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Information on EC 1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase and Organism(s) Cupriavidus necator and UniProt Accession Q0KEG0
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1.1.1.35 3-hydroxyacyl-CoA dehydrogenaseIUBMB Comments
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]).
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Word Map
- 1.1.1.35
- citrate
- acyl-coas
- peroxisomal
-
thiolase
- carnitine
-
trifunctional
-
phosphofructokinase
- hexokinase
-
endurance
-
vastus
- lateralis
- acetoacetyl-coa
-
medium-chain
- soleus
- hypoglycemia
-
extensor
- lchad
- acylcarnitines
- hyperinsulinism
-
2-enoyl-coa
-
fast-twitch
-
plantaris
-
2,4-dienoyl-coa
-
schulz
- crotonase
-
hypoketotic
-
4.1.3.7
-
glyoxysomes
-
hellp
- 3-oxoacyl-coa
-
hydroxyacyl-coas
- trans-2-enoyl-coa
- gluteus
- medicine
- biofuel production
- diagnostics
- pharmacology
- synthesis
The taxonomic range for the selected organisms is: Cupriavidus necator
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
3-hydroxyacyl-coa dehydrogenase, l-3-hydroxyacyl-coa dehydrogenase, beta-hydroxyacyl coa dehydrogenase, hadhsc, 3-hydroxyacyl-coenzyme a dehydrogenase, short-chain 3-hydroxyacyl-coa dehydrogenase, short-chain l-3-hydroxyacyl-coa dehydrogenase, 3-ketoacyl-coa reductase, beta-ketoacyl-coa reductase, 3-hydroxyacyl coenzyme a dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(S)-stereospecific 3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase
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1-specific DPN-linked beta-hydroxybutyric dehydrogenase
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-
-
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3-hydroxyacetyl-coenzyme A dehydrogenase
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-
-
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3-hydroxyacyl coenzyme A dehydrogenase
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-
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3-hydroxyisobutyryl-CoA dehydrogenase
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-
-
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3-keto reductase
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-
-
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3-L-hydroxyacyl-CoA dehydrogenase
-
-
-
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3-L-hydroxybutyryl-CoA dehydrogenase
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-
-
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3beta-hydroxyacyl coenzyme A dehydrogenase
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-
-
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beta hydroxyacyl dehydrogenase
-
-
-
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beta-hydroxy acid dehydrogenase
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-
-
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beta-hydroxyacyl CoA dehydrogenase
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-
-
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beta-hydroxyacyl-coenzyme A synthetase
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-
-
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beta-hydroxybutyrylcoenzyme A dehydrogenase
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-
-
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beta-keto-reductase
-
-
-
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beta-ketoacyl-CoA reductase
-
-
-
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betahydroxyacylcoenzyme A dehydrogenase
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-
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endoplasmic reticulum-associated amyloid beta-peptide binding protein
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-
-
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HCDH
-
-
-
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L-3-hydroxyacyl CoA dehydrogenase
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-
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L-3-hydroxyacylcoenzyme A dehydrogenase
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-
-
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PaaH1
Scully protein
-
-
-
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type II HADH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Benzoate degradation, Biosynthesis of secondary metabolites, Butanoate metabolism, Caprolactam degradation, Carbon fixation pathways in prokaryotes, Fatty acid degradation, Fatty acid elongation, Geraniol degradation, Lysine degradation, Microbial metabolism in diverse environments, Toluene degradation, Tryptophan metabolism, Valine, leucine and isoleucine degradation
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
9028-40-4
-
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
(S)-3-hydroxybutanoyl-CoA + NADP+
acetoacetyl-CoA + NADPH + H+
relative activity of FadB' measured with NADP+ is less than 10% in comparison to the activity measured with NAD+
-
-
?
3-acetoacyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
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highest activity
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-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
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-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
enzyme FadB' converts (S)-3-hydroxybutyryl-CoA to acetoacetyl-CoA, while no conversion of (R)-3-hydroxybutyryl-CoA is detected
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-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
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-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
substrates binding structure analysis, overview. The acetoacetyl-CoA substrate is positioned within the deep cleft between the N-terminal domain and C-terminal domain. The acetoacetyl moiety is positioned near the conserved catalytic residues Ser119, His140, and Asn190
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-
r
additional information
?
-
the N-terminal part of FadB' comprises an NAD+ binding site and is responsible for 3-hydroxyacyl-CoA dehydrogenase activity converting (S)-3-hydroxybutyryl-CoA to acetoacetyl-CoA. FadB' is strictly stereospecific to (S)-3-hydroxybutyryl-CoA and to prefers NAD+. NADP(H) is utilized at a rate of less than 10% in comparison to activity with NAD(H)
-
-
?
additional information
?
-
-
the activity of enzymes PaaH1 and Had with NADPH is as low as 2.2% and 1.2%, respectively, of the respective activity with NADH
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-
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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
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
the enzyme prefers NAD+. NADP(H) is utilized at a rate of less than 10% in comparison to activity with NAD(H)
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NAD+
the NAD+ cofactor is bound to the N-terminal Rossmann fold, the NAD+-binding pocket is made up of 5 loops, enzyme binding structure analysis, overview
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetyl-CoA
inhibits the enzyme by 50% at 0.1 mM, further increase of inhibitor concentration reduces the activity of FadB' drastically
CoA
inhibits the enzyme by 20% at 0.1 mM, further increase of inhibitor concentration reduces the activity of FadB' drastically
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.076
acetoacetyl-CoA
pH 6.5, 30°C, recombinant enzyme in presence of 0.1 mM acetyl-CoA
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.5
purified recombinant enzyme, pH 6.5, 30°C, substrate (S)-3-hydroxybutanoyl-CoA with NADP+
16.5
purified recombinant enzyme, pH 6.5, 30°C, substrate (S)-3-hydroxybutanoyl-CoA with NAD+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
maximal activity at pH 6.0-7.0, 65% and 75% activity at pH 5.0 and pH 8.0, respectively, and 46% of the maximal activity at pH 10.0, and 26% of maximal activity at pH 4.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
two (S)-3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratases, H16_A0461/FadB' and H16_A1526/FadB1, are involved in the FA degradation in Ralstonia eutropha H16. FadB' and FadB1 possess an enoyl-CoA hydratase activity, catalyzing hydrogenation of the unsaturated enoyl coenzyme A (CoA), and a 3-hydroxyacyl-CoA dehydrogenase activity, i.e. oxidation of the hydroxyl group into a keto group using one NAD+ molecule
metabolism
the enzyme is involved in fatty acid degradation metabolism
metabolism
the enzyme catalyzes the second step in the biosynthesis of n-butanol from acetyl-CoA by the reduction of acetoacetyl-CoA to 3-hydroxybutyryl-CoA
additional information
additional information
FadB' is an enzyme with two catalytic domains exhibiting a single monomeric structure and possessing a molecular weight of 86 kDa. The C-terminal part of the enzyme harbors enoyl-CoA hydratase activity, EC 4.2.1.17, and is able to convert trans-crotonyl-CoA to 3-hydroxybutyryl-CoA. The N-terminal part of FadB' comprises an NAD+ binding site and is responsible for 3-hydroxyacyl-CoA dehydrogenase activity converting (S)-3-hydroxybutyryl-CoA to acetoacetyl-CoA
additional information
conserved catalytic residues are Ser119, His140, and Asn190
additional information
-
conserved catalytic residues are Ser119, His140, and Asn190
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
1 * 86000, recombinant His-tagged enzme, SDS-PAGE, 1 * 85900, about, sequence calculation
additional information
FadB' is a polypeptide comprising a N-terminal 3HCDH_N-domain, responsible for NAD+ binding, and a C-terminal enoyl-CoA hydratase domain, an with inverted domain order
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme in apoform, as selenomethionine-labeled enzyme, and in complex with substrates acetoacetyl-CoA and NAD+, hanging drop vapour diffusion method, mixing of 50 mg/ml wild-type protein or selenomethionine-labeled enzyme in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with reservoir solution containing 2 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.5, and 0.2 M sodium chloride, 22°C, 7 days, X-ray diffraction structure determination and analysis at 2.42-2.7 A resolution, molecular replacement using the crystal structure of the apo-form of RePaaH1, and structure modeling
purified recombinant wild-type and selenomethionine-labeled enzymes, hanging drop vapour diffusion method, mixing of 30 mg/ml wild-type protein or 25 mg/ml selenomethionine-labeled enzyme in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with reservoir solution containing 1.4 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.0, and 0.2 M sodium chloride, 22°C, 7 days, X-ray diffraction structure determination and analysis at 2.6 A resolution, single-wavelength anomalous dispersion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K56A
site-directed mutagenesis, the mutant shows about twofold increased activity compared to the wild-type enzyme
N190A
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
R52A
site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Q Sepharose column chromatography, HiTrap phenyl column chromatography and Superdex 200 gel filtration
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recombinant C-terminally His6-tagged wild-type or selenomethionine-labeled enzymes from Escherichia coli strain B834 by nickel affinity chromatography and gel filtration
recombinant C-terminally His6-tagged wild-type or selenomethionine-labeled enzymes from Escherichia coli strain B834 by nickel affinity chromatography and gel filtration
recombinant C-terminally His6-tagged wild-type or selenomethionine-labeled enzymes from Escherichia coli strain B834 by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, genetic organization, sequence comparisons and phylogenetic tree of 3-hydroxyacyl-CoA dehydrogenases, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene paaH1, recombinant expression of C-terminally His6-tagged wild-type or selenomethionine-labeled enzymes in Escherichia coli strain B834
gene paaH1, recombinant expression of C-terminally His6-tagged wild-type or selenomethionine-labeled enzymes in Escherichia coli strain B834
gene paaH1, recombinant expression of C-terminally His6-tagged wild-type or selenomethionine-labeled enzymes in Escherichia coli strain B834
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
3-hydroxybutyryl-CoA dehydrogenase is an enzyme involved in the synthesis of the biofuel n-butanol by converting acetoacetyl-CoA to 3-hydroxybutyryl-CoA, molecular mechanism of n-butanol biosynthesis, overview
synthesis
the enzyme is used in the biosynthesis of n-butanol from acetyl-CoA by the reduction of acetoacetyl-CoA to (S)-3-hydroxybutyryl-CoA
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, J.; Kim, K.
Cloning, expression, purification, crystallization and X-ray crystallographic analysis of the (S)-3-hydroxybutyryl-CoA dehydrogenase PaaH1 from Ralstonia eutropha H16
Acta Crystallogr. Sect. F
70
955-958
2014
Cupriavidus necator (Q0KEY8), Cupriavidus necator, Cupriavidus necator ATCC 17699 (Q0KEY8)
Volodina, E.; Steinbuechel, A.
(S)-3-hydroxyacyl-CoA dehydrogenase/enoyl-CoA hydratase (FadB) from fatty acid degradation operon of Ralstonia eutropha H16
AMB Express
4
69
2014
Cupriavidus necator (Q0KEG0), Cupriavidus necator DSM 428 (Q0KEG0)
Kim, J.; Chang, J.H.; Kim, K.J.
Crystal structure and biochemical properties of the (S)-3-hydroxybutyryl-CoA dehydrogenase PaaH1 from Ralstonia eutropha
Biochem. Biophys. Res. Commun.
448
163-168
2014
Cupriavidus necator (Q0KEY8), Cupriavidus necator, Cupriavidus necator ATCC 17699 (Q0KEY8)
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