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
1.3.8.1
-
RECOMMENDED NAME
GeneOntology No.
short-chain acyl-CoA dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
mechanism
-
a short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
mechanism
-
a short-chain acyl-CoA + electron-transfer flavoprotein = a short-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
show the reaction diagram
mechanism for stereospecific catalysis
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
4-aminobutyrate degradation V
-
acetyl-CoA fermentation to butyrate II
-
Biosynthesis of secondary metabolites
-
Butanoate metabolism
-
Fatty acid degradation
-
gallate degradation III (anaerobic)
-
glutamate degradation V (via hydroxyglutarate)
-
lysine fermentation to acetate and butyrate
-
Metabolic pathways
-
pyruvate fermentation to butanoate
-
pyruvate fermentation to butanol I
-
succinate fermentation to butyrate
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
17beta-hydroxysteroid dehydrogenase type 10
-
-
2-methyl-3-hydroxybutyryl-CoA dehydrogenase
-
-
3-hydroxy-2-methylbutyryl-CoA dehydrogenase
-
-
3-hydroxyacyl CoA reductase
-
-
ambiguous
-
acyl-CoA dehydrogenase short chain
-
-
BCAD
-
-
-
-
bcd2
Clostridium difficile
Q18AQ1
-
butyryl CoA dehydrogenase
-
-
butyryl coenzyme A dehydrogenase
-
-
ambiguous
-
butyryl coenzyme A dehydrogenase
-
-
butyryl-CoA dehydrogenase
-
-
ambiguous
-
butyryl-CoA dehydrogenase
-
ambiguous
butyryl-CoA dehydrogenase
D4QEZ8
-
butyryl-CoA dehydrogenase complex
Clostridium difficile
Q18AQ1
-
butyryl-CoA dehydrogenase/Etf complex
-
-
CD1054
Clostridium difficile
Q18AQ1
gene name
dehydrogenase, butyryl coenzyme A
-
-
-
-
EC 1.3.2.1
-
-
formerly
-
enoyl-coenzyme A reductase
-
-
ambiguous
-
ethylene reductase
-
-
ambiguous
-
HADHSC
-
-
MHBD
-
-
SCAD
-
-
-
-
SCAD
D4QEZ8
-
short chain 3-hydroxyacyl-CoA dehydrogenase
-
-
short chain acyl-CoA dehydrogenase
-
-
short-chain 3-hydroxyacyl-CoA dehydrogenase
-
-
short-chain acyl CoA dehydrogenase
-
-
ambiguous
-
short-chain acyl-CoA dehydrogenase
D4QEZ8
-
short-chain acyl-CoA dehydrogenase
-
-
short-chain acyl-coenzyme A dehydrogenase
-
-
ambiguous
-
short-chain acyl-coenzyme A dehydrogenase
-
ambiguous
short-chain acyl-coenzyme A dehydrogenase
-
ambiguous
short-chain acylCoA dehydrogenase
-
-
type II 3-hydroxyacyl-CoA dehydrogenase
-
-
unsaturated acyl coenzyme A reductase
-
-
ambiguous
-
CAS REGISTRY NUMBER
COMMENTARY
9027-88-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
type I strain ATCC 19171T and type II strain ATCC 51255
SwissProt
Manually annotated by BRENDA team
Clostridium acetobutylicum P262
strain P262
-
-
Manually annotated by BRENDA team
Clostridium difficile
-
UniProt
Manually annotated by BRENDA team
gene ACADS
-
-
Manually annotated by BRENDA team
gram-negative anaerobe, formerly Peptostreptococcus elsdenii
-
-
Manually annotated by BRENDA team
BALB/cJ mice
-
-
Manually annotated by BRENDA team
strain KT2440
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
-
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
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
metabolism
D4QEZ8
mutations in the gene encodine acyl-CoA dehydrogenase, ACAD, cause alterations in SCAD activity, overview
physiological function
-
Clostridium homopropionicum using the acryloyl-CoA pathway with low growth yield obtains its specific competitive advantage compared to Propionibacterium freudenreichii not through higher substrate affinity or metabolic shift toward enhanced acetate-plus-hydrogen formation but through faster specific substrate turnover
physiological function
D4QEZ8
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
physiological function
-
SCAD catalyzes the dehydrogenation of butyryl-CoA during the first step of the short-chain fatty acid beta-oxidation spiral
metabolism
Clostridium difficile
-, Q18AQ1
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; the genes necessary for butyrate formation from the genome of Clostridium difficile are expressed in Escherichia coli. The individual genes are assembled in a single plasmid vector into an artificial operon , which allows functional coexpression of the required genes and confers butyrate-forming capability to the host
additional information
-
short-chain acyl-CoA dehydrogenase-deficient mice, SCAD-/- mice, have increased brown adipose tissue mass as well as modest cardiac hypertrophy. Uncoupling protein-1 is reduced by 70% in brown adipose tissue, not due to a change in mitochondrial number, nor to decreased signal transduction through protein kinase A, which is known to be a major regulator of uncoupling protein-1 expression, phenotype, overview. Reduced brown adipose tissue function is not the major factor causing cold sensitivity in acyl-CoA dehydrogenase knockout strains, but other mechanisms such as shivering capacity, cardiac function, and reduced hepatic glycogen stores are involved
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
-
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
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
butyryl-CoA + acceptor
show the reaction diagram
-
trans-addition of hydrogen
-
?
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-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
-
-
-
-
-
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
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
-
-
-
-
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
-
-
-
-
r
butanoyl-CoA + acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
r
butanoyl-CoA + acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
P15651
-
-
-
r
butanoyl-CoA + acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
r
butanoyl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
butanoyl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
butanoyl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
show the reaction diagram
D4QEZ8
-
-
-
?
butanoyl-CoA + FAD
but-2-enoyl-CoA + FADH2
show the reaction diagram
D4QEZ8
-
-
-
?
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
Clostridium acetobutylicum, Clostridium acetobutylicum P262
-
-
-
?
butyryl-CoA + electron acceptor
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 acceptor
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 acceptor
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 acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
r
butyryl-CoA + electron acceptor
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 acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
r
butyryl-CoA + electron acceptor
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 acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptors phenazine methosulfate or electron transfer flavoprotein
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptors phenazine methosulfate or electron transfer flavoprotein
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptors phenazine methosulfate or electron transfer flavoprotein
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptors phenazine methosulfate or phenazine ethosulfate
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptors phenazine methosulfate or phenazine ethosulfate
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
no activity towards dicarboxylic-CoAs
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
enzyme may also have an intrinsic crotonase activity
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor iodonitrotetrazolium chloride
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor iodonitrotetrazolium chloride
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
terminal electron acceptor iodonitrotetrazolium chloride
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptor phenazine methosulfate
-
?
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptor phenazine methosulfate
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptor phenazine methosulfate
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptor phenazine methosulfate
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptor phenazine methosulfate
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptor phenazine methosulfate
-
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptor phenazine methosulfate
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
-
intermediate electron acceptor phenazine methosulfate
-
-
butyryl-CoA + electron acceptor
2-butenoyl-CoA + reduced acceptor
show the reaction diagram
Clostridium acetobutylicum P262
-
terminal electron acceptor 2,6-dichlorophenol-indophenol
-
-
?
butyryl-CoA + electron transfer flavoprotein
crotonyl-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-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 + 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
Clostridium difficile
-, Q18AQ1
-
-
-
?
crotonyl-CoA + reduced acceptor
butyryl-CoA + oxidized acceptor
show the reaction diagram
-
-
-
-
?
cyclobutanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-butenecarboxyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
-
cyclobutanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-butenecarboxyl-CoA + reduced acceptor
show the reaction diagram
-
1.0% of activity with butyryl-CoA
-
?
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
-
-
-
-
-
cyclopentanecarboxyl-CoA + phenazine ethosulfate + dichloroindophenol
cyclo-2-pentenecarboxyl-CoA + reduced acceptor
show the reaction diagram
-
2.1% of activity with butyryl-CoA
-
?
ethyl vinyl ketone + reduced methylviologen
? + oxidized methylviologen
show the reaction diagram
-
-
-
-
?
heptanoyl-CoA + electron acceptor
2-heptenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
-
heptanoyl-CoA + electron acceptor
2-heptenoyl-CoA + reduced acceptor
show the reaction diagram
-
low activity
-
-
?
hexanoyl-CoA + acceptor
hex-2-enoyl-CoA + reduced acceptor
show the reaction diagram
D4QEZ8
-
-
-
?
hexanoyl-CoA + acceptor
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
r
hexanoyl-CoA + electron acceptor
2-hexenoyl-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 + electron transfer flavoprotein
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
D4QEZ8
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
-
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
13% of butyryl-CoA activity
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
4.2% of activity with butyryl-coA
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
52% of activity with butyryl-CoA
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
40% of activity with butyryl-CoA
-
-
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
-
-
-
-
-
octanoyl-CoA + Meldola's Blue + iodonitrotetrazolium chloride
2-octenoyl-CoA + reduced acceptor
show the reaction diagram
-
14.4% of activity with butyryl-CoA
-
?
pentanoyl-CoA + 2,6-dichlorophenolindophenol + phenazine ethosulfate
2-pentenoyl-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 + 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
D4QEZ8
-
-
-
?
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
D4QEZ8
-
-
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
-
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
-
45% of activity with butyryl-CoA, 2,6-dichlorophenolindophenol as final electron acceptor
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
-
pentanoyl-CoA i.e. valeryl-CoA
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
-
pentanoyl-CoA i.e. valeryl-CoA
-
?
pentanoyl-CoA + phenazine methosulfate
2-pentenoyl-CoA + reduced acceptor
show the reaction diagram
-
pentanoyl-CoA i.e. valeryl-CoA
-
?
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 + 2,6-dichlorophenolindophenol
2-propenoyl-CoA + reduced acceptor
show the reaction diagram
-
30% of activity with butyryl-CoA
-
?
propionyl-CoA + 2,6-dichlorophenolindophenol
2-propenoyl-CoA + reduced acceptor
show the reaction diagram
Clostridium acetobutylicum, Clostridium acetobutylicum P262
-
20% of activity with butyryl-CoA
-
?
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
-
-
-
?
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
-
-
-
-
?
hexanoyl-CoA + phenazine methosulfate + dichloroindophenol
2-hexenoyl-CoA + reduced acceptor
show the reaction diagram
-
acceptor Meldola's Blue and iodonitrotetrazolium chloride
-
?
additional information
?
-
-
acts on a wide spectrum of substrates, including steroids, cholic acids, and fatty acids, with a preference for short chain methyl-branched acyl-CoAs
-
-
-
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
?
-
-
catalyzes the first step in the beta-oxidation cycle with substrate optima of 4 carbon chains
-
-
-
additional information
?
-
-
no activity with octanoyl-CoA and acetyl-CoA
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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 + acceptor
but-2-enoyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
?
butanoyl-CoA + acceptor
but-2-enoyl-CoA + reduced acceptor
show the reaction diagram
D4QEZ8
-
-
-
?
butanoyl-CoA + oxidized acceptor
crotonyl-CoA + reduced acceptor
show the reaction diagram
-
-
-
-
r
pentanoyl-CoA + acceptor
pent-2-enoyl-CoA + reduced acceptor
show the reaction diagram
D4QEZ8
-
-
-
?
hexanoyl-CoA + acceptor
hex-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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
1 mol per mol of subunit
FAD
-
1 mol per mol of subunit
FAD
-
1 mol per mol of subunit; tightly bound
FAD
-
1 mol per mol of subunit; FAD can be removed by dialysis at pH 6 against 100 mM potassium phosphate buffer containing 2 M KBr
FAD
-
1 mol per mol of subunit
FAD
-
about 5 or 6 FAD molecules per enzyme molecule
FAD
-
enzyme-bound, flavin D
FAD
-
one per subunit
FAD
Clostridium difficile
-, Q18AQ1
in the absence of ferredoxin, a remarkable stimulation of crotonyl-CoA reduction by FAD is observed
Ferredoxin
Clostridium difficile
-, Q18AQ1
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
-
-
NADH
Clostridium difficile
-, Q18AQ1
-
riboflavin
-
enzyme-bound
FMN
-
about 1.5 per mol of dimer
additional information
-
flavoprotein, electron-transferring flavoprotein as redox partner
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(Methylenecyclopropyl)acetyl-CoA
-
0.01 mM, 81% inhibition, 0.001 mM, 49% inhibition
(Methylenecyclopropyl)acetyl-CoA
-
0.0025 mM, 50% inhibition after 2.2 min, preincubation with 1 molar substrate/enzyme equivalent of butyryl-CoA increases half-life to 38 min
(Methylenecyclopropyl)acetyl-CoA
-
0.0129 mM and 0.0172 mM, strong inhibition of enzyme activity in enzyme mixture
(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
-
competitive product inhibition
2-butenoyl-CoA
-
competitive product inhibition
3-Chloro-3-butenoylpantetheine
-
-
3-Pentenoylpantetheine
-
0.31 mM, complete loss of activity after 40 s
3-Pentenoylpantetheine
-
0.62 mM, rapid irreversible inactivation
4-chloromercuribenzoate
-
0.1 mM, 40% inhibition
4-chloromercuribenzoate
-
inhibition is reversible by glutathione
acetoacetyl-CoA
-
0.5 mM, 60% inhibition, apo-enzyme reconstituted with FAD
acetoacetyl-CoA
-
-
acetoacetyl-CoA
-
-
acetoacetyl-CoA
P15651
-
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
HgCl2
-
0.1 mM, complete inhibition
iodoacetamide
-
2 mM, 63% inhibition
iodoacetamide
-
1 mM, 38% residual activity
isovaleryl-CoA dehydrogenase E254G
-
inhibits wild-type SCAD
-
light
-
loss of 95% activity after anaerobic or aerobic photolysis
-
Methylmercury chloride
-
1 mM, 82% inhibition
N-ethylmaleimide
-
2 mM, 41% inhibition, 0.2 mM, 23% 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
-
-
Methylmercury iodide
-
0.1 mM, 58% inhibition
additional information
-
not inactivated by N-ethylmaleimide and iodoacetic acid
-
additional information
-
-
-
additional information
-
CoA persulfide could serve as a regulatory ligand, enzyme would be activated when a threshold quantity of substrate is present that displaces enzyme bound CoA persulfide
-
additional information
-
no inhibition by CN-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
Q65Y10
level of operon-mRNA not affected by acetate concentration in the medium
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
Butanoyl-CoA
-
32C, pH 7.0
0.00045
-
Butanoyl-CoA
-
32C, pH 7.0, R147W mutant
0.00075
-
Butanoyl-CoA
-
32C, pH 7.0, G185S mutant
0.0006
-
Butyryl-CoA
-
wild-type enzyme
0.0006
-
Butyryl-CoA
-
-
0.0015
-
Butyryl-CoA
-
E368D mutant enzyme
0.002
-
Butyryl-CoA
-
E368G/G247E double mutant enzyme
0.002
-
Butyryl-CoA
-
-
0.0024
-
Butyryl-CoA
-
partially purified enzyme, enzyme mixture
0.0027
-
Butyryl-CoA
-
-
0.003
-
Butyryl-CoA
-
-
0.005
-
Butyryl-CoA
-
recombinant enzyme
0.006
-
Butyryl-CoA
-
-
0.009
-
Butyryl-CoA
-
-
0.01
-
Butyryl-CoA
Clostridium difficile
-, Q18AQ1
pH 7.5, temperature not specified in the publication
0.0107
-
Butyryl-CoA
-
-
0.0112
-
Butyryl-CoA
-
-
0.0129
-
Butyryl-CoA
-
-
0.014
-
Butyryl-CoA
-
-
0.014
-
Butyryl-CoA
-
native enzyme
0.015
-
Butyryl-CoA
-
-
0.017
-
Butyryl-CoA
-
electron transfer protein as acceptor
0.02
-
Butyryl-CoA
-
phenazine methyl sulfate as acceptor
0.055
-
Butyryl-CoA
-
wild-type
0.065
-
Butyryl-CoA
-
R147W mutant
0.124
-
Butyryl-CoA
-
G185S mutant
0.1253
-
Butyryl-CoA
-
-
0.0025
-
crotonyl-CoA
Clostridium difficile
-, Q18AQ1
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
-
Hexanoyl-CoA
-
E368G/G247E double mutant enzyme
0.0038
-
Hexanoyl-CoA
-
wild-type enzyme
0.004
-
Hexanoyl-CoA
-
32C, pH 7.0
0.005
-
Hexanoyl-CoA
-
E368D mutant enzyme
0.012
-
Hexanoyl-CoA
-
-
0.02
-
Hexanoyl-CoA
-
-
0.0339
-
Hexanoyl-CoA
-
-
0.034
-
Hexanoyl-CoA
-
-
0.053
-
Hexanoyl-CoA
-
-
0.09303
-
Hexanoyl-CoA
-
-
0.285
-
Hexanoyl-CoA
-
-
0.035
-
N-acetyl-S-acryloyl-cysteamine
-
22C, pH 6.4
0.0011
-
Octanoyl-CoA
-
E368G/G247E double mutant enzyme
0.005
-
Octanoyl-CoA
-
E368D mutant enzyme
0.0081
-
Octanoyl-CoA
-
wild-type enzyme
0.032
-
Octanoyl-CoA
-
-
0.04231
-
Octanoyl-CoA
-
-
0.016
-
Pentanoyl-CoA
-
-
0.0329
-
Pentanoyl-CoA
-
-
0.0333
-
Pentanoyl-CoA
-
-
0.59
-
phenazine ethosulfate
-
phenazine ethosulfate as intermediate electron carrier
0.179
-
phenazine methosulfate
-
-
0.27
-
phenazine methosulfate
-
-
0.8
-
phenazine methosulfate
-
-
0.83
-
phenazine methosulfate
-
phenazine methosulfate as intermediate electron carrier
0.13
0.15
propionyl-CoA
-
-
0.13
0.15
propionyl-CoA
-
-
0.213
-
S-2-methylbutyryl-CoA
-
-
0.1238
-
Valeryl-CoA
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
6
-
2-Methylbutanoyl-CoA
-
32C, pH 7.0
9.6
-
Butanoyl-CoA
-
32C, pH 7.0
0.293
-
Butyryl-CoA
-
at pH 5.5
0.5
-
Butyryl-CoA
-
native enzyme, O2 as electron acceptor
0.533
-
Butyryl-CoA
-
recombinant enzyme, O2 as electron acceptor
0.5883
-
Butyryl-CoA
-
at pH 6.0
0.7267
-
Butyryl-CoA
-
at pH 8.0
0.73
-
Butyryl-CoA
-
at pH 6.5
0.967
-
Butyryl-CoA
-
at pH 7.0; at pH 7.5
1.743
-
Butyryl-CoA
-
-
2
8
Butyryl-CoA
Clostridium difficile
-, Q18AQ1
pH 7.5, temperature not specified in the publication
2.5
-
Butyryl-CoA
-
-
3.33
-
Butyryl-CoA
-
-
4.5
-
Butyryl-CoA
-
electron transfer protein as acceptor
5
-
Butyryl-CoA
-
exchange of alpha and beta hydrogens
8.43
-
Butyryl-CoA
-
phenazine ethosulfate as intermediate electron carrier
9.17
-
Butyryl-CoA
-
phenazine methyl sulfate as acceptor
20.7
-
Butyryl-CoA
-
-
20.8
-
Butyryl-CoA
-
-
20.8
-
Butyryl-CoA
-
phenazine methosulfate as intermediate electron carrier
33.3
-
Butyryl-CoA
-
based on an estimated MW of 150000 Da
19
-
crotonyl-CoA
Clostridium difficile
-, Q18AQ1
pH 7.5, temperature not specified in the publication
0.00567
-
Heptanoyl-CoA
-
-
0.25
-
Heptanoyl-CoA
-
-
0.2992
-
Hexanoyl-CoA
-
-
1.35
-
Hexanoyl-CoA
-
-
10
-
Hexanoyl-CoA
-
32C, pH 7.0
16.5
-
Hexanoyl-CoA
-
-
0.00183
-
Octanoyl-CoA
-
-
0.1
-
Octanoyl-CoA
-
-
3
-
Pentanoyl-CoA
-
C-2 proton/deuteron exchange
3.3
-
Pentanoyl-CoA
-
-
24.5
-
Pentanoyl-CoA
-
-
0.03
-
propionyl-CoA
-
-
0.0333
-
propionyl-CoA
-
-
2.403
-
Valeryl-CoA
-
-
40.7
-
Valeryl-CoA
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2800
-
Butyryl-CoA
Clostridium difficile
-, Q18AQ1
pH 7.5, temperature not specified in the publication
8156
7600
-
crotonyl-CoA
Clostridium difficile
-, Q18AQ1
pH 7.5, temperature not specified in the publication
8822
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00036
-
2-butenoyl-CoA
-
-
0.0102
-
2-butenoyl-CoA
-
-
0.00012
-
acetoacetyl-CoA
-
apo-enzyme reconstituted with FAD
0.01
-
acetoacetyl-CoA
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
5.9
-
-
-
7.4
-
-
-
17.9
-
-
-
170
-
-
22C, pH 6.4
additional information
-
-
0.2-0.3 mmol/min/micromol enzyme
additional information
-
-
0.2 mmol/min/micromol enzyme bound flavin
additional information
-
-
0.017 micromol/min/unit of citrate synthase, riboflavin deficient rats, activity in liver mitochondria; 0.157 micromol/min/unit of citrate synthase, activity in liver mitochondria; 0.250 micromol/min/unit of citrate synthase, clofibrate-fed rats, activity in liver mitochondria
additional information
-
-
DELTA D600 = 12.2/min/mg protein
additional information
-
-
0.1-0.4 mM/min/micromol of FAD, enzyme activity in crude extracts and activity of purified cloned enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.9
-
-
and 6.4
6.4
-
-
and 5.9
6.8
6.9
-
with electron transfer flavoprotein
7
-
-
in cell extracts
7
-
-
-
7
-
-
assay at
7
-
D4QEZ8
assay at
7.1
-
-
-
7.5
-
Clostridium difficile
-, Q18AQ1
assay at
7.6
-
-
-
8
-
-
little decline in activity until pH 6.0
8
-
-
assay at
8
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.9
-
-
30% resiudal activity
4.5
7
Q65Y10
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
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
38
-
assay at
37
-
D4QEZ8
assay at
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
26
41
D4QEZ8
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
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.9
-
-
polyacrylamide slab gel
7.5
-
-
chromatofocusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
expressed in different regions
Manually annotated by BRENDA team
-
levels of SCHAD/HADII are significantly reduced in the ventral midbrain of a Parkinsons disease mouse model
Manually annotated by BRENDA team
-
wild type enzyme expression at protein level is only detected in brain
Manually annotated by BRENDA team
-
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
D4QEZ8
SCAD activity levels in different tissues vary greatly, immunohistochemic analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
enzyme activity is at least partially membrane-associated
Manually annotated by BRENDA team
-
subunits of the SCAD enzyme are synthesised in the cytosol as precursor proteins that are then imported into the mitochondrial matrix
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28400
-
-
gel filtration
41000
-
-
mature enzyme, SDS-PAGE
42770
-
Q65Y10
sequence analysis, type I strain
42840
-
Q65Y10
sequence analysis, type II strain
44000
-
-
SDS-PAGE
44000
-
-
precursor protein, SDS-PAGE
90000
-
-
gel filtration
110000
-
Clostridium difficile
-, Q18AQ1
-
120000
220000
-
analytical ultracentrifugation
120000
220000
-
gel filtration
150000
-
-
gel filtration
160000
-
-
gel filtration
160000
-
-
gel filtration
162000
-
-
gel filtration
168000
-
-
gel filtration
169000
-
-
gel filtration
188000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 14200, SDS-PAGE
homotetramer
-
-
tetramer
-
4 * 42188, mature enzyme, calculated from nucleotide sequence
tetramer
-
4 * 41200, SDS-PAGE
tetramer
-
4 * 43000, SDS-PAGE
tetramer
-
4 * 40300, SDS-PAGE
tetramer
-
4 * 41000, SDS-PAGE
tetramer
-
4 * 39000, SDS-PAGE
tetramer
-
4 * 36500, SDS-PAGE
tetramer
-
4 * 38500, SDS-PAGE, 4 * 40529, amino acid sequence analysis, 4 * 40488, MALDI TOF mass spectroscopy
tetramer
-
wild type enzyme
tetramer
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
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
proteolytic modification
-
enzyme is most probably synthesized as 41000 Da precursor that is transported into the mitochondrion coupled with proteolytic removal of a 4500 Da peptide extension
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
P15651
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
no loss of activity after 5 h below 37C in the presence of less than 3% glycerol
6
-
-
most stable
7
-
-
unstable above
additional information
-
-
enzyme is more stable at pH 8.0 than at pH 6.0
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
LITERATURE
photoinactivation at 450 nm, loss of 95% activity after 45 min of anaerobic photolysis
-
no inactivation by freezing/thawing
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme is not oxygen-sensitive
-
696519
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-18C, 30% ethylene glycol, 15 mM phosphate pH 8.0, 20% loss of activity within 1 year
-
4C, in the presence of FAD and under anoxic conditions, 2-3 days, 50% loss of activity
-
-80C, phosphate buffer, pH 7.6, 20% glycerol
-
-18C, 50% ethylene glycol, 6 months, 80% activity after reconstitution with FAD
-
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
-
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
-
-20C, 10 mM KH2PO4, pH 8.0, 0.2 M NaCl, 50% glycerol, at least 3 months
-
-20C, at least 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme exhibits a bright green color from a strong absorption band at 710 nm due to tightly bound CoA persulfide
-
DEAE cellulose, gel filtration, partially purified
-
Q-Sepharose column chromatography, hydroxyapatite column chromatography, Phenyl-Sepharose column chromatography, Superdex 200 gel filtration, and Mono Q column chromatography
-
by chromatography and fractionation, to ca. 95% homogeneity
-
by gel filtration, to more than 95% purity
-
recombinant SCAD
-
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
-
recombinant bSCAD
-
recombinant wild-type and E367Q mutant enzyme
-
by successive fractionations of anion-exchange chromatography, ammonium sulfate precipitation and gel filtration, to more than 99% homogeneity
-
wild-type enzyme purified, E368Q, E368G and E368L mutant enzyme, partially purified
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expressed in Escherichia coli
Clostridium difficile
-, Q18AQ1
expressed in Escherichia coli
-
expressed in Escherichia coli XL1 Blue
-
expressed in Mus musculus
-
expression in Escherichia coli
-
expression in mouse liver
-
expression of mutant R83C in wild-type astrocytes
-
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
-
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
D4QEZ8
SCAD DNA and amino acid sequence determination and analysis, the enzyme is encoded at 12q22-qter
-
expression in Escherichia coli
-
expression in Escherichia coli, wild-type and Glu367Gln mutant enzyme
-
into plasmid pRSET B and overexpressed in Escherichia coli C41(DE3)
-
expression of wild-type, E368G/G247E, E368D, E368Q and E368G mutant enzyme in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
D4QEZ8
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
D4QEZ8
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
-
80% of wild-type kcat with butanoyl-CoA
G185S
-
58% of wild-type activity at 41C after expression in COS-7 cells, mutation may confer susceptibility to accumulation of ethylmalonic acid in affected individuals
G185S
-
impairments of both its kinetic and electron transfer properties
G185S
-
the mutant is not detected at protein level but shows high mRNA levels
G185S
-
625G>A polymorphism
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
D4QEZ8
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
R147W
-
135% of wild-type kcat with butanoyl-CoA
R147W
-
45% and 13% of wild-type activity at 37Cand 41C, 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
R147W
-
511C>T polymorphism
R171W
-
mutant shows a temperature-dependent production of SCAD tetramers with reduced amounts compared to the wild type enzyme
R83C
-
unable to form tetramers, soluble mutant enzyme is not detected at steady-state
R83C
-
the mutant enzyme does not form tetramers and is inactive
R83C
-
a naturally occuring mutation, c.319C>T, of SCAD involved in SCAD deficiency, SCADD
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
-
disruption of the scdA gene results in 7.5fold reduction in butyryl-CoA dehydrogenase activity
L122V
-
affects brain development and brain function in patients
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
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
reconstitution of holoenzyme after removal of FAD
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
important in brain development and aging, SCHAD deficiency is an inherited defect in mitochondrial fatty acid oxidation, reported cases of SCHAD deficiency are actually due to a deficiency of HAD, abnormal levels may contribute to the pathogenesis of some neural disorders, potential target for intervention in Alzheimer's disease, Parkinson's disease, and an X-linked mental retardation
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
additional information
Q65Y10
type I strain has the same clustered genes with the same arrangement as type II strain, deduced amino acid sequences of these enzymes do not greatly differ between the two strains, and even between Butyrivibrio fibrisolvens and clostridia. Amino acid identity appears to be higher within the same type than between types I and II, clustered genes are cotranscribed, and constitutively transcribed without being affected significantly by culture conditions
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
-
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
additional information
-
development of a novel surface plasmon resonance assay to measure substrate binding