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Information on EC 1.3.8.1 - short-chain acyl-CoA dehydrogenase and Organism(s) Homo sapiens
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1.3.8.1 short-chain acyl-CoA dehydrogenaseIUBMB Comments
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 or pentanoyl-CoA . The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA . 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.
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Word Map
- 1.3.8.1
-
ethylmalonic
-
medium-chain
- dehydrogenases
-
beta-oxidation
-
inborn
- aciduria
- carnitine
- acylcarnitines
-
scadd
- butyrylcarnitine
-
methylsuccinic
- isobutyryl-coa
- isovaleryl-coa
- phenylketonuria
- vlcad
-
very-long-chain
-
isovaleric
- crotonyl-coa
- octanoyl-coas
-
megasphaera
- 3-methylcrotonyl-coa
- elsdenii
- synthesis
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
acads, short-chain acyl-coa dehydrogenase, short chain acyl-coa dehydrogenase, short-chain acyl-coenzyme a dehydrogenase, short-chain acyl coa dehydrogenase, acyl-coa dehydrogenase short chain, bscad, butyryl-coa dehydrogenase complex, enoyl-coenzyme a reductase, short-chain acylcoa dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BCAD
-
-
-
-
dehydrogenase, butyryl coenzyme A
-
-
-
-
SCAD
short-chain acyl-CoA dehydrogenase
SCAD
-
-
-
-
SCAD
-
-
short-chain acyl-CoA dehydrogenase
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -
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
9027-88-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-methylbutanoyl-CoA + acceptor
2-methyl-2-butenoyl-CoA + reduced acceptor
-
-
-
-
r
butyryl-CoA + electron transfer flavoprotein
2-butenoyl-CoA + reduced electron transfer flavoprotein
-
-
-
-
?
butyryl-CoA + electron transfer flavoprotein
crotonyl-CoA + reduced electron transfer flavoprotein
-
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
-
-
-
?
octanoyl-CoA + electron transfer flavoprotein
octenoyl-CoA + reduced acceptor
-
-
-
-
?
pentanoyl-CoA + electron transfer flavoprotein
2-pentenoyl-CoA + reduced acceptor
-
-
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
-
pentanoyl-CoA i.e. valeryl-CoA
-
?
pentenoyl-CoA + oxidized electron transfer flavoprotein
valeryl-CoA + reduced electron transfer flavoprotein
-
-
-
-
?
propionyl-CoA + electron transfer flavoprotein
2-propenoyl-CoA + reduced acceptor
-
-
-
?
propionyl-CoA + phenazine methosulfate
2-propenoyl-CoA + reduced acceptor
-
-
-
?
additional information
?
-
-
catalyzes the first step in the beta-oxidation cycle with substrate optima of 4 carbon chains
-
-
?
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
-
?
hexanoyl-CoA + electron transfer flavoprotein
2-hexenoyl-CoA + reduced acceptor
-
-
-
?
hexanoyl-CoA + electron transfer flavoprotein
2-hexenoyl-CoA + reduced acceptor
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
catalyzes the first step in the beta-oxidation cycle with substrate optima of 4 carbon chains
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(methylenecyclopropyl)acetyl-CoA
-
0.01 mM, 81% inhibition, 0.001 mM, 49% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26 - 41
activities of SCAD constructs are entirely lower at 26°C incubation temperature and slightly higher at 41°C incubation temperature than those at 37°C incubation temperature
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
SCAD activity levels in different tissues vary greatly, immunohistochemic analysis, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
subunits of the SCAD enzyme are synthesised in the cytosol as precursor proteins that are then imported into the mitochondrial matrix
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
expression of the R107C mutant variant SCAD protein gives rise to inactive misfolded protein species, eliciting a mild toxic response manifested though a decreased proliferation rate and oxidative stress, as shown by an increased demand for the mitochondrial antioxidant SOD2, occurance of increased markers of apoptotic activity in the mutant protein expressing cells. 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, overview
malfunction
-
patients with mutated beta-oxidation enzyme short-chain 3-hydroxyacyl-CoA dehydrogenase show hyperinsulinemia associated with non-ketotic hypoglycemia, analysis of the mechanism underlying HADHSC-mediated regulation of insulin secretion, overview. Enhanced glucose-stimulated insulin secretion induced by HADHSC knockdown is independent of changes in cytosolic Ca2+ and also occurs in the presence of fatty acids. The pan transaminase inhibitor amino-oxyacetate reverses HADHSC knockdown-mediated increases in glucose-stimulated insulin secretion. Oxidation of palmitate and octanoate is not reduced in HADHSC knockdown cells. L-3-Hydroxybutyryl-carnitine and L-3-hydroxyglutarate, which accumulate in blood and urine, respectively, of HADHSC-deficient patients, do not change insulin secretion. Transamination reaction(s) and the formation of short-chain acylcarnitines and CoAs may be implicated in the mechanism whereby HADHSC deficiency results in enhanced insulin secretion and hyperinsulinemia
malfunction
-
SCAD deficiency causes a defect in the beta-oxidation of short-chain fatty acids of four to eight carbons in length. The majority of individuals with short-chain acyl-CoA dehydrogenase deficiency have normal growth and development. Two variants in the ACADS gene, 625G-A and 511C-T, are commonly found in the general population, that are associated with ethylmalonic aciduria and some decreased enzyme activity
metabolism
mutations in the gene encodine acyl-CoA dehydrogenase, ACAD, cause alterations in SCAD activity, overview
metabolism
-
SCAD functions in mitochondria and is involved in the beta-oxidation of fatty acyl-CoA compounds in chains of 4-6 carbons.The mitochondrial pathway of fatty acid beta-oxidation is an alternative source of energy, especially during stress or fasting
physiological function
-
SCAD catalyzes the dehydrogenation of butyryl-CoA during the first step of the short-chain fatty acid beta-oxidation spiral
physiological function
SCAD is a mitochondrial enzyme involved in the beta-oxidation of fatty acids and mediates the metabolic transition from acyl-CoA with four or six carbon chains to 2-enoyl-CoA in the first step of the beta-oxidation spiral. Genetic defect of SCAD cause clinical symptoms such as progressive psychomotor retardation, muscle hypotonia, and myopathy
additional information
-
patients with short-chain acyl-CoA dehydrogenase deficiency, a rare disorder of fatty acid oxidation, may show an increased risk of thyroid and other autoimmune diseases. The pathologic phenotype can include pernicious anaemia, vitiligo, autoimmune thyroiditis and lichen scleroatrophicus, overview
additional information
-
SCAD misfolding leads to production of reactive oxygen species, which in turn leads to fission and a grain-like structure of the mitochondrial reticulum, indicating a toxic response elicited by misfolded R83C SCAD proteins, detailed overview
additional information
-
short-chain acyl-CoA dehydrogenase deficiency, SCADD, is an autosomal recessive inborn error of mitochondrial fatty acid oxidation due to mutations in the SCAD protein. SCADD is biochemically characterized by increased C4-carnitine in plasma and ethylmalonic acid in urine, phenotype, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). IVD_HUMAN
426
0
46651
Swiss-Prot
Mitochondrion (Reliability: 2)
ACADS_HUMAN
412
0
44297
Swiss-Prot
Mitochondrion (Reliability: 1)
A0A0A0MT83_HUMAN
423
0
46319
TrEMBL
Mitochondrion (Reliability: 1)
A0A2L0RI88_HUMAN
426
0
46639
TrEMBL
Mitochondrion (Reliability: 2)
A0A2L0RI93_HUMAN
426
0
46679
TrEMBL
Mitochondrion (Reliability: 2)
A0A2L0RI76_HUMAN
426
0
46665
TrEMBL
Mitochondrion (Reliability: 2)
A0A0S2Z4K7_HUMAN
393
0
42724
TrEMBL
Mitochondrion (Reliability: 1)
A0A384MR53_HUMAN
423
0
46236
TrEMBL
Mitochondrion (Reliability: 1)
A0A2L0RIE3_HUMAN
426
0
46602
TrEMBL
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
subunits of the SCAD enzyme are synthesised in the cytosol as precursor proteins that are then imported into the mitochondrial matrix
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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
G185S
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
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
R147W
R171W
-
mutant shows a temperature-dependent production of SCAD tetramers with reduced amounts compared to the wild type enzyme
R83C
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
additional information
G185S
-
58% of wild-type activity at 41°C after expression in COS-7 cells, mutation may confer susceptibility to accumulation of ethylmalonic acid in affected individuals
R147W
-
45% and 13% of wild-type activity at 37°Cand 41°C, respectively, after expression in COS-7 cells, mutation may confer susceptibility to accumulation of ethylmalonic acid in affected individuals
R147W
-
exhibits almost identical physical and redox properties to wild-type but only half of the specific activity and substrate activation shifts observed in wild-type enzyme
R83C
-
unable to form tetramers, soluble mutant enzyme is not detected at steady-state
R83C
-
a naturally occuring mutation, c.319C>T, of SCAD involved in SCAD deficiency, SCADD
additional information
-
coupled gene mutations G625A and C511T impair C4-C6 fatty acid metabolism and variably causes neonatal/infantile hypotonia with developmental delays
additional information
-
knockdown of HADHSC expression by RNA interference in INS832/13 beta-cells using short hairpin RNA and short interference RNA
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
no loss of activity after 5 h below 37°C in the presence of less than 3% glycerol
654618
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
45
-
approx. 50% loss of activity after 3 h, R147W mutant expressed without GroEL
45
-
approx. 85% loss of activity after 3 h, G185S mutant expressed without GroEL
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
medicine
-
newborn screening assays for short-chain acyl-CoA dehydrogenase deficiency are based on the detection of elevated butyrylcarnitine (C4) levels
medicine
-
short-chain-acyl-CoA-dehydrogenase deficiency is an inborn error of mitochondrial fatty acid metabolism caused by rare mutations as well as common susceptibility variations in the SCAD gene
medicine
-
short-chain acyl-coenzyme A dehydrogenase deficiency is attributed to alterations in the SCAD gene
additional information
-
common variant SCAD enzymes and their potential contribution to clinical disease in humans
additional information
-
development of a novel surface plasmon resonance assay to measure substrate binding
additional information
-
overall high degree of thermodynamic modulation of wild-type SCAD, substrate binding appears to make a larger contribution than does product to thermodynamic modulation, substrate redox activation leading to a large enzyme midpoint potential shift
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
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
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
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
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
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
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
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
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
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
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
Jethva, R.; Bennett, M.J.; Vockley, J.
Short-chain acyl-coenzyme A dehydrogenase deficiency
Mol. Genet. Metab.
95
195-200
2008
Homo sapiens
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
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)
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
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
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
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
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
EXTERNAL LINKS (specific for EC-Number 1.3.8.1)
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Release 2023.1 (January 2023)
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