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Enzyme Nomenclature
Information on EC 1.1.1.35 - 3-hydroxyacyl-CoA dehydrogenase
for references in articles please use BRENDA:EC1.1.1.35
Word Map on EC 1.1.1.35
- 1.1.1.35
- citrate
-
long-chain
- peroxisomal
- acyl-coas
-
thiolase
- carnitine
- hexokinase
-
trifunctional
-
phosphofructokinase
-
vastus
- lateralis
- hypoglycemia
- soleus
-
medium-chain
-
endurance
- acetoacetyl-coa
-
2-enoyl-coa
- hyperinsulinism
- lchad
- acylcarnitines
-
extensor
-
plantaris
-
hypoketotic
-
schulz
-
beta-hydroxyacyl-coa
- trans-2-enoyl-coa
-
hydroxyacyl-coas
-
hellp
- 3-oxoacyl-coa
-
2,4-dienoyl-coa
-
4.1.3.7
- crotonase
- synthesis
- medicine
- biofuel production
- diagnostics
- pharmacology
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
1.1.1.35
-
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RECOMMENDED NAME
GeneOntology No.
3-hydroxyacyl-CoA dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
-
-
-
-
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
highly conserved residue Ser137 is essential for activity
-
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
molecular reaction mechanism, a His-Glu pair is essential for actalysis in the active site
-
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
reaction mechanism via enolate intermediate
-
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
structure-function analysis using the crystal structure, PDB ID 4j0f, and catalytic mechanism, overview
-
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
structure-function analysis and catalytic mechanism, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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]).
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CAS REGISTRY NUMBER
COMMENTARY
9028-40-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
multifunctional beta-oxidation enzyme complex composed of 2 different 3-hydroyacyl-CoA dehydrogenases, 2 different 2-enoyl-CoA hydratases, thiolase, and epimerase activities
-
-
multifunctional beta-oxidation enzyme complex composed of 2 different 3-hydroyacyl-CoA dehydrogenases, 2 different 2-enoyl-CoA hydratases, thiolase, and epimerase activities
-
-
-
286590, 286593, 286594, 286596, 286598, 286606, 286607, 286608, 286609, 286610, 286611, 33713, 673530
-
-
isozyme 3-ketoacyl-CoA reductase 1; high erucic acid rapeseed variant, two isozymes encoded by genes Bn-kcr1 and Bn-kcr2, two cultivars Gaspard and ISLR4
SwissProt
isozyme 3-ketoacyl-CoA reductase 2; high erucic acid rapeseed variant, two isozymes encoded by genes Bn-kcr1 and Bn-kcr2, two cultivars Gaspard and ISLR4
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
based on the chain length of the substrates, the HAD family is divided into three subclasses: 3-hydroxyacyl-CoA dehydrogenases (HADs), long-chain 3-hydroxyacyl-CoA dehydrogenases (LCHADs) and short-chain 3-hydroxyacyl-CoA dehydrogenases (SCHADs). HADs are soluble dimeric enzymes that exhibit substrate specificity for an acyl-chain length of C4-C10 and are previously referred to as short-chain HADs
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
evolution
-
Caenorhabditis elegans HAD is highly conserved to human HAD
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
-
malfunction
a null mutant of fadB2 shows no significant differences from the wild-type strain with regard to lipid composition, utilization of different fatty acid carbon sources and tolerance to various stresses
malfunction
-
mice lacking SCHAD, hadh-/-, display a lower body weight and a reduced fat mass in comparison with hadh+/+ mice under high-fat diet conditions, presumably due to an impaired fuel efficiency, the loss of acylcarnitines via the urine, and increased body temperature. Food intake, total energy expenditure, and locomotor activity are not altered in knockout mice
malfunction
-
mutations in HADH cause hyperinsulinemic hypoglycemia that is precipitated by protein in a similar manner to the hyperinsulinism/hyperammonemia (HI/HA) syndrome, which is caused by mutations in the GLUD1 gene, encoding the enzyme glutamate dehydrogenase (GDH), suggesting a link between mitochondrial fatty acid oxidation, amino acid metabolism, and insulin secretion, clinical phenotypes, overview
malfunction
-
mutantions with attenuated interactions on the dimerization interface significantly decrease the enzyme activity compared to the wild-type. Such reduced activities are in consistency with the reduced ratios of the catalytic intermediate formation. Further molecular dynamics simulations results reveal that the alteration of the dimerization interface will increase the fluctuation of a distal region that plays an important role in the substrate binding. The increased fluctuation decreases the stability of the catalytic intermediate formation, and therefore the enzymatic activity is attenuated
malfunction
-
numerous human diseases are found related to mutations at HAD dimerization interface that is away from the catalytic pocket
malfunction
-
a null mutant of fadB2 shows no significant differences from the wild-type strain with regard to lipid composition, utilization of different fatty acid carbon sources and tolerance to various stresses
-
metabolism
-
the enzyme catalyzes the third reaction of the mitochondrial beta-oxidation cascade, the oxidation of 3-hydroxyacyl-CoA to 3-ketoacyl-CoA, for medium-andshort-chain fatty acids
metabolism
-
the enzyme is the penultimate enzyme of mitochondrial fatty acid beta-oxidation
metabolism
the enzyme is involved in benzoyl-coenzyme A degradation
metabolism
-
3-hydroxyacyl-CoA dehydrogenase catalyzes the third step in fatty acid beta-oxidation, oxidizing the hydroxyl group of 3-hydroxyacyl-CoA to a keto group
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
metabolism
the enzyme is involved in fatty acid degradation metabolism
metabolism
the enzyme specifically catalyzes the third step of beta oxidation
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
metabolism
-
3-hydroxyacyl-CoA dehydrogenase catalyzes the third step in fatty acid beta-oxidation
metabolism
-
3-hydroxyacyl-CoA dehydrogenase catalyzes the third step in fatty acid beta-oxidation
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
-
metabolism
-
the enzyme is involved in fatty acid degradation metabolism
-
metabolism
-
the enzyme is involved in benzoyl-coenzyme A degradation
-
metabolism
-
the enzyme specifically catalyzes the third step of beta oxidation
-
physiological function
-
PaaH functions as an NAD+-dependent [probably (S)-3–specific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview
physiological function
-
PaaH functions as an NAD+-dependent [probably (S)-3–specific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview
physiological function
-
the enzyme is involved in thermogenesis, in the maintenance of body weight, and in the regulation of nutrient-stimulated insulin secretion. It plays an important role in adaptive thermogenesis
physiological function
-
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
physiological function
-
the enzyme is involved in autotrophic carbon fixation
physiological function
the enzyme is classified as an oxidoreductase in fatty acid metabolic processes. It specifically catalyzes the third step of beta oxidation. Long-chain fatty acids are utilized by Leptospira as the sole carbon source and are metabolized by beta-oxidation. Therefore, a large amount of HADH may be produced intracellularly and released to get carbons and energy by oxidizing free fatty acid
physiological function
-
the enzyme is classified as an oxidoreductase in fatty acid metabolic processes. It specifically catalyzes the third step of beta oxidation. Long-chain fatty acids are utilized by Leptospira as the sole carbon source and are metabolized by beta-oxidation. Therefore, a large amount of HADH may be produced intracellularly and released to get carbons and energy by oxidizing free fatty acid
-
physiological function
-
the enzyme is involved in autotrophic carbon fixation; the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
physiological function
-
PaaH functions as an NAD+-dependent [probably (S)-3–specific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview
-
additional information
-
enzyme-protein interaction analysis in different tissues and subcellular compartments, detailed overview
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
-
the adenosine diphosphate moiety of NAD+ is not highly stabilized compared with the remainder of the acetoacetyl-CoA molecule
additional information
-
molecular mechanism about the essential role of the HAD dimerization interface in its catalytic activity via allosteric effects, molecular dynamics simulation, overview
additional information
-
molecular mechanism about the essential role of the HAD dimerization interface in its catalytic activity via allosteric effects, molecular dynamics simulation, overview
additional information
-
conserved catalytic residues are Ser119, His140, and Asn190
-
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
-
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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
(R)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
cf. EC 1.1.1.36
-
-
r
1-propanol + NAD+
n-propanal + NADH
-
multifunctional enzyme from brain
-
ir
2-fluoro-3-hydroxy-4-octenoyl-CoA + NAD+
2-fluoro-3-oxo-4-octenoyl-CoA + NADH
-
-
-
-
r
2-fluoro-3-hydroxyoctanoyl-CoA + NAD+
2-fluoro-3-oxooctanoyl-CoA + NADH
-
-
-
-
r
2-propanol + NAD+
acetone + NADH
-
multifunctional enzyme from brain
-
ir
3-hydroxy-2-methylacyl-CoA + NAD+
3-oxo-2-methylacyl-CoA + NADH
-
preferred substrate of SCHAD, no activity towards 3-hydroxy-2-methylacyl-CoA by HAD
-
-
-
3-oxoacyl-CoA + NADH
3-hydroxyacyl-CoA + NAD+
-
key enzyme involved in fatty acid oxidation
-
-
r
5alpha-dihydrotestosterone + NADH
(3beta,5alpha,17beta)-androstane-3,17-diol + NAD+
-
-
-
r
8-(acetoacetylthio)-6-ethyloctanoic acid + NADH
6-ethyl-8-[[(1S)-1-hydroxy-3-oxobutyl]thio]octanoic acid + NAD+
-
-
-
r
8-(acetoacetylthio)-6-mercaptooctanoic acid + NADH
8-[[(1S)-1-hydroxy-3-oxobutyl]thio]-6-mercaptooctanoic acid + NAD+
-
-
-
r
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+
-
-
-
r
acetoacetyl-N-beta-alanylcysteamine + NADH
(S)-3-hydroxybutyryl-N-beta-alanylcysteamine + NAD+
-
-
-
r
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+
-
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in fatty acid beta-oxidation in beta cells, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in fatty acid beta-oxidation in beta cells, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is a B-side-specific dehydrogenase with hydride transfer occurring on the si face of the nicotinamide ring
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
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
-
-
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
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
-
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
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
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
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
the enzyme is involved in autotrophic carbon fixation
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
no activity with (R)-3-hydroxybutanoyl-CoA, no activity with NADP+. Bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase (EC 4.2.1.150/EC 1.1.1.35)
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
the enzyme is involved in autotrophic carbon fixation
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
no activity with (R)-3-hydroxybutanoyl-CoA, no activity with NADP+. Bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase (EC 4.2.1.150/EC 1.1.1.35)
-
-
?
(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+
-
-
?
(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+
-
-
?
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
the enzyme is involved in betaq-oxidation cycle
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
no activity woth NADP+
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
the enzyme is involved in betaq-oxidation cycle
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
no activity woth NADP+
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
both enzyme activities are specific for L-isomers
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
both enzyme activities are specific for L-isomers
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
highest activity with acetoacetyl-CoA, significant activity with increasing chain length up to C16
-
r
(S)-3-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH
-
-
-
-
(S)-3-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH
-
low activity for mitochondrial enzyme
-
r
17beta-estradiol + NAD+
estrone + NADH
-
enzyme from brain contains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
17beta-estradiol + NAD+
estrone + NADH
-
enzyme conatains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
-
-
-
r
3-acetoacetyl-CoA + NADH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
-
-
-
r
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
no dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA with NADP+ as cofactor
-
-
ir
3-acetoacetyl-CoA + NADPH + H+
(S)-3-hydroxybutyryl-CoA + NAD+
no dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA with NADP+ as cofactor
-
-
ir
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
the enzyme is involved in benzoyl-coenzyme A degradation
-
-
?
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
?
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
the enzyme is involved in benzoyl-coenzyme A degradation
-
-
?
3-ketohexadecanoyl-CoA + NADH
(S)-3-hydroxhexadecanoyl-CoA + NAD+
-
-
r
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
-
the enzyme is required for biosynthesis of fumonisins
-
-
?
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
-
3-keto reduction
-
-
?
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
-
the enzyme is required for biosynthesis of fumonisins
-
-
?
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
-
3-keto reduction
-
-
?
5alpha-androstane-3,17-diol + NAD+
5alpha-dihydrotestosterone + NADH
-
inactivation
-
-
?
acetoacetyl-CoA + NADH
(S)-3-hydroxybutyryl-CoA + NAD+
-
-
both enzyme activities are specific for L-isomers
-
r
acetoacetyl-CoA + NADH
(S)-3-hydroxybutyryl-CoA + NAD+
-
-
both enzyme activities are specific for L-isomers
-
r
acetoacetyl-CoA + NADH
3-hydroxybutyryl-CoA + NAD+
-
for the purpose of specifically measuring intracellular Hadh2 activities, branched-chain acyl-CoA thioesters, instead of acetoacetyl-CoA, shall be used as the substrate in either the forward or reverse reaction. In contrast to 3-hydroxyacyl-CoA dehydrogenase catalyzing the third reaction of straight-chain fatty acid oxidation spiral, HSD10 (formerly Hadh2) functions in isoleucine and steroid metabolism
-
-
?
acetoacetyl-N-acetylcysteamine + NADH
(S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
-
-
-
-
-
acetoacetyl-N-acetylcysteamine + NADH
(S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
-
-
-
-
acetoacetyl-N-acetylcysteamine + NADH
(S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
-
-
-
-
-
acetoacetyl-N-acetylcysteamine + NADH
(S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
-
-
-
r
acetoacetyl-pantetheine + NADH
(S)-3-hydroxybutyryl-pantetheine
-
-
-
-
-
additional information
?
-
-
KCR1 can complement the yeast ybr159DELTA mutant, KCR proteins are divergent, only KCR1 can restore heterologous elongase activity, thus only KCR1 is a functional KCR isoform involved in microsomal fatty acid elongation
-
-
-
additional information
?
-
-
high erucic acid rapeseed variants show higher enzyme expression than low erucic acid rapeseed variants
-
-
-
additional information
?
-
high erucic acid rapeseed variants show higher enzyme expression than low erucic acid rapeseed variants
-
-
-
additional information
?
-
high erucic acid rapeseed variants show higher enzyme expression than low erucic acid rapeseed variants
-
-
-
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 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 enzyme is essentially involved in mitochondrial fatty acid beta-oxidation by catalyzing straight chain 3-hydroxyacyl-CoAs, the enzyme plays a role in Alzheimer's disease and Parkinson's disease, overview
-
-
-
additional information
?
-
-
the enzyme is involved in intracrinology and is essential for the metabolism of isoleucine and branched-chain fatty acids
-
-
-
additional information
?
-
-
the enzyme is involved in the penultimate step in mitochondrial fatty acid oxidation and in development of type 2 diabetes
-
-
-
additional information
?
-
-
short-chain L-3-hydroxyacyl-CoA dehydrogenase shows a wide substrate spectrum including cholic acids, steroids, and fatty acids with a preference for short-chain methyl-branched acyl-CoAs, SCHAD might be identical with 17beta-hydroxysteroid dehyxrogenase in human mitochondria, overview
-
-
-
additional information
?
-
-
HADH gene with a novel homozygous missense mutation M188V. Mutations in the HADH gene are associated with significantly decreased short-chain L-HADH activity, mildly decreased medium- and long-chain L-HADH activity, protein-induced hyperinsulinemic hypoglycemia. Patients with hyperinsulinemic hypoglycemia due to HADH gene mutations may have normal acylcarnitines and urine organic acids
-
-
-
additional information
?
-
-
no activity of the wild-type enzyme with 2,2-difluoro-3-hydroxyoctanoyl-CoA and 2,2-difluoro-3-hydroxy-4-octenoyl-CoA, substrate specificity of wild-type and mutant enzymes, y, overview
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
17beta-estradiol + NAD+
estrone + NADH
-
enzyme conatains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
3-oxoacyl-CoA + NADH
3-hydroxyacyl-CoA + NAD+
-
key enzyme involved in fatty acid oxidation
-
-
r
5alpha-androstane-3,17-diol + NAD+
5alpha-dihydrotestosterone + NADH
-
inactivation
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in fatty acid beta-oxidation in beta cells, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
Q72M90
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
Q72M90
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
-
the enzyme is involved in fatty acid beta-oxidation in beta cells, overview
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
C4IEM5
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
Q0KEY8
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
Q0KEG0
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
Q0KEY8
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
Q0KEG0
-
-
-
r
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
the enzyme is involved in autotrophic carbon fixation
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
A4YDS4
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
A4YDS4
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
(S)-3-hydroxybutanoyl-CoA + NAD+
acetoacetyl-CoA + NADH + H+
-
the enzyme is involved in autotrophic carbon fixation
-
-
?
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
P9WNP7
the enzyme is involved in betaq-oxidation cycle
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
3-acetoacetyl-CoA + NADH + H+
P9WNP7
the enzyme is involved in betaq-oxidation cycle
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
both enzyme activities are specific for L-isomers
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
both enzyme activities are specific for L-isomers
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
-
-
-
r
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
D3RXI4
the enzyme is involved in benzoyl-coenzyme A degradation
-
-
?
3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
D3RXI4
the enzyme is involved in benzoyl-coenzyme A degradation
-
-
?
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
-
the enzyme is required for biosynthesis of fumonisins
-
-
?
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
-
the enzyme is required for biosynthesis of fumonisins
-
-
?
additional information
?
-
-
high erucic acid rapeseed variants show higher enzyme expression than low erucic acid rapeseed variants
-
-
-
additional information
?
-
Q84X95
high erucic acid rapeseed variants show higher enzyme expression than low erucic acid rapeseed variants
-
-
-
additional information
?
-
Q84X96
high erucic acid rapeseed variants show higher enzyme expression than low erucic acid rapeseed variants
-
-
-
additional information
?
-
-
the enzyme is essentially involved in mitochondrial fatty acid beta-oxidation by catalyzing straight chain 3-hydroxyacyl-CoAs, the enzyme plays a role in Alzheimer's disease and Parkinson's disease, overview
-
-
-
additional information
?
-
-
the enzyme is involved in intracrinology and is essential for the metabolism of isoleucine and branched-chain fatty acids
-
-
-
additional information
?
-
-
the enzyme is involved in the penultimate step in mitochondrial fatty acid oxidation and in development of type 2 diabetes
-
-
-
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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)
-
NAD+
-
-
NAD+
no dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA with NADP+ as cofactor
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
NAD+
-
mode of cofactor binding, overview. The NAD+-binding site is located at the G-x-G-x-x-G nucleotide-binding motif, comprising residues Gly8-Ala9-Gly10-Thr11-Met12-Gly13. The hydroxyl groups of a phosphate moiety are hydrogen-bonded with the main chain nitrogen atoms of Thr11 and Met12. The nicotinamide and the two ribose rings of NAD+ are stabilized through hydrogen bond interactions mediated by the conserved Asp31, Glu90, Lys95, Asn115, Ser117, and Asn141 residues. The adenine moiety of NAD+ is positioned at the hydrophobic pocket formed by hydrophobic residues such as Leu7, Ile32, Ala88, Ile89, Ile94, and Ile98. One exception is Arg30, which assists the binding of the adenine moiety of NAD+ through a hydrogen bond
NADH
conversion of acetoacetyl-CoA to beta-hydroxybutyryl-CoA
NADPH
conversion of acetoacetyl-CoA to beta-hydroxybutyryl-CoA
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
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
EDTA
about 35% inhibition at 1 mM, about 25% inhibition at 10 mM
K+
about 30% inhibition at 1 mM, about 20% inhibition at 10 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
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.088
(S)-3-hydroxydecanoyl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxydecanoyl-CoA
0.0721
(R)-3-hydroxyacyl-CoA
-
recombinant wild-type enzyme, pH 7.0, 25°C
0.1157
(R)-3-hydroxyacyl-CoA
-
recombinant mutant R204A/Y209A, pH 7.0, 25°C
0.000058
(S)-3-hydroxybutyryl-CoA
-
isozyme SCHAD II, at pH 8.0; isozyme SCHAD II, at pH 9.3
0.0699
(S)-3-hydroxybutyryl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxybutyryl-CoA
0.0286
(S)-3-hydroxyhexanoyl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxyhexanoyl-CoA
0.0163
(S)-3-hydroxyoctanoyl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxyoctanoyl-CoA
0.076
acetoacetyl-CoA
pH 6.5, 30°C, recombinant enzyme in presence of 0.1 mM acetyl-CoA
additional information
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics of recombinant wild-type and mutant enzymes, detailed overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
(R)-3-hydroxyacyl-CoA
-
recombinant mutant R204A/Y209A, pH 7.0, 25°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
90
(R)-3-hydroxyacyl-CoA
-
recombinant mutant R204A/Y209A, pH 7.0, 25°C
300
(R)-3-hydroxyacyl-CoA
-
recombinant mutants R204A and Y209A, pH 7.0, 25°C
600
(R)-3-hydroxyacyl-CoA
-
recombinant wild-type enzyme, pH 7.0, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.48
-
enzyme activity in inner membrane of liver mitochondria, substrate acetoacetyl-CoA
0.75
-
72% activivty is bound to the matrix surface of the inner mitochondria membrane, binding is inhibited by increasing ionic strength and pH
1.5
3 - 8
-
pH 8.0, 65°C, 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
16.5
purified recombinant enzyme, pH 6.5, 30°C, substrate (S)-3-hydroxybutanoyl-CoA with NAD+
23.4
-
L-3-hydroxyacyl-CoA dehydrogenase activity of the trifunctional beta-oxidation protein
additional information
-
the N-terminal His-tag does notinfluence enzyme activity
1.5
purified recombinant enzyme, pH 6.5, 30°C, substrate (S)-3-hydroxybutanoyl-CoA with NADP+
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6.5
conversion of acetoacetyl-CoA to beta-hydroxybutyryl-CoA decreases above pH 6.5
9.6
10
10
NAD+-dependent dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA
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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
9 - 11
pH 9.0: about 45% of maximal activity, pH 11.0: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
37
NAD+-dependent dehydration of beta-hydroxybutyryl-CoA to acetoacetyl-CoA
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity of the enzyme it encodes is particularly high in the pancreas and especially in the islets of Langerhans
-
in oocytes from diabetic mice, activity of Hadh2 is significantly reduced
-
high level expression in malignant prostatic epithelial cells
additional information
-
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase
-
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase
-
-
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase
-
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase
-
-
immunohistochemic analysis, more intense staining in islets than in the surrounding exocrine tissue, being strongly present in insulin-positive cells and only weakly in glucagon-positive alpha cells
-
high HADH expression level, activity of the enzyme it encodes is particularly high in the pancreas and especially in the islets of Langerhans
additional information
-
KCR1 and KCR2 transcripts in inflorescence stems
additional information
enzyme detection in urine of infected Mesocricetus auratus: leptospiral protein, 3-hydroxyacyl-CoA dehydrogenase (HADH), is found to be excreted in the urine of hamsters during the early phase of infection
additional information
-
enzyme detection in urine of infected Mesocricetus auratus: leptospiral protein, 3-hydroxyacyl-CoA dehydrogenase (HADH), is found to be excreted in the urine of hamsters during the early phase of infection
-
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
O28262
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)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
34000
60000
65000
70000
75000
93000
-
4 * 93000, trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3, SDS-PAGE
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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
tetramer
additional information
?
x * 52000, recombinant His-tagged enzyme, SDS-PAGE, x * 47865, sequence calculation; x * 60000, native enzyme isolated from hamster urine, SDS-PAGE
?
-
x * 52000, recombinant His-tagged enzyme, SDS-PAGE, x * 47865, sequence calculation; x * 60000, native enzyme isolated from hamster urine, SDS-PAGE
-
homodimer
-
structure-function analysis using the crystal structure, PDB ID 4j0f
monomer
1 * 86000, recombinant His-tagged enzme, SDS-PAGE, 1 * 85900, about, sequence calculation
monomer
-
1 * 86000, recombinant His-tagged enzme, SDS-PAGE, 1 * 85900, about, sequence calculation
-
tetramer
-
4 * 93000, trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3, SDS-PAGE
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
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
-
additional information
-
the hydratase and the thiolase functions are located on the large subunit, whereas 2 dehydrogenase functions are located on the 2 smaller subunits, epimerase activity is only measurable in the complete enzyme complex
additional information
-
the hydratase and the thiolase functions are located on the large subunit, whereas 2 dehydrogenase functions are located on the 2 smaller subunits, epimerase activity is only measurable in the complete enzyme complex
-
additional information
-
primary structure analysis, structure-function relationship of SCHAD, overview
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged enzyme, hanging drop vapour diffusion method, 10 mg/ml protein in 25 mM sodium acetate trihydrate, pH 5.0, and 300 mM sodium chloride is mixed with an equal volume of reservoir solution, containing 21% PEG 3350, 0.2 M sodium chloride, 0.1 M MES, pH 6.5, for parallelepiped-shaped crystals and 23% PEG 3350, 0.2 M sodium chloride, 0.1 M bicine, pH 8.0, for cuboid-shaped crystals, equilibration against 0.20 ml reservoir solution, 3-5days at 18°C, X-ray diffraction structure determination and analysis of parallelepiped-shaped cuboid-shaped crystal at 1.60 A and 2.20 A resolution, respectively
-
purified recombinant detagged wild-type enzyme, crystals are grown by hanging drop method from 23% PEG 3350, 0.2 M sodium chloride, 0.1M N,N-bis (2-hydroxyethyl)glycine, pH 8.0, X-ray diffraction structure determination and analysis at 2.20 A resolution, molecular replacement with the human HAD structure as search model, PDB ID 3had
-
hanging drop vapour diffusion method, mixing of 30 mg/ml protein in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with reservoir solution containing 2 M ammonium sulfate, 0.1 M CAPS, pH 10.5, and 0.2 M lithium sulfate, 22°C, 7 days, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement method and structure modeling
-
purified recombinant His6-tagged wild-type enzyme in apoform and in complex with substrates acetoacetyl-CoA and NAD+, hanging drop vapour diffusion method, mixing of 30 mg/ml protein in 40 mM Tris-HCl, pH 8.0, 1 mM DTT, with or without 20 mM NAD+, and 20 mM acetoacetyl-CoA, with reservoir solution containing 0.2 M Li2SO4, 0.1 M CAPS, pH 10.5, and 2 M ammonium sulfate, 22°C, 7 days, X-ray diffraction structure determination and analysis at 1.8-2.54 A resolution, molecular replacement and structure modeling
-
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
-
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 18°C, 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, 4°C, 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
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 120 mM potassium phosphate, pH 7.0, several months without loss of activity
-
-76°C, 0.2 M potassium phosphate, pH 6.6, 25% glycerol, 10 mM mercaptoethanol, several months, no loss in activity
-
-80°C, purified recombinant His-tagged wild-type and mutant enzymes, stable for at least 3 months
-
4°C, purified recombinant His-tagged wild-type enzyme, 1 week, no significant loss of activity
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, first CM-cellulose, gelfiltration, second and third CM-cellulose
-
beta-oxidation enzyme complex 67fold to homogeneity by ammonium sulfate precipitation, density gradient centrifugation, and ion-exchange chromatography
-
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
-
recombinant C-terminally GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity and anion exchange chromatography, with cleavage of the GST-tag
-
recombinant C-terminally GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, cleavage of the GST-tag by PPase, followed by gel filtration, anion exchange chromatography, and ultrafiltration
-
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain B834 by nickel affinity chromatography and gel filtration to about 95% purity
-
recombinant C-terminally His6-tagged wild-type or selenomethionine-labeled enzymes from Escherichia coli strain B834 by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli by Co2+ affinity chromatography
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His6-tagged enzyme from Escherichia coli strain B834 by nickel affinity chromatography and gel filtration
-
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
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)
DNA and amino acid sequence determination and analysis, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain B834
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expressed in Escherichia coli
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 F54C8.1, recombinant expression of C-terminally GST-tagged enzyme in Escherichia coli strain BL21(DE3)
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 paaH1, recombinant expression of C-terminally His6-tagged wild-type or selenomethionine-labeled enzymes in Escherichia coli strain B834
overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) as soluble N-terminally His-tagged enzymes
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recombinant expression of His-tagged enzyme in Escherichia coli
recombinant expression of His6-tagged enzyme in Escherichia coli strain B834
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R204A
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site-directed mutagenesis, the mutant with attenuated interactions on the dimerization interface still maintains a dimerization form, but the enzymatic activity is significantly decreased compared the wild-type
R204A/Y209A
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site-directed mutagenesis, the mutant with attenuated interactions on the dimerization interface still maintains a dimerization form, but the enzymatic activity is significantly decreased compared the wild-type
Y209A
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site-directed mutagenesis, the mutant with attenuated interactions on the dimerization interface still maintains a dimerization form, but the enzymatic activity is significantly decreased compared the wild-type
K50A
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site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
K50A//L232Y
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site-directed mutagenesis, the mutant shows about 3fold increased activity compared to the wild-type enzyme
K50A/K54
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site-directed mutagenesis, the mutant shows about 3fold increased activity compared to the wild-type enzyme
K50A/K54A/L232Y
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site-directed mutagenesis, the mutant shows about 5fold increased activity compared to the wild-type enzyme
K54A
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site-directed mutagenesis, the mutant shows about 2fold increased activity compared to the wild-type enzyme
K54A/L232Y
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site-directed mutagenesis, the mutant shows about 4fold increased activity compared to the wild-type enzyme
L232Z
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site-directed mutagenesis, the mutant shows about 2.5fold increased activity compared to the wild-type enzyme
K56A
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site-directed mutagenesis, the mutant shows about twofold increased activity compared to the wild-type enzyme
N190A
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site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
R52A
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site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
K56A
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site-directed mutagenesis, the mutant shows about twofold increased activity compared to the wild-type enzyme
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N190A
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site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
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R52A
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site-directed mutagenesis, the mutant shows highly decreased activity compared to the wild-type enzyme
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D279E
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naturally occuring polymorphism probably involved in development of type 2 diabetes