Information on EC 1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.1.1.35
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxyacyl-CoA dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(R)- and (S)-3-hydroxybutanoate biosynthesis (engineered)
-
-
2-methylpropene degradation
-
-
3-hydroxypropanoate/4-hydroxybutanate cycle
-
-
4-hydroxybenzoate biosynthesis V
-
-
adipate degradation
-
-
androstenedione degradation
-
-
Benzoate degradation
-
-
benzoyl-CoA degradation I (aerobic)
-
-
Biosynthesis of antibiotics
-
-
Biosynthesis of secondary metabolites
-
-
butanoate fermentation
-
-
Butanoate metabolism
-
-
Caprolactam degradation
-
-
Carbon fixation pathways in prokaryotes
-
-
cholesterol degradation to androstenedione I (cholesterol oxidase)
-
-
cholesterol degradation to androstenedione II (cholesterol dehydrogenase)
-
-
CO2 fixation in Crenarchaeota
-
-
crotonate fermentation (to acetate and cyclohexane carboxylate)
-
-
fatty acid beta-oxidation I
-
-
fatty acid beta-oxidation II (peroxisome)
-
-
fatty acid beta-oxidation VI (peroxisome)
-
-
Fatty acid degradation
-
-
Fatty acid elongation
-
-
fatty acid salvage
-
-
Geraniol degradation
-
-
glutaryl-CoA degradation
-
-
jasmonic acid biosynthesis
-
-
L-glutamate degradation V (via hydroxyglutarate)
-
-
lipid metabolism
-
-
Lysine degradation
-
-
Metabolic pathways
-
-
methyl ketone biosynthesis (engineered)
-
-
methyl tert-butyl ether degradation
-
-
Microbial metabolism in diverse environments
-
-
phenylacetat degradation (aerobic)
-
-
phenylacetate degradation I (aerobic)
-
-
Primary bile acid biosynthesis
-
-
pyruvate fermentation to butanoate
-
-
pyruvate fermentation to butanol I
-
-
pyruvate fermentation to butanol II (engineered)
-
-
pyruvate fermentation to hexanol (engineered)
-
-
Toluene degradation
-
-
toluene degradation to benzoyl-CoA (anaerobic)
-
-
tryptophan metabolism
-
-
Tryptophan metabolism
-
-
Valine, leucine and isoleucine degradation
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-3-hydroxyacyl-CoA:NAD+ oxidoreductase
Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and S-3-hydroxyacyl-hydrolipoate. Some enzymes act, more slowly, with NADP+. Broad specificity to acyl chain-length (cf. EC 1.1.1.211 [long-chain-3-hydroxyacyl-CoA dehydrogenase]).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-40-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain 1224-5/25, multifunctional beta-oxidation enzyme complex composed of 2 different 3-hydroyacyl-CoA dehydrogenases, 2 different 2-enoyl-CoA hydratases, thiolase, and epimerase activities
-
-
Manually annotated by BRENDA team
Euglena gracilis 1224-5/25
strain 1224-5/25, multifunctional beta-oxidation enzyme complex composed of 2 different 3-hydroyacyl-CoA dehydrogenases, 2 different 2-enoyl-CoA hydratases, thiolase, and epimerase activities
-
-
Manually annotated by BRENDA team
strain A0149, gene FUM13
-
-
Manually annotated by BRENDA team
strain A0149, gene FUM13
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain KT2442, gene fadB
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
-
enzyme-protein interaction analysis in different tissues and subcellular compartments, detailed overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(3S)-3-hydroxyadipyl-CoA + NAD+
3-oxoadipyl-CoA + NADH + H+
show the reaction diagram
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
show the reaction diagram
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
show the reaction diagram
(S)-3-hydroxybutyryl-CoA + NAD+
3-oxobutyryl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
?
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
?
(S)-3-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH
show the reaction diagram
(S)-3-hydroxydecanoyl-CoA + ?
3-oxodecanoyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
?
(S)-3-hydroxydecanoyl-CoA + NAD+
3-ketodecanoyl-CoA + NADH
show the reaction diagram
(S)-3-hydroxyhexanoyl-CoA + NAD+
3-ketohexanoyl-CoA + NADH
show the reaction diagram
(S)-3-hydroxyhexenoyl-CoA + NAD+
3-ketohexenoyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxylauryl-CoA + NAD+
3-ketolauryl-CoA + NADH
show the reaction diagram
-
-
-
r
1-propanol + NAD+
n-propanal + NADH
show the reaction diagram
-
multifunctional enzyme from brain
-
ir
17beta-estradiol + NAD+
estrone + NADH
show the reaction diagram
17beta-estradiol + NAD+
estrone + NADH + H+
show the reaction diagram
2-fluoro-3-hydroxy-4-octenoyl-CoA + NAD+
2-fluoro-3-oxo-4-octenoyl-CoA + NADH
show the reaction diagram
-
-
-
-
r
2-fluoro-3-hydroxyoctanoyl-CoA + NAD+
2-fluoro-3-oxooctanoyl-CoA + NADH
show the reaction diagram
-
-
-
-
r
2-propanol + NAD+
acetone + NADH
show the reaction diagram
-
multifunctional enzyme from brain
-
ir
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
3-hydroxy-2-methylacyl-CoA + NAD+
3-oxo-2-methylacyl-CoA + NADH
show the reaction diagram
-
preferred substrate of SCHAD, no activity towards 3-hydroxy-2-methylacyl-CoA by HAD
-
-
-
3-hydroxy-4-octenoyl-CoA + NAD+
3-oxo-4-octenoyl-CoA + NADH
show the reaction diagram
-
-
-
-
r
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
3-hydroxyoctanoyl-CoA + NAD+
3-oxooctanoyl-CoA + NADH
show the reaction diagram
-
-
-
-
r
3-ketohexadecanoyl-CoA + NADH
(S)-3-hydroxhexadecanoyl-CoA + NAD+
show the reaction diagram
3-ketooctanoyl-CoA + NADH
(S)-3-hydroxyoctanoyl-CoA + NAD+
show the reaction diagram
3-oxoacyl-CoA + NADH
3-hydroxyacyl-CoA + NAD+
show the reaction diagram
-
key enzyme involved in fatty acid oxidation
-
-
r
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
show the reaction diagram
3-oxohexadecanoyl-CoA + NADH + H+
(S)-3-hydroxhexadecanoyl-CoA + NAD+
show the reaction diagram
-
-
-
-
?
3-oxooctanoyl-CoA + NADH + H+
(S)-3-hydroxyoctanoyl-CoA + NAD+
show the reaction diagram
-
-
-
-
?
5alpha-androstane-3,17-diol + NAD+
5alpha-dihydrotestosterone + NADH
show the reaction diagram
5alpha-dihydrotestosterone + NADH
(3beta,5alpha,17beta)-androstane-3,17-diol + NAD+
show the reaction diagram
-
-
-
r
8-(acetoacetylthio)-6-ethyloctanoic acid + NADH
6-ethyl-8-[[(1S)-1-hydroxy-3-oxobutyl]thio]octanoic acid + NAD+
show the reaction diagram
-
-
-
r
8-(acetoacetylthio)-6-mercaptooctanoic acid + NADH
8-[[(1S)-1-hydroxy-3-oxobutyl]thio]-6-mercaptooctanoic acid + NAD+
show the reaction diagram
-
-
-
r
acetoacetyl-CoA + NADH
(S)-3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
acetoacetyl-CoA + NADH
3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
acetoacetyl-CoA + NADH + H+
3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
-
-
-
-
?
acetoacetyl-cysteamine-2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid amide + NADH
(S)-3-hydroxybutyryl-cysteamine-2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid amide + NAD+
show the reaction diagram
-
-
-
r
acetoacetyl-N-acetylcysteamine + NADH
(S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
show the reaction diagram
acetoacetyl-N-beta-alanylcysteamine + NADH
(S)-3-hydroxybutyryl-N-beta-alanylcysteamine + NAD+
show the reaction diagram
-
-
-
r
acetoacetyl-pantetheine + NADH
(S)-3-hydroxybutyryl-pantetheine
show the reaction diagram
acetoacetyl-pantetheine-4'-(2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid ester) + NADH
(S)-3-hydroxybutyryl-pantetheine-4'-(2,2,5,5-tetramethyl-1-oxy-3-pyrroline-3-carboxylic acid ester) + NAD+
show the reaction diagram
-
-
-
r
acetoacetyldecanoate + NADH
(S)-3-hydroxybutyryldecanoate + NAD+
show the reaction diagram
-
-
-
r
allopregnanolone + NAD+
5alpha-dihydroprogesterone + NADH
show the reaction diagram
androsterone + NAD+
androstanedione + NADH
show the reaction diagram
-
-
-
ir
tiglyl-CoA + NAD+
3-oxo-2-methylacyl-CoA + NADH
show the reaction diagram
-
activity of SCHAD
-
-
-
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(3S)-3-hydroxyadipyl-CoA + NAD+
3-oxoadipyl-CoA + NADH + H+
show the reaction diagram
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
show the reaction diagram
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
show the reaction diagram
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
17beta-estradiol + NAD+
estrone + NADH
show the reaction diagram
-
enzyme conatains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
17beta-estradiol + NAD+
estrone + NADH + H+
show the reaction diagram
-
inactivation
-
-
?
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
3-oxoacyl-CoA + NADH
3-hydroxyacyl-CoA + NAD+
show the reaction diagram
-
key enzyme involved in fatty acid oxidation
-
-
r
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
show the reaction diagram
5alpha-androstane-3,17-diol + NAD+
5alpha-dihydrotestosterone + NADH
show the reaction diagram
-
inactivation
-
-
?
allopregnanolone + NAD+
5alpha-dihydroprogesterone + NADH
show the reaction diagram
-
inactivation
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
enhances activity at 1 mM or 10 mM
Mg2+
enhances activity at 1 mM or 10 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
Co2+
1 mM, about 50% inhibition
EDTA
about 35% inhibition at 1 mM, about 25% inhibition at 10 mM
iodoacetamide
-
-
iodoacetic acid
-
-
K+
about 30% inhibition at 1 mM, about 20% inhibition at 10 mM
N-bromsuccinimide
-
-
N-ethylmaleimide
-
-
Ni2+
1 mM, about 60% inhibition
p-chloromercuribenzoate
-
-
p-Chloromercuriphenyl sulfonic acid
-
95% inhibition at 0.1 mM
RNAi
-
suppressed KCR activity results in a reduction of cuticular wax load and affects very-long-chain fatty acid composition of sphingolipids, seed triacylglycerols, and root glycerolipids
-
Zn2+
1 mM, about 60% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AMP-activated protein kinase
-
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.034
(3beta,5alpha,17beta)-androstane-3,17-diol
-
enzyme from brain
0.06 - 0.2
(S)-3-hydroxybutanoyl-CoA
0.000058 - 43.5
(S)-3-hydroxybutyryl-CoA
0.088
(S)-3-hydroxydecanoyl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxydecanoyl-CoA
0.0286 - 0.34
(S)-3-hydroxyhexanoyl-CoA
0.1
(S)-3-hydroxylauryl-CoA
-
-
0.0163 - 0.35
(S)-3-hydroxyoctanoyl-CoA
0.043
17beta-estradiol
-
enzyme from brain
65.6
3-acetoacetyl-CoA
pH 7.0, 30C
0.003 - 0.263
acetoacetyl-CoA
44.4
acetoacetyl-N-acetyl-cysteamine
-
-
10
acetoacetyl-N-acetylcysteamine
-
-
1.4
acetoacetyl-N-beta-alanylcysteamine
-
-
10
acetoacetyl-Nacetylcysteamine
-
-
0.08 - 1.19
acetoacetyl-pantetheine
0.045
androsterone
-
enzyme from brain
0.00009 - 29.5
NAD+
0.0009 - 50
NADH
11
NADP+
-
-
0.435
NADPH
-
-
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.093
(3beta,5alpha,17beta)-androstane-3,17-diol
Homo sapiens
-
enzyme from brain
15
(S)-3-hydroxybutanoyl-CoA
Metallosphaera sedula
-
pH 8.0, 70C
0.012 - 1420
(S)-3-hydroxybutyryl-CoA
0.011
17beta-estradiol
45
3-ketohexadecanoyl-CoA
Sus scrofa
-
-
24
3-ketohexdecanoyl-CoA
Homo sapiens
Q99714
enzyme from brain, pH 7.0
28 - 102
3-ketooctanoyl-CoA
0.019 - 1287
acetoacetyl-CoA
0.011
androsterone
Homo sapiens
-
enzyme from brain
0.004 - 1817
NAD+
0.189 - 510
NADH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
260
(S)-3-hydroxybutanoyl-CoA
Metallosphaera sedula
-
pH 8.0, 70C
7958
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.002
-
enzyme from brain, substrate 1-propanol
0.0121
-
enzyme from brain, substrate androsterone
0.0156
-
enzyme from brain, substrate 17beta-estradiol
0.033
-
enzyme activity in brain mitochondria, substrate acetoacetyl-CoA
0.087
-
enzyme from brain, substrate 5alpha-dihydrotestosterone
0.13
-
enzyme from brain, substrate dihydroandrosterone
0.41
-
enzyme activity in solubilized sediments of homogenized cells
0.48
-
enzyme activity in inner membrane of liver mitochondria, substrate acetoacetyl-CoA
0.5
85C, pH 7.0, highly enriched enzyme
0.75
-
72% activivty is bound to the matrix surface of the inner mitochondria membrane, binding is inhibited by increasing ionic strength and pH
0.78
-
enzyme activity in kidney mitochondria, substrate acetoacetyl-CoA
1.5
-
enzyme activity in heart mitochondria, substrate acetoacetyl-CoA
1.67
-
enzyme activity in liver mitochondria, substrate acetoacetyl-CoA
2.3
-
enzyme activity in liver mitoplasts, substrate acetoacetyl-CoA
2.77
-
trans-3-decenoyl-CoA as a substrate
3 - 8
-
pH 8.0, 65C, native enzyme, autotrophically- or heterotrophically-grown cell
3.4
-
enzyme activity in matrix of liver mitochondria, substrate acetoacetyl-CoA
4.17
-
(S)-3-hydroxydecanoyl-CoA as substrate, activity of L-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-I
4.22
-
(S)-3-hydroxybutyryl-CoA as substrate, activity of L-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-I
12.6
-
peroxisomal enzyme
17.35
enzyme from brain
23.4
-
L-3-hydroxyacyl-CoA dehydrogenase activity of the trifunctional beta-oxidation protein
40
-
purified enzyme
176
-
-
220
-
-
452
-
purified recombinant His-tagged wild-type enzyme
511
-
recombinant enzyme
565
-
mitochondrial enzyme
1200
-
His-tagged recombinant enzyme
additional information
-
the N-terminal His-tag does notinfluence enzyme activity
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
mitochondrial enzyme, reduction of acetoacetyl-CoA
5
-
phosphate buffer
5.5 - 6.5
conversion of acetoacetyl-CoA to beta-hydroxybutyryl-CoA decreases above pH 6.5
6
-
reduction of acetoacetyl-CoA
6 - 7
-
reduction of acetoacetyl-CoA
6.2
-
peroxisomal enzyme, reduction of acetoacetyl-CoA
6.5 - 7
-
enzyme from brain, reduction of acetoacetyl-CoA
7
-
SCAD I and SCHAD II, pH optimum the reduction
7.2
assay at; assay at
8.5
-
SCAD I, pH optimum for oxidation
9
-
oxidation of (S)-3-hydroxybutyryl-CoA
9.3
-
SCHAD II, pH optimum for oxidation
9.5 - 10
-
enzyme from brain, oxidation of 17beta-estradiol
9.8
-
peroxisomal enzyme, oxidation of (S)-3-hydroxybutyryl-CoA
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 11
pH 9.0: about 45% of maximal activity, pH 11.0: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at; assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.2
calculated, native protein
6.1
calculated, recombinant protein
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
activated, high level expression
Manually annotated by BRENDA team
-
KCR1 and KCR2 transcripts
Manually annotated by BRENDA team
-
KCR1 and KCR2 transcripts
Manually annotated by BRENDA team
-
KCR1 and KCR2 transcripts
Manually annotated by BRENDA team
-
in oocytes from diabetic mice, activity of Hadh2 is significantly reduced
Manually annotated by BRENDA team
-
high level expression in malignant prostatic epithelial cells
Manually annotated by BRENDA team
-
KCR1 and KCR2 transcripts
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
-
liver enzyme
50300
-
gel filtration
66000
-
gel filtration
76000
-
gel filtration
108000
enzyme from brain, gel filtration
260000
-
gel filtration
270000
-
gel filtration
365000
-
trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3, gel filtration
460000
-
native enzyme complex, sucrose density gradient centrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 77000, peroxisomal enzyme, SDS-PAGE
tetramer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
50 mM N(2-acetamido)-2-iminodiacetic acid, pH 6.5, polyethylene glycol 4000, 5 mM NAD+ hanging drop, crystals within 3 to 5 days at 18C, enzyme structure is compromised of two domains, a NAD+-binding domain and a helical C-terminal domain
-
50% saturation with ammonium sulfate solution, 0.1 M potassium phosphate, pH 6.8, 1 mM EDTA, 2 mM beta-mercaptoethanol, 4C, crystals appear after 2 days
-
dialysis against 40% saturated ammonium sulfate containing 100 mM phosphate, 2 mM beta-mercaptoethanol, 1 mM EDTA, pH 6.9, 7.5 or 8.2, vapor diffusion crystallization, crystals are obtained in the ammonium sulfate saturation range of 41% to 48%
-
polyethylene glycol, pH 8, orthorhombic crystals, 2.7 A resolution, crystallisation at pH 5 leads to trigonal space group
-
two dimers of the enzyme in the asymmetric unit of an orthorombic cell, two coenzyme binding sites per dimer
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 120 mM potassium phosphate, pH 7.0, several months without loss of activity
-
-76C, 0.2 M potassium phosphate, pH 6.6, 25% glycerol, 10 mM mercaptoethanol, several months, no loss in activity
-
-80C, purified recombinant His-tagged wild-type and mutant enzymes, stable for at least 3 months
-
4C, 90% ammonium sulfate, at least 6 monts, no loss of activity
-
4C, purified recombinant His-tagged wild-type enzyme, 1 week, no significant loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
60C for 10 min, phosphocellulose, Sephacryl S200
-
ammonium sulfate, 50C for 20 min, Zn(OH)2-gel
-
ammonium sulfate, first CM-cellulose, gelfiltration, second and third CM-cellulose
-
ammonium sulfate, Sephadex G-150, hydroxyapatite, NAD-Sepharose 4B
-
beta-oxidation enzyme complex 67fold to homogeneity by ammonium sulfate precipitation, density gradient centrifugation, and ion-exchange chromatography
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calcium phosphate gel, ammonium sulfate, CM-Sephadex, Blue Dextran-Sepharose 4B, calcium phosphate gel-cellulose, Blue Dextran-Sepharose 4B, mitochondrial enzyme; phosphocellulose, ammonium sulfate, CM-cellulose, ammonium sulfate, peroxisomal enzyme
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overexpressed in Escherichia coli, hydroxylapatite
overexpressed in Escherichia coli, phosphocellulose
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
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recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
C-terminal hexameric histidine tag, expressed in Escherichia coli
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expressed in Escherichia coli
expressed in yeast ybr159DELTA mutant
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expression in Escherichia coli
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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gene Bn-kcr1, DNA library screening, DNA and amino acid sequence determination and analysis, expression analysis, expression in Saccharomyces cerevisiae BY4742 mutant strains, functional complementation study, overview; gene Bn-kcr2, DNA library screening, DNA and amino acid sequence determination and analysis, expression analysis, expression in Saccharomyces cerevisiae BY4742 mutant strains, functional complementation study, overview
gene FUM13, expression of His-tagged enzyme in Escherichia coli, expression in and functional complementation of Saccharomyces cerevisiae 3-ketosphinganine reductase mutant strain tsc10, overview
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gene hadh, quantitative real-time PCR expression analysis
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gene HADHSC, located on chromosome 4q22-26
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overexpression in Escherichia coli
overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) as soluble N-terminally His-tagged enzymes
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recombinantly expressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D279E
-
naturally occuring polymorphism probably involved in development of type 2 diabetes
H152Q
-
naturally occuring polymorphism probably involved in development of type 2 diabetes
P86L
-
naturally occuring polymorphism probably involved in development of type 2 diabetes
N208A
-
site-directed mutagenesis, the substrate binding of the mutant enzyme is affected
S137C
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
S137T
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
after denaturation with 2-3 M urea or guanidinium-HCl, 94% activity can be recovered by dialyzing the enzyme at 4C against 100 mM sodium diphosphate, pH 7.3, 10 mM 2-mercaptoethanol
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
pharmacology
-
the short-chain 3-hydroxyacyl-CoA dehydrogenase is a target for intervention in case of Alzheimer's disease and Parkinson's disease
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