Information on EC 1.3.8.1 - short-chain acyl-CoA dehydrogenase and Organism(s) Homo sapiens

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The taxonomic range for the selected organisms is: Homo sapiens

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.3.8.1
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RECOMMENDED NAME
GeneOntology No.
short-chain acyl-CoA dehydrogenase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-aminobutanoate degradation V
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acetyl-CoA fermentation to butanoate II
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gallate degradation III (anaerobic)
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L-glutamate degradation V (via hydroxyglutarate)
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L-lysine fermentation to acetate and butanoate
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pyruvate fermentation to butanoate
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pyruvate fermentation to butanol I
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succinate fermentation to butanoate
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alanine metabolism
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butanoate fermentation
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glutamate and glutamine metabolism
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lipid metabolism
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Fatty acid degradation
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Valine, leucine and isoleucine degradation
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Butanoate metabolism
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Microbial metabolism in diverse environments
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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
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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
2-methylbutanoyl-CoA + acceptor
2-methyl-2-butenoyl-CoA + reduced acceptor
show the reaction diagram
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-
-
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r
butanoyl-CoA + acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
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r
butanoyl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
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
-
-
-
-
?
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 + oxidized acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
crotonyl-CoA + electron acceptor
butyryl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
crotonyl-CoA + reduced acceptor
butyryl-CoA + oxidized acceptor
show the reaction diagram
-
-
-
-
?
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
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-
-
-
r
hexanoyl-CoA + acceptor
hex-2-enoyl-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
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-
-
?
octanoyl-CoA + electron transfer flavoprotein
octenoyl-CoA + reduced acceptor
show the reaction diagram
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-
-
-
?
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
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-
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
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pentanoyl-CoA i.e. valeryl-CoA
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?
pentenoyl-CoA + oxidized electron transfer flavoprotein
valeryl-CoA + reduced electron transfer flavoprotein
show the reaction diagram
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-
-
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?
propionyl-CoA + electron transfer flavoprotein
2-propenoyl-CoA + reduced acceptor
show the reaction diagram
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-
-
?
propionyl-CoA + phenazine methosulfate
2-propenoyl-CoA + reduced acceptor
show the reaction diagram
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?
additional information
?
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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
butanoyl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
show the reaction diagram
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
show the reaction diagram
D4QEZ8
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-
-
?
pentanoyl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
show the reaction diagram
D4QEZ8
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?
additional information
?
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catalyzes the first step in the beta-oxidation cycle with substrate optima of 4 carbon chains
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(Methylenecyclopropyl)acetyl-CoA
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0.01 mM, 81% inhibition, 0.001 mM, 49% inhibition
1-azepan-1-yl-2-phenyl-2-(4-thioxo-1,4-dihydro-pyrazolo[3,4-d]pyrimidin-5-yl)-ethanone
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specific inhibitor of SCHAD, forms a covalent adduct with NAD+ by a catalytic suicide mechanism
iodoacetamide
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2 mM, 63% inhibition
isovaleryl-CoA dehydrogenase E254G
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inhibits wild-type SCAD
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N-ethylmaleimide
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2 mM, 41% inhibition, 0.2 mM, 23% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.019
2-methylbutanoyl-CoA
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32C, pH 7.0
0.0003 - 0.00075
Butanoyl-CoA
0.0129 - 0.124
butyryl-CoA
0.0041
electron transfer flavoprotein
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0.004 - 0.0339
Hexanoyl-CoA
0.0333
pentanoyl-CoA
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0.179
phenazine methosulfate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6
2-methylbutanoyl-CoA
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32C, pH 7.0
9.6
Butanoyl-CoA
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32C, pH 7.0
20.8
butyryl-CoA
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10 - 16.5
Hexanoyl-CoA
40.7
valeryl-CoA
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
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less than 50% of maximal activity above and below
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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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
PDB
SCOP
CATH
ORGANISM
UNIPROT
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41200
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4 * 41200, SDS-PAGE
44000
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SDS-PAGE
168000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
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tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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subunits of the SCAD enzyme are synthesised in the cytosol as precursor proteins that are then imported into the mitochondrial matrix
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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no loss of activity after 5 h below 37C in the presence of less than 3% glycerol
654618
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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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
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80C, phosphate buffer, pH 7.6, 20% glycerol
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by chromatography and fractionation, to ca. 95% homogeneity
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by gel filtration, to more than 95% purity
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recombinant SCAD
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli XL1 Blue
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expressed in Mus musculus
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expression in Escherichia coli
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expression in mouse liver
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expression of mutant R83C in wild-type astrocytes
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gene ACADS, DNA and amino acid sequence determination and analysis, genotyping
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gene ASCAD, expression analysis of wild-type and mutant R107C enzymes in A-172 cells and transfected Mus musculus GP+E86 cells, phenotypes, overview
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gene HADHSC, real-time quantitative PCR expression analysis in in INS832/13 beta-cells
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into Escherichia coli XL1 Blue
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into Escherichia coli XL1 Blue, mutant expressed from Escherichia coli K19
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SCAD DNA and amino acid sequence determination and analysis
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C1147T/G625A
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
C319G/G625A
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine and upper reaspiratory infections
C319T
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
C319T/G1095T
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
C488A/C988T
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine and reactive airway disease
C527A/T1164/G1165del/G625A
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
C867A
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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
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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
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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
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
G1153T/G625A
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
G209S
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mutant shows a temperature-dependent production of SCAD tetramers with reduced amounts compared to the wild type enzyme
G268A/1C147T/G625A
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
G268A/C1147T/G625A
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
G320A/G417C
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naturally occuring mutation, genotype, mutant shows highly increased acylglycines and organic acid levels in the urine and eczema
G625A
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
G682/A683del/C988T
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
L122V
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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
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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
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affects brain development and brain function in patients
R171W
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mutant shows a temperature-dependent production of SCAD tetramers with reduced amounts compared to the wild type enzyme
T455C/T443T
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naturally occuring mutation, genotype, mutant shows increased isobutyrylcarnitine levels in the urine, and pyelonephritisand emesis
T529C
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine
T529C/G625A
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naturally occuring mutation, genotype, mutant shows increased acylglycines and organic acid levels in the urine and atrial septal defect
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
additional information