryl-CoA + ferricytochrome c
butenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
r
butyryl-CoA + ferrocenium
2-butenoyl-CoA + ferrocene
show the reaction diagram
-
-
-
-
?
butyryl-CoA + O2
2-butenoyl-CoA + H2O2
show the reaction diagram
butyryl-CoA + oxidized acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
butyryl-CoA + pyocyanine + triphenyltetrazolium chloride
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
r
crotonyl-CoA + electron acceptor
butyryl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
crotonyl-CoA + electron transfer for flavoprotein
butyryl-CoA + ?
show the reaction diagram
-
-
-
?
crotonyl-CoA + O2 + 2 NADH + 2 H+
butanoyl-CoA + H2O2 + 2 NAD+
show the reaction diagram
crotonyl-CoA + reduced acceptor
butyryl-CoA + oxidized acceptor
show the reaction diagram
-
-
-
-
?
crotonyl-CoA + reduced ferredoxin
butanoyl-CoA + oxidized ferredoxin
show the reaction diagram
cyclobutanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-butenecarboxyl-CoA + reduced acceptor
show the reaction diagram
cycloheptanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-heptenecarboxyl-CoA + reduced acceptor
show the reaction diagram
-
3.2% of activity with butyryl-CoA
-
?
cyclohexanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-hexenecarboxyl-CoA + reduced acceptor
show the reaction diagram
-
6.7% of activity with butyryl-CoA
-
?
cyclopentanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-pentenecarboxyl-CoA + reduced acceptor
show the reaction diagram
ethyl vinyl ketone + reduced methylviologen
? + oxidized methylviologen
show the reaction diagram
-
-
-
-
?
heptanoyl-CoA + electron acceptor
2-heptenoyl-CoA + reduced acceptor
show the reaction diagram
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
r
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
hexanoyl-CoA + electron acceptor
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
hexanoyl-CoA + electron transfer flavoprotein
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
hexanoyl-CoA + FAD
hex-2-enoyl-CoA + FADH2
show the reaction diagram
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
N-acetyl-S-acryloyl-cysteamine + reduced methylviologen
? + oxidized methylviologen
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + electron acceptor
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
low activity
-
-
?
octanoyl-CoA + electron transfer flavoprotein
octenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
octanoyl-CoA + electron transfer protein
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
octanoyl-CoA + Meldola's Blue + iodonitrotetrazolium chloride
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
pentanoyl-CoA + 2,6-dichlorophenolindophenol + phenazine ethosulfate
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
pentanoyl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
pentanoyl-CoA + electron transfer flavoprotein
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
pentanoyl-CoA + FAD
pent-2-enoyl-CoA + FADH2
show the reaction diagram
-
-
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
pentenoyl-CoA + oxidized electron transfer flavoprotein
valeryl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
-
-
-
-
?
propionyl-CoA + 2,6-dichlorophenolindophenol
2-propenoyl-CoA + reduced acceptor
show the reaction diagram
propionyl-CoA + electron transfer flavoprotein
2-propenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
propionyl-CoA + phenazine methosulfate
2-propenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
reduced ferredoxin + NAD+ + H+
oxidized ferredoxin + NADH
show the reaction diagram
S-butyrylpantetheine + phenazine ethosulfate + dichloroindophenol
S-but-2-eneoylpantetheine + reduced acceptor
show the reaction diagram
-
51.0% of activity with butyryl-CoA
-
?
valeryl-CoA + electron acceptor
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-butenoyl-CoA + reduced acceptor
butanoyl-CoA + acceptor
show the reaction diagram
-
reduction in vivo
-
-
r
2-butenoyl-CoA + reduced electron transfer flavoprotein
butanoyl-CoA + electron transfer protein
show the reaction diagram
-
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
show the reaction diagram
-
enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro
-
r
2-pentenoyl-CoA + reduced electron transfer flavoprotein
pentanoyl-CoA + electron transfer protein
show the reaction diagram
-
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
show the reaction diagram
-
enzyme functions as C3-C6 enoyl-CoA reductase in vivo and catalyzes the oxidation of butyryl-CoA and related substrates in vitro
-
r
butanoyl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
show the reaction diagram
butanoyl-CoA + oxidized acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
r
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
show the reaction diagram
D4QEZ8
-
-
-
?
pentanoyl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
show the reaction diagram
D4QEZ8
-
-
-
?
additional information
?
-
-
catalyzes the first step in the beta-oxidation cycle with substrate optima of 4 carbon chains
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ferredoxin
butyryl-CoA dehydrogenase from Clostridium difficile belongs to the subfamily of bifurcating enzymes capable of coupling the exergonic reduction of crotonyl-CoA by NADH with the endergonic reduction of ferredoxin by NADH
-
ferricytochrome c
-
-
FMN
-
about 1.5 per mol of dimer
NAD+
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
riboflavin
-
enzyme-bound
additional information
-
flavoprotein, electron-transferring flavoprotein as redox partner
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
-
2 mol copper /mol FAD, cupric ion can be removed by dialysis against cyanide, copper is not involved in redox reaction
Cu2+
-
10-12 copper ions per enzyme molecule, enzyme-bound copper. The Cu2+ does not play a role in the primary reduction of the flavin-bound enzyme
Iron
-
less than 0.2 g-atom per mol protein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Methylenecyclopropyl)acetyl-CoA
1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-ethanone
-
specific inhibitor of SCHAD, forms a covalent adduct with NAD+ by a catalytic suicide mechanism
2-butenoyl-CoA
3-Chloro-3-butenoylpantetheine
-
-
3-Pentenoylpantetheine
4-chloromercuribenzoate
acetoacetyl-CoA
AgNO3
-
0.1 mM, complete inhibition
CoA-persulfide
-
90% inhibition after incubation with artificially high concentrations of the ligand CoA-persulfide
CuCl2
-
0.1 mM, complete inhibition
diethyl dicarbonate
-
1 mM, 83% residual activity
Hg2+
-
-
HgCl2
-
0.1 mM, complete inhibition
iodoacetamide
isovaleryl-CoA dehydrogenase E254G
-
inhibits wild-type SCAD
-
light
-
loss of 95% activity after anaerobic or aerobic photolysis
-
Methylmercury chloride
-
1 mM, 82% inhibition
Methylmercury iodide
-
0.1 mM, 58% inhibition
N-ethylmaleimide
p-hydroxymercuribenzoate
-
0.1 mM, 97% inhibition, 4 min half-time at 0.067 mM, enzyme is protected from inactivation by the prior addition of butyryl-CoA
palmitoyl-CoA
-
-
propionyl-CoA
-
-
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CN-
-
activates the enzyme in reaction with ferricytochrome c or ferricyanide as electron acceptors, but not with flavin D or FAd
additional information
level of operon-mRNA not affected by acetate concentration in the medium
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008
(E)-2-butenoyl-CoA
-
22C, pH 6.4
0.33
2,6-dichlorophenolindophenol
-
-
0.019
2-methylbutanoyl-CoA
-
32C, pH 7.0
0.161
2-methylpropionyl-CoA
-
-
0.097
4-methylpentanoyl-CoA
-
-
5.6
acrolein
-
22C, pH 6.4
0.00083
acrylyl-CoA
-
22C, pH 6.4
0.0003 - 0.01
Butanoyl-CoA
0.0006 - 0.1253
Butyryl-CoA
0.0025
crotonyl-CoA
pH 7.5, 37C; pH 7.5, temperature not specified in the publication
0.119
cyclobutanecarboxyl-CoA
-
-
0.198
cycloheptanecarboxyl-CoA
-
-
0.082
cyclohexanecarboxyl-CoA
-
-
0.095
cyclopentanecarboxyl-CoA
-
-
0.0041
electron transfer flavoprotein
-
-
0.77
ethyl vinyl ketone
-
22C, pH 6.4
0.083
ferricytochrome c
-
-
0.02547
heptanoyl-CoA
-
-
0.0017 - 0.285
Hexanoyl-CoA
0.035
N-acetyl-S-acryloyl-cysteamine
-
22C, pH 6.4
0.145
NADH
pH 7.5, 37C
0.0011 - 0.04231
Octanoyl-CoA
0.016 - 0.0333
pentanoyl-CoA
0.59
phenazine ethosulfate
-
phenazine ethosulfate as intermediate electron carrier
0.179 - 0.83
phenazine methosulfate
0.13 - 0.15
propionyl-CoA
0.002
reduced ferredoxin
pH 7.5, 37C
0.213
S-2-methylbutyryl-CoA
-
-
0.1238
valeryl-CoA
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6
2-methylbutanoyl-CoA
Homo sapiens
-
32C, pH 7.0
2 - 9.6
Butanoyl-CoA
0.293 - 33.3
Butyryl-CoA
19
crotonyl-CoA
Peptoclostridium difficile
Q18AQ1
pH 7.5, 37C; pH 7.5, temperature not specified in the publication
0.00567 - 0.25
heptanoyl-CoA
0.2992 - 16.5
Hexanoyl-CoA
3 - 6
NADH
Peptoclostridium difficile
Q18AQ1
pH 7.5, 37C
0.00183 - 0.1
Octanoyl-CoA
3 - 24.5
pentanoyl-CoA
0.03 - 0.0333
propionyl-CoA
37
reduced ferredoxin
Peptoclostridium difficile
Q18AQ1
pH 7.5, 37C
2.403 - 40.7
valeryl-CoA
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2800
Butanoyl-CoA
7600
crotonyl-CoA
Peptoclostridium difficile
Q18AQ1
pH 7.5, 37C; pH 7.5, temperature not specified in the publication
406
250
NADH
Peptoclostridium difficile
Q18AQ1
pH 7.5, 37C
8
18500
reduced ferredoxin
Peptoclostridium difficile
Q18AQ1
pH 7.5, 37C
265
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00036 - 0.0102
2-butenoyl-CoA
0.00012 - 0.01
acetoacetyl-CoA
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.003
-
enzyme activity in cell extracts
0.01
-
enzyme activity in mitochondria of riboflavin-deficient rats
0.013
-
enzyme activity in mitochondria of riboflavin-deficient rats
0.02
-
enzyme activity in mitochondria of riboflavin-deficient rats after 24 h starvation
0.025 - 0.034
-
enzyme activity in membrane fraction
0.0329
-
wild type enzyme
0.038
-
enzyme activity in mitochondria
0.04
-
enzyme activity in mitochondria of riboflavin-deficient rats after 48 h starvation
0.06
-
enzyme activity in crude extracts of cells grown on lactate
0.12 - 0.13
-
enzyme activity in soluble fraction
0.127
-
enzyme activity in mitochondria
0.13
-
with hexanoyl-CoA as substrate
0.19
-
enzyme activity in crude extracts
0.3
-
E368G/G247E double mutant enzyme, electron transfer protein as electron acceptor
0.47
-
with 0.21 mM butyryl-CoA as substrate at pH 8.0
0.48
-
partially purified enzyme mixture, substrate butyryl-CoA
0.76
-
activity in extracts of crotonate grown cells
0.77
-
-
0.86
-
with valeryl-CoA as substrate
0.871
-
activity in extracts of gallate-formate grown cells
1.2
-
enzyme activity in crude extracts
1.42
-
-
1.9
-
E368D mutant enzyme, electron transfer protein as electron acceptor
3.3
-
enzyme activity in crude extracts of cells harboring a plasmid with cloned gene
3.8
-
wild-type enzyme, electron transfer protein as electron acceptor
17.9
-
-
170
-
22C, pH 6.4
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 6.9
-
with electron transfer flavoprotein
7
-
assay at
7.1
-
-
7.6
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.9
-
30% resiudal activity
4.5 - 7
level of operon-mRNA not affected within this range
6 - 10
-
70% activity at pH 6, 48% activity at pH 10
6.5 - 8
-
42% activity at pH 6.5, 78% at pH 7.5 and 65% at pH 8.0
6.5 - 9
-
less than 50% of maximal activity above and below
7.5 - 9
-
57% activity at pH 7.6, 72% activity at pH 9
8.3
-
30% residual activity
additional information
-
pH-dependency of electron transfer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 38
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26 - 41
activities of SCAD constructs are entirely lower at 26C incubation temperature and slightly higher at 41C incubation temperature than those at 37C incubation temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
-
polyacrylamide slab gel
7.5
-
chromatofocusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
northern blot
Manually annotated by BRENDA team
-
low expression of ACADS during high expression of L-3-hydroxyacyl-CoA dehydrogenase short chain
Manually annotated by BRENDA team
-
an astrocyte cell line
Manually annotated by BRENDA team
additional information
SCAD activity levels in different tissues vary greatly, immunohistochemic analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
enzyme activity is at least partially membrane-associated
Manually annotated by BRENDA team
additional information
-
localized on GLUT4-containing vesicles via association with insulin-regulated aminopeptidase
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28400
-
gel filtration
41000
-
mature enzyme, SDS-PAGE
42770
sequence analysis, type I strain
42840
sequence analysis, type II strain
90000
-
gel filtration
120000 - 220000
150000
-
gel filtration
160000
162000
-
gel filtration
168000
-
gel filtration
169000
-
gel filtration
188000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 14200, SDS-PAGE
homotetramer
-
-
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging- or sitting-drop method, 120 mM potassium phosphate, pH 6.0, 60 mM Bis-Tris acetate, pH 6.0, 190 mM ammonium sulfate, 4.3% poly(ethylene glycol) 4500, resolution 2.5 A, space group P422, monomer consists of three domains: 2 alpha-helical domains at the N- and C-terminal regions and a beta-sheet in the middle, FAD is located between the beta-domain and the C-terminal domain of one subunit and the C-terminal domain of a neighboring subunit
-
crystals of SCAD complexed with acetoacetyl-CoA are grown by sitting drop vapor diffusion, 8.8 mg/ml SCAD in the presence of 1.2 molar equivalents of acetoacetyl-CoA in 85 mM Tris-acetate, pH 7.0 and 270 mM amonium sulfate are equilibrated against a solution containing 85 mM Tris-acetate, pH 7.0 and 3.78 M ammonium sulfate, crystals diffract to 2.25 A
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
no loss of activity after 5 h below 37C in the presence of less than 3% glycerol
654618
6
-
most stable
391260, 391266
7
-
unstable above
391266
additional information
-
enzyme is more stable at pH 8.0 than at pH 6.0
696519
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
15% loss of activity after 3 h, wild-type SCAD coexpressed with GroEL; approx. 50% loss of activity after 3 h, R147W mutant expressed without GroEL; approx. 50% loss of activity after 3 h, wild-type expressed without GroEL; approx. 85% loss of activity after 3 h, G185S mutant expressed without GroEL
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no inactivation by freezing/thawing
-
photoinactivation at 450 nm, loss of 95% activity after 45 min of anaerobic photolysis
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme is not oxygen-sensitive
-
696519
enzyme is oxygen stable and apparently uses oxygen as a cooxidant of NADH in the presence of air
725287
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, 30% ethylene glycol, 15 mM phosphate pH 8.0, 20% loss of activity within 1 year
-
-18C, 50% ethylene glycol, 6 months, 80% activity after reconstitution with FAD
-
-20C, 10 mM KH2PO4, pH 8.0, 0.2 M NaCl, 50% glycerol, at least 3 months
-
-20C, at least 1 month
-
-80C, phosphate buffer, pH 7.6, 20% glycerol
-
4C, 0.1 M potassium phosphate buffer, pH 7, 0.02% sodium azide, 96 h, CoA-free enzyme 75% activity, CoA-containing enzyme 100% activity
-
4C, in the presence of FAD and under anoxic conditions, 2-3 days, 50% loss of activity
-
short term: 4C, 0.1 M potassium phosphate buffer, pH 7, 0.02% sodium azide or 0.002% chlorhexidine, long term: frozen in ammonium sulfate
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by chromatography and fractionation, to ca. 95% homogeneity
-
by gel filtration, to more than 95% purity
-
by successive fractionations of anion-exchange chromatography, ammonium sulfate precipitation and gel filtration, to more than 99% homogeneity
-
DEAE cellulose, gel filtration, partially purified
-
enzyme exhibits a bright green color from a strong absorption band at 710 nm due to tightly bound CoA persulfide
-
preparation of apoprotein
-
preparation of CoA-persulfide free enzyme
-
pure enzyme has a characteristic green colour, CoA-persulfide may be the donor in a charge-transfer complex that is responsible for the green colour
-
Q-Sepharose column chromatography, hydroxyapatite column chromatography, Phenyl-Sepharose column chromatography, Superdex 200 gel filtration, and Mono Q column chromatography
-
recombinant bSCAD
-
recombinant SCAD
-
recombinant wild-type and E367Q mutant enzyme
-
wild-type enzyme purified, E368Q, E368G and E368L mutant enzyme, partially purified
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expressed in Escherichia coli
expressed in Escherichia coli
-
expressed in Escherichia coli XL1 Blue
-
expressed in Mus musculus
-
expression in Escherichia coli
expression in Escherichia coli, wild-type and Glu367Gln mutant enzyme
-
expression in mouse liver
-
expression of mutant R83C in wild-type astrocytes
-
expression of wild-type, E368G/G247E, E368D, E368Q and E368G mutant enzyme in Escherichia coli
-
gene ACADS, DNA and amino acid sequence determination and analysis, genotyping
-
gene ASCAD, expression analysis of wild-type and mutant R107C enzymes in A-172 cells and transfected Mus musculus GP+E86 cells, phenotypes, overview
-
gene HADHSC, real-time quantitative PCR expression analysis in in INS832/13 beta-cells
-
into Escherichia coli XL1 Blue
-
into Escherichia coli XL1 Blue, mutant expressed from Escherichia coli K19
-
into plasmid pRSET B and overexpressed in Escherichia coli C41(DE3)
-
SCAD DNA and amino acid sequence determination and analysis
-
SCAD DNA and amino acid sequence determination and analysis of wild-type and mutant enzymes, coexpression iin HEK-293 cells, expression of fluorescent-labeled enzyme mutants in U2-OS cells
SCAD DNA and amino acid sequence determination and analysis, the enzyme is encoded at 12q22-qter
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C1147T/G625A
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
C319G/G625A
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine and upper reaspiratory infections
C319T
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
C319T/G1095T
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
C488A/C988T
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine and reactive airway disease
C527A/T1164/G1165del/G625A
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
C867A
-
naturally occuring homozygote mutation, genotype, mutant shows increased isobutyrylcarnitine levels in the urine
E344G
site-directed mutagenesis, the SCAD mutant shows reduced activity compared to the wild-typ enzyme, but does not influence the wild-type SCAD activity when co-transfected in HEK-293 cells
E368G
-
is unable to form a charge-transfer complex with substrate/product, does not efficiently compete with the wild-type enzyme for the physiological electron acceptor
E368Q
-
inactivates the reductive and oxidative pathways
G108D
site-directed mutagenesis, the SCAD mutant shows reduced activity compared to the wild-typ enzyme, but does not influence the wild-type SCAD activity when co-transfected in HEK-293 cells
G1095T/G625A
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
G1153T/G625A
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
G209S
-
mutant shows a temperature-dependent production of SCAD tetramers with reduced amounts compared to the wild type enzyme
G268A/1C147T/G625A
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
G268A/C1147T/G625A
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
G320A/G417C
-
naturally occuring mutation, genotype, mutant shows highly increased acylglycines and organic acid levels in the urine and eczema
G625A
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
G682/A683del/C988T
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
L122V
-
affects brain development and brain function in patients
P55L
site-directed mutagenesis, the SCAD mutant shows reduced activity compared to the wild-typ enzyme, but does not influence the wild-type SCAD activity when co-transfected in HEK-293 cells
R107C
-
naturally occuring mutation, development of a cell model system, stably expressing either the SCAD wild-type protein or the misfolding SCAD variant protein, R107C, genotype C319T. The model system is used for investigation of SCAD with respect to expression, degree of misfolding, and enzymatic SCAD activity
R130C
-
affects brain development and brain function in patients
R171W
-
mutant shows a temperature-dependent production of SCAD tetramers with reduced amounts compared to the wild type enzyme
T455C/T443T
-
naturally occuring mutation, genotype, mutant shows increased isobutyrylcarnitine levels in the urine, and pyelonephritisand emesis
T529C
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
T529C/G625A
-
naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine and atrial septal defect
E367Q
-
mutant enzyme shows less than 0.03% of the activity seen in normal cloned enzyme, E367 is responsible for catalytic activity
E368D
-
mutant exhibits enzyme activity
E368G
-
inactive enzyme, E368 is responsible for catalytic activity
E368G/G247E
-
mutant exhibits enzyme activity
E368L
-
inactive enzyme, E368 is responsible for catalytic activity
E368Q
-
inactive enzyme, E368 is responsible for catalytic activity
E368R
-
inactive enzyme, E368 is responsible for catalytic activity
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution of holoenzyme after removal of FAD
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
synthesis
additional information
Show AA Sequence (3278 entries)
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