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

EC NUMBER
COMMENTARY
1.1.1.35
-
RECOMMENDED NAME
GeneOntology No.
3-hydroxyacyl-CoA dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
show the reaction diagram
highly conserved residue Ser137 is essential for activity
-
(S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H+
show the reaction diagram
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+
show the reaction diagram
reaction mechanism via enolate intermediate
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
(R)- and (S)-3-hydroxybutyrate biosynthesis
-
3-hydroxypropionate/4-hydroxybutyrate cycle
-
4-hydroxybenzoate biosynthesis V
-
androstenedione degradation
-
benzoyl-CoA degradation I (aerobic)
-
Biosynthesis of secondary metabolites
-
Butanoate metabolism
-
Caprolactam degradation
-
Carbon fixation pathways in prokaryotes
-
cholesterol degradation to androstenedione I (cholesterol oxidase)
-
cholesterol degradation to androstenedione II (cholesterol dehydrogenase)
-
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
-
Lysine degradation
-
Metabolic pathways
-
methyl ketone biosynthesis
-
Microbial metabolism in diverse environments
-
phenylacetate degradation I (aerobic)
-
Primary bile acid biosynthesis
-
pyruvate fermentation to butanoate
-
pyruvate fermentation to butanol I
-
pyruvate fermentation to butanol II
-
pyruvate fermentation to hexanol
-
Toluene degradation
-
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]).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1-specific DPN-linked beta-hydroxybutyric dehydrogenase
-
-
-
-
17beta-HSD10
-
-
3-hydroxyacetyl-coenzyme A dehydrogenase
-
-
-
-
3-hydroxyacyl coenzyme A dehydrogenase
-
-
-
-
3-hydroxyacyl-CoA dehydrogenase
-
-
3-hydroxyacyl-CoA dehydrogenase
-
-
3-hydroxyacyl-CoA dehydrogenase
-
-
3-hydroxyacyl-CoA dehydrogenase
-
-
3-hydroxyacyl-CoA dehydrogenase II
-
-
3-hydroxyacyl-coenzyme A dehydrogenase
-
-
3-hydroxyacyl-coenzyme A dehydrogenase
Euglena gracilis 1224-5/25
-
-
-
3-hydroxyacyl-coenzyme A dehydrogenase
-
-
3-hydroxyadipyl-CoA dehydrogenase
-
-
3-hydroxyadipyl-CoA dehydrogenase (NAD+) (probably (S)-3-specific)
-
-
3-hydroxyisobutyryl-CoA dehydrogenase
-
-
-
-
3-keto reductase
-
-
-
-
3-ketoacyl-CoA reductase
Q84X95, Q84X96
-
3-L-hydroxyacyl-CoA dehydrogenase
-
-
-
-
3-L-hydroxybutyryl-CoA dehydrogenase
-
-
-
-
3beta-hydroxyacyl coenzyme A dehydrogenase
-
-
-
-
beta hydroxyacyl dehydrogenase
-
-
-
-
beta-hydroxy acid dehydrogenase
-
-
-
-
beta-hydroxyacyl CoA dehydrogenase
-
-
-
-
beta-hydroxyacyl-coenzyme A synthetase
-
-
-
-
beta-hydroxybutyrylcoenzyme A dehydrogenase
-
-
-
-
beta-keto-reductase
-
-
-
-
beta-ketoacyl reductase
-
-
beta-ketoacyl-CoA reductase
-
-
-
-
beta-ketoacyl-CoA reductase
Q84X95, Q84X96
-
beta-ketoacyl-coenzyme A reductase
-
-
betahydroxyacylcoenzyme A dehydrogenase
-
-
-
-
endoplasmic reticulum-associated amyloid beta-peptide binding protein
-
-
-
-
Fum13p
Gibberella moniliformis A0149
-
-
-
HADH
-
-
HADH
-
-
HADH2
-
-
HCDH
-
-
-
-
L-3-hydroxyacyl CoA dehydrogenase
-
-
-
-
L-3-hydroxyacyl-CoA dehydrogenase
-
-
L-3-hydroxyacyl-CoA dehydrogenase, short chain
-
-
L-3-hydroxyacylcoenzyme A dehydrogenase
-
-
-
-
L-3-hydroxybutyryl CoA dehydrogenase
-
-
L-specific 3-hydroxyacyl-CoA dehydrogenase
-
-
medium- and short-chain-3-hydroxyacyl-CoA dehydrogenase
-
-
multifunctional beta-oxidation enzyme
-
-
multifunctional beta-oxidation enzyme
Euglena gracilis 1224-5/25
-
-
-
PaaH
-
gene name
-
SCHAD
-
-
SCHAD I
-
isozyme
SCHAD II
-
isozyme
SCHSD
-
-
Scully protein
-
-
-
-
short chain L-3-hydroxyacyl-CoA dehydrogenase
-
displays optimal activity using 6-carbon substrates
short-chain 3-hydroxyacyl-CoA dehydrogenase
-
-
short-chain 3-hydroxyacyl-CoA dehydrogenase
-
-
short-chain 3-hydroxyacyl-CoA dehydrogenase
-
-
short-chain 3-hydroxyacyl-coenzyme A dehydrogenase
-
-
short-chain hydroxyacyl CoA dehydrogenase
-
-
short-chain L-3-hydroxyacyl-CoA dehydrogenase
-
-
short-chain L-3-hydroxyacyl-CoA dehydrogenase
-
-
TFP
-
trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3
type 10 17beta-hydroxysteroid dehydrogenase
-
-
type II HADH
-
-
-
-
medium- and short-chain-3-hydroxyacyl-coenzyme A dehydrogenase
-
-
additional information
-
PaaH is a member of the alcohol dehydrogenase family
additional information
-
PaaH is a member of the alcohol dehydrogenase family
-
CAS REGISTRY NUMBER
COMMENTARY
9028-40-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
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
Manually annotated by BRENDA team
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
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
Gibberella moniliformis A0149
strain A0149, gene FUM13
-
-
Manually annotated by BRENDA team
gene HADHSC
-
-
Manually annotated by BRENDA team
gene hadh
-
-
Manually annotated by BRENDA team
KT2442, KTOY01 and KTOY07
-
-
Manually annotated by BRENDA team
strain KT2442, gene fadB
-
-
Manually annotated by BRENDA team
Pseudomonas putida KT2442
strain KT2442, gene fadB
-
-
Manually annotated by BRENDA team
Wistar rat
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
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
-
PaaH functions as an NAD+-dependent [probably (S)-3–specific] 3-hydroxyadipyl-CoA dehydrogenase forming 3-oxoadipyl-CoA in the aerobic phenylacetate pathway, overview
-
metabolism
-
the enzyme is the penultimate enzyme of mitochondrial fatty acid beta-oxidation
additional information
-
enzyme-protein interaction analysis in different tissues and subcellular compartments, 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
(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-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
-
the enzyme is involved in fatty acid beta-oxidation in beta cells, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
-
the nezyme is involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
-
the enzyme is a B-side-specific dehydrogenase with hydride transfer occurring on the si face of the nicotinamide ring
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
Pseudomonas putida KT2442
-
-, the nezyme is involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates, overview
-
-
?
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
Q99714
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
Q16836
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
highest activity with acetoacetyl-CoA, significant activity with increasing chain length up to C16
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
both enzyme activities are specific for L-isomers
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
Escherichia coli B.
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
Euglena gracilis 1224-5/25
-
both enzyme activities are specific for L-isomers
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
3-oxobutyryl-CoA + NADH + H+
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-hydroxybutyryl-CoA + NADP+
acetoacetyl-CoA + NADPH
show the reaction diagram
-
low activity for mitochondrial enzyme
-
r
(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
-
-
-
r
(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
-
-
-
r
(S)-3-hydroxyhexanoyl-CoA + NAD+
3-ketohexanoyl-CoA + NADH
show the reaction diagram
-
-
-
r
(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
-
enzyme from brain contains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity, enzyme conatains 17beta-hydroxysteroid and 3alpha-hydroxysteroid dehydrogenase activity
-
ir
17beta-estradiol + NAD+
estrone + NADH + H+
show the reaction diagram
-
-, inactivation
-
-
?
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-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-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
Q99714
-
-
r
3-ketohexadecanoyl-CoA + NADH
(S)-3-hydroxhexadecanoyl-CoA + NAD+
show the reaction diagram
-
-
-
r
3-ketooctanoyl-CoA + NADH
(S)-3-hydroxyoctanoyl-CoA + NAD+
show the reaction diagram
Q99714
-
-
r
3-ketooctanoyl-CoA + NADH
(S)-3-hydroxyoctanoyl-CoA + NAD+
show the reaction diagram
-
-
-
-
3-ketooctanoyl-CoA + NADH
(S)-3-hydroxyoctanoyl-CoA + NAD+
show the reaction diagram
-
-
-
r
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
-
the enzyme is required for biosynthesis of fumonisins, 3-keto reduction
-
-
?
3-oxofumonisin B3 + NADPH
fumonisin B3 + NADP+
show the reaction diagram
Gibberella moniliformis A0149
-
the enzyme is required for biosynthesis of fumonisins, 3-keto reduction
-
-
?
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
-
-, inactivation
-
-
?
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
3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
-
-
-
-
r
acetoacetyl-CoA + NADH
3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
-
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-CoA + NADH
(S)-3-hydroxybutyryl-CoA + NAD+
show the reaction diagram
Euglena gracilis, Euglena gracilis 1224-5/25
-
-
both enzyme activities are specific for L-isomers
-
r
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-acetylcysteamine + NADH
(S)-3-hydroxybutyryl-N-acetylcysteamine + NAD+
show the reaction diagram
-
-
-
-
-
acetoacetyl-N-acetylcysteamine + NADH
(S)-3-hydroxybutyryl-N-acetylcysteamine + 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 + NADH
(S)-3-hydroxybutyryl-pantetheine
show the reaction diagram
-
-
-
-
acetoacetyl-pantetheine + NADH
(S)-3-hydroxybutyryl-pantetheine
show the reaction diagram
-
-
-
-
-
acetoacetyl-pantetheine + NADH
(S)-3-hydroxybutyryl-pantetheine
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
-
-, inactivation
-
-
?
S-3-OH-acyl-CoA + NADP+
3-ketoacyl-CoA + NADH + H+
show the reaction diagram
-
FadB plays a role in the last steps of the beta-oxidation pathway
-
-
?
tiglyl-CoA + NAD+
3-oxo-2-methylacyl-CoA + NADH
show the reaction diagram
-
activity of SCHAD
-
-
-
androsterone + NAD+
androstanedione + NADH
show the reaction diagram
-
-
-
ir
additional information
?
-
-, Q84X95, 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
-
-
-
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
?
-
-
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
-
-
-
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
?
-
-
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
-
-
-
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
(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-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
-
-
-
-
r
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
-
the enzyme is involved in fatty acid beta-oxidation in beta cells, overview
-
-
?
(S)-3-hydroxyacyl-CoA + NAD+
3-oxoacyl-CoA + NADH + H+
show the reaction diagram
Pseudomonas putida, Pseudomonas putida KT2442
-
the nezyme is involved in the biosynthesis of medium-chain-length polyhydroxyalkanoates, overview
-
-
?
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
Q99714
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
Q16836
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
-
both enzyme activities are specific for L-isomers
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
Escherichia coli B.
-
-
-
r
(S)-3-hydroxybutyryl-CoA + NAD+
acetoacetyl-CoA + NADH
show the reaction diagram
Euglena gracilis 1224-5/25
-
both enzyme activities are specific for L-isomers
-
-
r
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-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
Gibberella moniliformis, Gibberella moniliformis A0149
-
the enzyme is required for biosynthesis of fumonisins
-
-
?
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
?
-
-, Q84X95, 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
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
iodoacetamide
-
-
iodoacetic acid
-
-
N-bromsuccinimide
-
-
N-ethylmaleimide
-
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
AMP-activated protein kinase
-
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.034
-
(3beta,5alpha,17beta)-androstane-3,17-diol
-
enzyme from brain
0.000058
-
(S)-3-hydroxybutyryl-CoA
-
isozyme SCHAD II, at pH 8.0; isozyme SCHAD II, at pH 9.3
0.00261
-
(S)-3-hydroxybutyryl-CoA
-
isozyme SCHAD I, at pH 8.0
0.00529
-
(S)-3-hydroxybutyryl-CoA
-
isozyme SCHAD I, at pH 8.5
0.0699
-
(S)-3-hydroxybutyryl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxybutyryl-CoA
0.31
-
(S)-3-hydroxybutyryl-CoA
-
-
0.088
-
(S)-3-Hydroxydecanoyl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxydecanoyl-CoA
0.0286
-
(S)-3-Hydroxyhexanoyl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxyhexanoyl-CoA
0.34
-
(S)-3-Hydroxyhexanoyl-CoA
-
-
0.1
-
(S)-3-hydroxylauryl-CoA
-
-
0.0163
-
(S)-3-hydroxyoctanoyl-CoA
-
mitochondrial enzyme, oxidation of (S)-3-hydroxyoctanoyl-CoA
0.35
-
(S)-3-hydroxyoctanoyl-CoA
-
-
0.043
-
17beta-estradiol
-
enzyme from brain
0.003
-
acetoacetyl-CoA
-
-
0.0138
-
acetoacetyl-CoA
-
pH 8.0
0.0166
-
acetoacetyl-CoA
-
isozyme SCHAD I, at pH 7.0
0.0169
-
acetoacetyl-CoA
-
-
0.0187
-
acetoacetyl-CoA
-
pH 7.0
0.0222
-
acetoacetyl-CoA
-
isozyme SCHAD I, at pH 8.0
0.0257
-
acetoacetyl-CoA
-
isozyme SCHAD II, at pH 7.0
0.03
-
acetoacetyl-CoA
-
pH 5.0, recombinant His-tagged mutant S137C
0.0315
-
acetoacetyl-CoA
-
isozyme SCHAD II, at pH 8.0
0.0345
-
acetoacetyl-CoA
-
pH 5.0
0.036
-
acetoacetyl-CoA
-
-
0.044
-
acetoacetyl-CoA
-
pH 5.0, recombinant His-tagged wild-type enzyme
0.045
-
acetoacetyl-CoA
-
pH 6.0
0.05
-
acetoacetyl-CoA
-
pH 6.5
0.06
-
acetoacetyl-CoA
-
-
0.066
-
acetoacetyl-CoA
-
-
0.089
-
acetoacetyl-CoA
Q99714
enzyme from brain
0.184
-
acetoacetyl-CoA
-
pH 5.0, recombinant His-tagged mutant S137A
0.263
-
acetoacetyl-CoA
-
pH 5.0, recombinant His-tagged mutant S137T
44.4
-
acetoacetyl-N-acetyl-cysteamine
-
-
10
-
acetoacetyl-N-acetylcysteamine
-
-
1.4
-
acetoacetyl-N-beta-alanylcysteamine
-
-
10
-
acetoacetyl-Nacetylcysteamine
-
-
0.08
-
acetoacetyl-pantetheine
-
-
0.4
-
acetoacetyl-pantetheine
-
-
0.56
-
acetoacetyl-pantetheine
-
-
1.19
-
acetoacetyl-pantetheine
-
-
0.00009
-
NAD+
-
isozyme SCHAD II, at pH 7.0
0.00119
-
NAD+
-
isozyme SCHAD I, at pH 7.0
0.05
-
NAD+
-
enzyme from brain, substrate 17beta-estradiol
0.0585
-
NAD+
-
-
0.21
-
NAD+
-
enzyme from brain, substrate dihydroandrosterone
0.242
-
NAD+
-
enzyme from brain, substrate androsterone
0.0009
-
NADH
-
isozyme SCHAD II, at pH 9.3
0.003
-
NADH
-
-
0.0054
-
NADH
-
-
0.02
-
NADH
Q99714
enzyme from brain
0.0338
-
NADH
-
isozyme SCHAD I, at pH 8.5
0.435
-
NADPH
-
-
0.045
-
androsterone
-
enzyme from brain
additional information
-
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.093
-
(3beta,5alpha,17beta)-androstane-3,17-diol
-
enzyme from brain
375
-
(S)-3-hydroxybutyryl-CoA
-
isozyme SCHAD I, at pH 8.5
533.3
-
(S)-3-hydroxybutyryl-CoA
-
isozyme SCHAD I, at pH 8.0
643.3
-
(S)-3-hydroxybutyryl-CoA
-
isozyme SCHAD II, at pH 8.0
1420
-
(S)-3-hydroxybutyryl-CoA
-
isozyme SCHAD II, at pH 9.3
0.011
-
17beta-estradiol
-
enzyme from brain
45
-
3-ketohexadecanoyl-CoA
-
-
24
-
3-ketohexdecanoyl-CoA
Q99714
enzyme from brain, pH 7.0
28
-
3-ketooctanoyl-CoA
Q99714
enzyme from brain, pH 7.0
102
-
3-ketooctanoyl-CoA
-
-
0.019
-
acetoacetyl-CoA
-
pH 5.0, recombinant His-tagged mutant S137C
0.026
-
acetoacetyl-CoA
-
pH 5.0, recombinant His-tagged mutant S137T
0.12
-
acetoacetyl-CoA
-
pH 5.0, recombinant His-tagged mutant S137A
21.3
-
acetoacetyl-CoA
-
isozyme SCHAD II, at pH 8.0
23.8
-
acetoacetyl-CoA
-
isozyme SCHAD II, at pH 7.0
37
-
acetoacetyl-CoA
Q99714
enzyme from brain, pH 7.0
113
-
acetoacetyl-CoA
-
pH 8.0
155
-
acetoacetyl-CoA
-
pH 5.0
246
-
acetoacetyl-CoA
-
pH 6.0
252
-
acetoacetyl-CoA
-
pH 7.0
330
-
acetoacetyl-CoA
-
pH 7.0
569
-
acetoacetyl-CoA
-
pH 5.0, recombinant His-tagged wild-type enzyme
681.7
-
acetoacetyl-CoA
-
isozyme SCHAD I, at pH 8.0
1287
-
acetoacetyl-CoA
-
isozyme SCHAD I, at pH 7.0
0.011
-
androsterone
-
enzyme from brain
705
-
NAD+
-
isozyme SCHAD II, at pH 7.0
1817
-
NAD+
-
isozyme SCHAD I, at pH 7.0
176.7
-
NADH
-
isozyme SCHAD I, at pH 8.5
510
-
NADH
-
isozyme SCHAD II, at pH 9.3
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
0.75
-
-
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
3.4
-
-
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
6
-
-
-
12.6
-
-
peroxisomal enzyme
17.35
-
Q99714
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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
mitochondrial enzyme, reduction of acetoacetyl-CoA
5
-
-
phosphate buffer
6
7
-
reduction of acetoacetyl-CoA
6
-
-
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
-
-, Q84X95, Q84X96
assay at; assay at
7.4
-
-
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
9.6
-
-
mitochondrial enzyme, oxidation of (S)-3-hydroxybutyryl-CoA
9.6
-
-
oxidation of (S)-3-hydroxybutyryl-CoA
9.8
-
-
peroxisomal enzyme, oxidation of (S)-3-hydroxybutyryl-CoA
10
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-, Q84X95, Q84X96
assay at; assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
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
Manually annotated by BRENDA team
-
high level expression in malignant prostatic epithelial cells
Manually annotated by BRENDA team
-, Q84X95, Q84X96
;
Manually annotated by BRENDA team
-
only KCR1 transcript
Manually annotated by BRENDA team
-, Q84X95, Q84X96
;
Manually annotated by BRENDA team
-
KCR1 and KCR2 transcripts
Manually annotated by BRENDA team
additional information
-, Q84X95, Q84X96
expression pattern; expression pattern
Manually annotated by BRENDA team
additional information
-
wide tissue distribution
Manually annotated by BRENDA team
additional information
-
KCR1 and KCR2 transcripts in inflorescence stems
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40000
-
-
liver enzyme
50300
-
-
gel filtration
65000
-
-
mitochondrial enzyme, gel filtration
65000
-
-
sedimentation equilibrium
65000
-
-
-
66000
-
-
gel filtration
70000
-
-
gel filtration
70000
-
-
peroxisomal enzyme, gel filtration
75000
-
-
gel filtration
75000
-
-
-
76000
-
-
gel filtration
108000
-
Q99714
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 ACCESSION NO.
COMMENTARY
LITERATURE
?
-, Q84X95, Q84X96
x * 35000, SDS-PAGE; x * 35000, SDS-PAGE
?
-
x * 34000, SDS-PAGE
dimer
-
2 * 34000, SDS-PAGE
dimer
-
2 * 33000, SDS-PAGE
dimer
-
2 * 32000, mitochondrial enzyme, SDS-PAGE
tetramer
-
2 * 78000 + 2 * 42000, SDS-PAGE
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
tetramer
Q99714
4 * 27000, enzyme from brain, SDS-PAGE
tetramer
-
1 * 45500 + 1 * 44500 + 1 * 34000 + 1 * 32000, SDS-PAGE
tetramer
Escherichia coli B.
-
2 * 78000 + 2 * 42000, SDS-PAGE
-
tetramer
Euglena gracilis 1224-5/25
-
1 * 45500 + 1 * 44500 + 1 * 34000 + 1 * 32000, SDS-PAGE
-
monomer
-
1 * 77000, peroxisomal enzyme, SDS-PAGE
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
-
structure-function relationship of SCHAD, overview
additional information
-
primary structure analysis, structure-function relationship of SCHAD, overview
additional information
Euglena gracilis 1224-5/25
-
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
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-76°C, 0.2 M potassium phosphate, pH 6.6, 25% glycerol, 10 mM mercaptoethanol, several months, no loss in activity
-
-20°C, 120 mM potassium phosphate, pH 7.0, several months without loss of 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
-
4°C, 90% ammonium sulfate, at least 6 monts, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ammonium sulfate, 50°C for 20 min, Zn(OH)2-gel
-
60°C for 10 min, phosphocellulose, Sephacryl S200
-
beta-oxidation enzyme complex 67fold to homogeneity by ammonium sulfate precipitation, density gradient centrifugation, and ion-exchange chromatography
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
overexpressed in Escherichia coli, hydroxylapatite
Q99714
ammonium sulfate, Sephadex G-150, hydroxyapatite, NAD-Sepharose 4B
-
trifunctional beta-oxidation protein with activities of EC 1.1.1.35, EC 4.2.1.17 and EC 5.1.2.3
-
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 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
-
ammonium sulfate, first CM-cellulose, gelfiltration, second and third CM-cellulose
-
overexpressed in Escherichia coli, phosphocellulose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in yeast ybr159DELTA mutant
-
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
-, Q84X95, Q84X96
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
-
-
Q99714
C-terminal hexameric histidine tag, expressed in Escherichia coli
-
expressed in Escherichia coli
-
gene HADHSC, located on chromosome 4q22-26
-
gene hadh, quantitative real-time PCR expression analysis
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) as soluble N-terminally His-tagged enzymes
-
expressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D279E
-
naturally occuring polymorphism probably involved in development of type 2 diabetes
N208A
-
site-directed mutagenesis, the substrate binding of the mutant enzyme is affected
S137A
-
site-directed mutagenesis, highly reduced activity compared to the wild-type enzyme
S137A
-
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
-
loss of KCR1 function results in embryo lethality, which cannot be rescued by KCR2 expression using the KCR1 promoter. Disruption of the KCR2 gene has no obvious phenotypic effect
H152Q
-
naturally occuring polymorphism probably involved in development of type 2 diabetes
additional information
-
inactivation of the enzyme by siRNA expression, the mutants show reduced beta-oxidation of fatty acids
P86L
-
naturally occuring polymorphism probably involved in development of type 2 diabetes
additional information
-
generation of hadh knockout mice by insertion of gene-trap vector pGT0Lxf in the ES cell line E14Tg2a.4, deletion of hadh results in a defective enzymatic activity of SCHAD, phenotype, overview. Deletion of hadh reduces body weight and adipose tissue depots, and leads to impaire thermogenesis
additional information
-
His-tagged SCHAD is immobilized on agarose beads, and interacting proteins from murine tissue extracts are isolated using affinity chromatography in preparation for LC-MS/MS identification, use of tissues from both wild-type and SCHAD knockout mice, protein interaction analysis using yeast-2 hybrid analysis and by pulldown assay, overview
additional information
-
construction of a deletion mutant of gene fadB encoding the enzyme, the mutant shows decreased production of medium-chain-length polyhydroxyalkanoates, e.g. of 3-hydroxyhexanoate, 3- hydroxyoctanoate, 3-hydroxydecanoate, 3-hydroxydodecanoate, and 3-hydroxytetradecanoate, overview
additional information
-
no extracellular 3-hydroxyalkanoic acid is produced by wild-type Pseudomonas putida KT2442 or the polyhydroxyalkanoate synthesis operon knockout mutant KTOY01 when lauric acid is used as carbon source. By expressing tesB gene encoding thioesterase II, Pseudomonas putida KT2442 can not produce extracellular 3-hydroxyalkanoic acid monomer, while the polyhydroxyalkanoate operon knockout mutant Pseudomonas putida KTOY01 (pSPD09) produces 0.35 g/l extracellular medium-chain-length 3-hydroxyalkanoic acid. KTOY07 is constructed by further knocking out fadB and fadA genes in Pseudomonas putida KTOY01. As a result, Pseudomonas putida KTOY07 increases medium-chain-length 3-hydroxyalkanoic acid to 1.68 from 0.35 g/l produced by the beta-oxidation intact mutant Pseudomonas putida KTOY01
additional information
Pseudomonas putida KT2442
-
construction of a deletion mutant of gene fadB encoding the enzyme, the mutant shows decreased production of medium-chain-length polyhydroxyalkanoates, e.g. of 3-hydroxyhexanoate, 3- hydroxyoctanoate, 3-hydroxydecanoate, 3-hydroxydodecanoate, and 3-hydroxytetradecanoate, overview
-
additional information
-
inactivation of the enzyme by siRNA expression, the mutants show reduced beta-oxidation of fatty acids, shRNA-mediated HADHSC silencing affects induced absolute and fractional insulin secretion in INS1 832-13 cells and the cellular insulin content, overview
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
after denaturation with 2-3 M urea or guanidinium-HCl, 94% activity can be recovered by dialyzing the enzyme at 4°C against 100 mM sodium diphosphate, pH 7.3, 10 mM 2-mercaptoethanol
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
HADH protects against excess amino acid-induced insulin secretion
pharmacology
-
the short-chain 3-hydroxyacyl-CoA dehydrogenase is a target for intervention in case of Alzheimer's disease and Parkinson's disease
medicine
-
lack of Hadh2 activity may impart early developmental problems, leading to embryo lethality. In addition to the 3-hydroxyacyl-CoA dehydrogenase activity, the HSD10 (formerly Hadh2) activity is also relevant to the metabolism and meiotic maturation of oocytes