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Enzyme Nomenclature
Information on EC 1.1.1.30 - 3-hydroxybutyrate dehydrogenase
for references in articles please use BRENDA:EC1.1.1.30
Word Map on EC 1.1.1.30
- 1.1.1.30
- ketone
- succinate
- acetoacetate
-
histochemical
-
lipid-requiring
- lecithin
- acetoacetyl-coa
-
thiolase
-
coa-transferase
-
submitochondrial
- alpha-glycerophosphate
-
3-oxoacid
-
ketogenic
-
enzyme-phospholipid
- synthesis
- diagnostics
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.1.1.30
-
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RECOMMENDED NAME
GeneOntology No.
3-hydroxybutyrate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
enzyme is completely dependent on the presence of phospholipid for activity
-
(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
; ordered Bi Bi mechanism, NAD+ first substrate, NADH last product to leave
-
-
-
(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
the enzyme shows a dynamical reaction mechanism. In the catalytic site, a water molecule is trapped by the catalytic Tyr155 and Ser142 residues in the vicinity of the bound NAD+ and acetate, substrate binding structure, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
(R)-3-hydroxybutanoate:NAD+ oxidoreductase
Also oxidizes other 3-hydroxymonocarboxylic acids.
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CAS REGISTRY NUMBER
COMMENTARY
9028-38-0
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
additional information
-
Gln94, His144, Lys152, and Gln196 form hydrogen bonds with carboxyl and/or ketone group of acetoacetate, Trp187, Trp257 form hydrophobic interactions with the carbon atoms of acetoacetate, and Ser142 and Tyr155 are directly related to the catalytic mechanism
malfunction
inhibiting expression of the 3-hydroxybutyrate dehydrogenase-2 gene results in abnormal accumulation of intracellular iron, increased oxidative stress, and mitochondrial iron deficiency
malfunction
enzyme inactivation in developing zebrafish embryo results in heme deficiency and delays erythrocyte maturation
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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)-2-hydroxybutanoate + NAD+
acetoacetate + NADH
-
isoenzyme from heavy mitochondria and isoenzyme from light mitochondria show no significant difference in activity
-
-
?
(R)-3-hydroxybutanoate + 3-acetylpyridine adenine dinucleotide
acetoacetate + 3-acetylpyridine adenine dinucleotideH2
-
-
-
r
(R)-3-hydroxybutanoate + NADP+
acetoacetate + NADPH
Q5KST5
activity with NADP+ is 2% of the activity with NAD+
-
-
?
2-methyl-3-hydroxybutyrate + NAD+
2-methylacetoacetate + NADH
-
-
-
r
4-hydroxybutanoate + NAD+
acetoacetate + NADH
-
isoenzyme from heavy mitochondria shows 40% lower activity than enzyme fromlight mitochondria
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
model of the binding mode of the substrate D-3-hydroxybutyrate, Gln193 is the only residue of the substrate-binding loop that interacts directly with the substrate, NAD+ binding increases the flexibility of the substrate-binding loop and shifts the equilibrium between the open and closed forms towards the closed form, overview
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
r
(R)-3-hydroxybutanoate + NADH + H+
acetoacetate + NAD+
-
the enzyme is involved in poly(3-hydroxybutyrate) biosynthesis together with acetoacetyl-CoA thiolase and PHB synthase, pathway overview, intracellular concentrations of key metabolites, i.e. CoA, acetyl-CoA, 3HB-CoA, NAD+/NADH, determine whether a cell accumulates or degrades PHB
-
-
r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
strain SA1 can degrade poly((R)-3-hydroxybutyrate), i.e. PHB
-
-
r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
-
during hibernation, the enzyme is responsible for bioconvertion of high amounts of ketone bodies, i.e. acetoacetate and (R)-3-hydroxybutyrate, in the liver for usage as energetic fuel
-
-
r
3-hydroxyvalerate + NAD+
3-oxovalerate + NADH + H+
-
-
-
-
?
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
-
the reversible reactions occur by shuttle movements of a hydrogen negative ion from the C3 atom of the substrate to the C4 atom of NAD+ and from the C4 atom of NADH to the C3 atom of the product. The reaction may be further coupled to the withdrawal of a proton from the hydroxyl group of the substrate by the ionized Tyr155 residue
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
BDH1 is needed to regulate the cytoplasmic redox state as well as to utilize 3-hydroxybutyrate
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
BDH2 is needed to regulate the cytoplasmic redox state as well as to utilize 3-hydroxybutyrate
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
BDH3 is specialized to utilize 3-hydroxybutyrate
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
BDH3 is specialized to utilize 3-hydroxybutyrate
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
BDH2 is needed to regulate the cytoplasmic redox state as well as to utilize 3-hydroxybutyrate
-
-
r
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
BDH1 is needed to regulate the cytoplasmic redox state as well as to utilize 3-hydroxybutyrate
-
-
r
levulinic acid + NADH + H+
4-hydroxyvaleric acid + NAD+
-
only the recombinant wild type enzyme with N-terminal His-tag shows activity with levulinic acid
-
-
?
levulinic acid + NADH + H+
4-hydroxyvaleric acid + NAD+
-
the wild type enzyme shows low activity with levulinic acid, while it's a good substrate for mutant enzyme H144L/W187F
-
-
?
poly-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
-
-
-
r
poly-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
-
-
-
r
additional information
?
-
-
no activity of the wild-type enzyme with levulinic acid, enzyme mutant H144L/W187F is active with levulinic acid producing 4-hydroxyvaleric acid
-
-
-
additional information
?
-
-
enzyme activity is differently regulated in liver and brain at euthermic, prehibernating,and hibernating state
-
-
-
additional information
?
-
-
a ketone body converting enzyme in mitochondria in liver jerboa, enzyme expression, activity and metabolism at different physiological states, 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
(R)-3-hydroxybutanoate + NADH + H+
acetoacetate + NAD+
-
the enzyme is involved in poly(3-hydroxybutyrate) biosynthesis together with acetoacetyl-CoA thiolase and PHB synthase, pathway overview, intracellular concentrations of key metabolites, i.e. CoA, acetyl-CoA, 3HB-CoA, NAD+/NADH, determine whether a cell accumulates or degrades PHB
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
Q5ZT49
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
Q5ZT49
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
-
?
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
Q767A0
strain SA1 can degrade poly((R)-3-hydroxybutyrate), i.e. PHB
-
-
r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
-
during hibernation, the enzyme is responsible for bioconvertion of high amounts of ketone bodies, i.e. acetoacetate and (R)-3-hydroxybutyrate, in the liver for usage as energetic fuel
-
-
r
additional information
?
-
-
enzyme activity is differently regulated in liver and brain at euthermic, prehibernating,and hibernating state
-
-
-
additional information
?
-
-
a ketone body converting enzyme in mitochondria in liver jerboa, enzyme expression, activity and metabolism at different physiological states, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
-
286513, 286514, 286516, 286517, 286521, 286522, 286525, 286527, 286528, 286530, 286535, 286538, 286540, 286542, 286543
NAD+
-
; the substrate-binding loop, residues 187-210, is partially disordered in several subunits, in both the presence and absence of NAD+, closed conformation in the complex structure with NAD+, interactions of Val185, Thr187 and Leu189 with the cosubstrate induced the conformational change from open to closed, NAD+ binding increases the flexibility of the substrate-binding loop and shifts the equilibrium between the open and closed forms towards the closed form
NAD+
-
NAD+ is bound in a large cleft in the domain. The diphosphate group of NAD+ is covered by the small additional domain, which is supported by two extended arms allowing domain movement
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,4-Dichlorophenoxyacetic acid
-
inhibits the enzyme, in vivo treatment of the animals with 2,4-dichlorophenoxyacetic acid leads to strong decrease of triglycerides level and HDL cholesterol and an increase in GOT level and LDL cholesterol, and necrosis of seminiferous tubules cells in testis, hyperplasia of hepatocytes in liver and presence of multinucleated giant cells in brain, overview
3-hydroxybutyrate
-
substrate inhibition at concentrations above 20 mM, 50% inhibition at 200 mM, cyanylated enzyme is 3fold more active at high substrate concentration
4-mercapto-3-nitrobenzoate
-
derivatization of enzyme sulfhydryl groups, less than 1% residual activity
ADP
-
2.85 mM, 0.025 mM NADH, 63% inhibition, competitive inhibitor vs. NADH and NAD+, pH 7-7.5, noncompetitive vs. acetoacetate
ADP-ribose
-
competitive inhibition vs. coenzyme, noncompetitive vs. substrate
AMP
-
2.85 mM, 0.025 mM NADH, 55% inhibition, competitive inhibitor vs. NADH and NAD+, pH 7-7.5
ATP
-
2.85 mM, 0.025 mM NADH, 79% inhibition, competitive inhibitor vs. NADH and NAD+, pH 7-7.5, noncompetitive vs. acetoacetate
D-lactate
-
5 mM, pH 8.5, 25°, 85% inhibition, uncompetitive vs. coenzyme, competitive vs. substrate
Methyl-2-methoxyphosphinylacetate
-
competitive inhibitor vs. acetoacetate
-
NAD+
-
substrate inhibition, high concentrations, noncompetitive vs. beta-hydroxybutyrate
sodium sulfite
-
uncompetitive vs. NAD+ and acetoacetate, competitive vs. beta-hydroxybutyrate
acetoacetate
-
substrate inhibition, above 5 mM, noncompetitive vs. NADH
diazenedicarboxylic acid bis(dimethylamide)
-
0.20 mM, activity can be recovered with dithiothreitol, enzyme contains a vicinal dithiol that is oxidized by diamide
L-3-hydroxybutyrate
-
5 mM, pH 8.5, 25°C, 23% inhibition; 5 mM, pH 8.5, 25°C, 32% inhibition
methylmalonate
-
brain 3-hydroxybutyrate dehydrogenase, 0.5 mM 69% inhibition, 0.75 mM 83%, 1 mM 87%, 1.5 mM 3-hydroxybutyrate, liver 3-hydroxybutyrate dehydrogenase, 0.1 mM 37% inhibition, 0.25 mM 41%, 0.5 mM 45%, 1 mM 3-hydroxybutyrate, competitive inhibition
p-chloromercuribenzoate
-
0.001 mM, extremely rapid inhibition, NAD+ and NADH protect against inhibition
p-chloromercuribenzoate
-
enzyme extremely sensitive, NADH and Ca2+ protect
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-hydroxybutyrate
induces the enzyme when contained in the growth medium
phosphatidylcholine
-
required for formation of tight and functional complexes of enzyme with NAD+, coenzyme binding strengthens the interaction of the enzyme with phosphatidylcholine
phosphatidylcholine
-
state of phosphatidylcholine determines nature of activation, noncooperative for soluble phosphatidylcholine, cooperative for bilayer phosphatidylcholine
phosphatidylcholine
-
-
286513, 286516, 286517, 286521, 286525, 286527, 286528, 286530, 286535, 286538, 286540, 286542, 286543
phosphatidylcholine
-
state of phosphatidylcholine determines nature of activation, noncooperative for soluble phosphatidylcholine, cooperative for bilayer phosphatidylcholine
phosphatidylcholine
-
-
additional information
BDH1 is abundant in cells grown on D-fructose, D-glucose, maltose, oxaloacetate, 2-oxoglutarate, L-alanine, L-arginine, L-methionine, poly-3-hydroxybutyrate, and nutrient broth, and poor in cells grown on pyruvate, gluconate, fumarate, L-malate, propionate, and n-butyrate; BDH2 is abundant in cells grown on acetate, ethanol, D-arabinose, D-ribose, oxaloacetate, 2-oxoglutarate, malaete, L-histidine, L-alanine, L-arginine, L-methionine, and poly-3-hydroxybutyrate, and scant in cells grown on pyruvate, n-butyrate, and oleate; BDH3 is produced only in cells grown on 3-hydroxybutyrate or poly-3-hydroxybutyrate as a carbon source. Expression of bdh3 may be coordinately regulated with a gene encoding putative 3-hydroxybutyrate permease
-
additional information
BDH1 is abundant in cells grown on D-fructose, D-glucose, maltose, oxaloacetate, 2-oxoglutarate, L-alanine, L-arginine, L-methionine, poly-3-hydroxybutyrate, and nutrient broth, and poor in cells grown on pyruvate, gluconate, fumarate, L-malate, propionate, and n-butyrate; BDH2 is abundant in cells grown on acetate, ethanol, D-arabinose, D-ribose, oxaloacetate, 2-oxoglutarate, malaete, L-histidine, L-alanine, L-arginine, L-methionine, and poly-3-hydroxybutyrate, and scant in cells grown on pyruvate, n-butyrate, and oleate; BDH3 is produced only in cells grown on 3-hydroxybutyrate or poly-3-hydroxybutyrate as a carbon source. Expression of bdh3 may be coordinately regulated with a gene encoding putative 3-hydroxybutyrate permease
-
additional information
BDH1 is abundant in cells grown on D-fructose, D-glucose, maltose, oxaloacetate, 2-oxoglutarate, L-alanine, L-arginine, L-methionine, poly-3-hydroxybutyrate, and nutrient broth, and poor in cells grown on pyruvate, gluconate, fumarate, L-malate, propionate, and n-butyrate; BDH2 is abundant in cells grown on acetate, ethanol, D-arabinose, D-ribose, oxaloacetate, 2-oxoglutarate, malaete, L-histidine, L-alanine, L-arginine, L-methionine, and poly-3-hydroxybutyrate, and scant in cells grown on pyruvate, n-butyrate, and oleate; BDH3 is produced only in cells grown on 3-hydroxybutyrate or poly-3-hydroxybutyrate as a carbon source. Expression of bdh3 may be coordinately regulated with a gene encoding putative 3-hydroxybutyrate permease
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
(R)-3-hydroxybutanoate
-
enzyme expressed in SF9 cells, C242S mutant, C242 important for substrate binding
0.17
acetoacetate
-
recombinant enzyme with N-terminal His-tag, at pH 6.5 and 30°C
10.47
acetoacetate
-
recombinant enzyme with C-terminal His-tag, at pH 6.5 and 30°C
2.2
beta-hydroxybutyrate
-
240 mM Na+, purified enzyme, reconstituted with total mitochondrial phospholipids
200
beta-hydroxybutyrate
-
240 mM Na+, purified enzyme, thiol group 1 modified with 1,1'-azobis(NN'-dimethylformamide), reconstituted with total mitochondrial phospholipids
260
beta-hydroxybutyrate
-
240 mM Na+, purified enzyme, thiol group 2 modified with 1,1'-azobis(NN'-dimethylformamide), reconstituted with total mitochondrial phospholipids
0.63
levulinic acid
-
recombinant mutant enzyme W187F with N-terminal His-tag, at pH 6.5 and 30°C
0.63
levulinic acid
-
mutant enzyme H144L/W187L, at pH 6.5 and 30°C; mutant enzyme W187F, at pH 6.5 and 30°C
0.64
levulinic acid
-
recombinant mutant enzyme H144L/W187F with N-terminal His-tag, at pH 6.5 and 30°C
0.78
levulinic acid
-
recombinant wild type enzyme with N-terminal His-tag, at pH 6.5 and 30°C
0.91
levulinic acid
-
recombinant mutant enzyme H144L with N-terminal His-tag, at pH 6.5 and 30°C
8.25
levulinic acid
-
recombinant mutant enzyme H144L/W187F with C-terminal His-tag, at pH 6.5 and 30°C
16.98
levulinic acid
-
recombinant mutant enzyme H144L with C-terminal His-tag, at pH 6.5 and 30°C
0.27
NAD+
-
240 mM Na+, purified enzyme, reconstituted with total mitochondrial phospholipids
additional information
additional information
-
dissociation constants for the cofactors and reaction kinetics at different physiological states in liver and brain
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.9
acetoacetate
-
recombinant enzyme with C-terminal His-tag, at pH 6.5 and 30°C
97.16
acetoacetate
-
recombinant enzyme with N-terminal His-tag, at pH 6.5 and 30°C
0.0003
levulinic acid
-
mutant enzyme W187I, at pH 6.5 and 30°C; mutant enzyme W187V, at pH 6.5 and 30°C
0.006
levulinic acid
-
recombinant wild type enzyme with N-terminal His-tag, at pH 6.5 and 30°C
0.019
levulinic acid
-
recombinant mutant enzyme W187F with N-terminal His-tag, at pH 6.5 and 30°C
0.028
levulinic acid
-
recombinant mutant enzyme H144L with C-terminal His-tag, at pH 6.5 and 30°C
0.06
levulinic acid
-
recombinant mutant enzyme H144L with N-terminal His-tag, at pH 6.5 and 30°C
0.079
levulinic acid
-
recombinant mutant enzyme H144L/W187F with C-terminal His-tag, at pH 6.5 and 30°C
0.164
levulinic acid
-
recombinant mutant enzyme H144L/W187F with N-terminal His-tag, at pH 6.5 and 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.47
acetoacetate
-
recombinant enzyme with C-terminal His-tag, at pH 6.5 and 30°C
560.1
acetoacetate
-
recombinant enzyme with N-terminal His-tag, at pH 6.5 and 30°C
0.006
levulinic acid
-
mutant enzyme W187A, at pH 6.5 and 30°C; wild type enzyme, at pH 6.5 and 30°C
0.016
levulinic acid
-
mutant enzyme H144F, at pH 6.5 and 30°C; mutant enzyme H144L/W187A, at pH 6.5 and 30°C
0.03
levulinic acid
-
mutant enzyme H144I, at pH 6.5 and 30°C; mutant enzyme H144V, at pH 6.5 and 30°C
1.62
levulinic acid
-
recombinant mutant enzyme H144L with C-terminal His-tag, at pH 6.5 and 30°C
7.68
levulinic acid
-
recombinant wild type enzyme with N-terminal His-tag, at pH 6.5 and 30°C
9.63
levulinic acid
-
recombinant mutant enzyme H144L/W187F with C-terminal His-tag, at pH 6.5 and 30°C
29.69
levulinic acid
-
recombinant mutant enzyme W187F with N-terminal His-tag, at pH 6.5 and 30°C
65.94
levulinic acid
-
recombinant mutant enzyme H144L with N-terminal His-tag, at pH 6.5 and 30°C
256.5
levulinic acid
-
recombinant mutant enzyme H144L/W187F with N-terminal His-tag, at pH 6.5 and 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.74
2,4-Dichlorophenoxyacetic acid
-
pH 8.0, 25°C, versus (R)-3-hydroxybutanoate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.07
-
heart 3-hydroxybutyrate dehydrogenase, mitochondrial extracts; kidney 3-hydroxybutyrate dehydrogenase, mitochondrial extracts
0.17
-
solubilized apo-3-hydroxybutyrate dehydrogenase, reconstituted with phosphatidylcholine/phosphatidylethanolamine/diphosphatidylglycerol, 5/4/1
0.22
-
apo-3-hydroxybutyrate dehydrogenase, reconstituted with phosphatidylcholine/phosphatidylethanolamine/diphosphatidylglycerol, 5/4/1
0.36
1.15
-
liver 3-hydroxybutyrate dehydrogenase, reconstituted with microsomal membranes
1.275
-
liver 3-hydroxybutyrate dehydrogenase, reconstituted with mitochondrial inner membranes
91
-
liver 3-hydroxybutyrate dehydrogenase, reconstituted with mitochondrial phospholipids
145
-
heart 3-hydroxybutyrate dehydrogenase, reconstituted with mitochondrial phospholipids
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.9 - 8.6
-
acetoacetate reduction, 50% activity at pH 5.0, 66% at pH 8.6
6.5 - 8.5
optimal pH of BDH3 is 8.5 in the oxidation reaction and 6.5 in the reduction reaction
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
37
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
30% of maximal activity at 20°C, 63% of maximal activity at 60°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
calculated from amino acid sequence; isoelectric focusing
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
-
additional information
-
the enzyme is localized in poly(3-hydroxybutyrate) granules, co-localization with acetoacetyl-CoA thiolase and PHB synthase, overview
additional information
-
during the cold adaptation process, the prehibernating stage, the enzyme activity is decreased compared to euthermic state, in the hibernation state, the rate of acetoacetate reduction is increased in liver, while the oxidation of D-beta-hydroxybutyrate is increased in brain
additional information
-
the physiological states of the organism, i.e. euthermic, prehibernating, and hibernating, vary between in terms of ketone bodies, glucose and lipid levels, the enzyme might lead an important conformational change depending on the state, overview, enzyme expression is increased in hibernating state
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
-
beta-hydroxybutyrate dehydrogenase from heavy and light mitochondria are isoforms
-
light and heavy mitochondria, enzyme expression and activity is increased in heavy mitochondria in hibernating state, overview
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
28000
31000
32000
33117
-
alpha4, 4 * 33117, mature protein, calculated from deduced amino acid sequence
38000
-
alpha4, 4 * 38000, preprotein, calculated from deduced amino acid sequence
110000
119000
-
reconstituted enzyme, radiation inactivation, irradiation leads to loss of activity and fragmentation
120000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
additional information
?
x * 27600, calculated from amino acid sequence; x * 32000, SDS-PAGE
?
-
x * 27600, calculated from amino acid sequence; x * 32000, SDS-PAGE
-
homotetramer
-
4 * 27200, calculated from amino acid sequence; 4 * 29000, SDS-PAGE
homotetramer
-
4 * 27200, calculated from amino acid sequence; 4 * 29000, SDS-PAGE
-
tetramer
-
alpha4, 4 * 27000, sedimentation equilibrium; alpha4, 4 * 31000, SDS-PAGE
tetramer
-
alpha4, 4 * 33117, mature protein, calculated from deduced amino acid sequence; alpha4, 4 * 38000, preprotein, calculated from deduced amino acid sequence
tetramer
-
alpha4, 4 * 27000, sedimentation equilibrium; alpha4, 4 * 31000, SDS-PAGE
additional information
-
secondary and tertiary enzyme structure analysis, overview
additional information
-
three-dimensional structure modelling, overview
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallization of the enzyme in the apo form and in the holo form with acetate as a substrate analogue, method screening, mother liquor consists of 30% w/v PEG 4000, 0.2 M sodium acetate trihydrate and 100 mM Tris-HCl, pH 8.5, at 20°C, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular-replacement method
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in complex with NAD+, malonate, or methylmalonate, hanging drop vapor diffusion method, using 30-34% (w/v) PEG 4000
-
in the presence of the substrate D-3-hydroxybutyrate and the cofactor NAD+ at the optimum pH for the catalytic reaction. At 277 and 293 K using the hanging-drop vapour-diffusion method, to 2.3 A resolution. Structure is isomorphous to that of the complex with the substrate analogue acetate
-
sitting drop vapor diffusion method at 20°C, structure determined at a resolution of 1.8 A in complex with NAD(H)
-
crystals of ternary complex of HBDH-NAD+-L-3-hydroxybutyrate and the binary complex of HBDH-NAD+. The former structure shows a closed-form conformation, which is considered an active form for catalysis, while the latter stays mostly in a open-form conformation. Crystals of mutants T190S and T190A
-
hanging-drop vapor-diffusion method, ligand-free enzyme and enzyme-NAD+ complex, 2.0 A resolution
-
hanging-drop vapour-diffusion method using PEG 3000 as a precipitating agent. The crystals belong to the orthorhombic group P2(1)2(1)2, with unit-cell parameters a = 64.3, b = 99.0, c = 110.2 A. The crystals are most likely to contain two tetrameric subunits in the asymmetric unit
Q5KST5
hanging drop vapour diffusion method with 17-20% polyethylene glycol 1500, 0.1 M Tris-HCl, pH 7.1, 0.2 mM CaCl2 and 10 mM acetoacetate; recombinant enzyme, hanging drop vapor diffusion method, 0.003 ml of HBDH, 10 mg/ml, is mixed with an equal volume of crystallization buffer containing 17-20% PEG 1500, 0.1 M Tris-HCl, pH 7.1, 0.2 mM CaCl2, and 10 mM acetoacetate, room temperature/22°C, three different crystal forms, X-ray diffraction structure determination and analysis at resolutions between 1.9 and 2.1 A
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 37
-
stable at, 30% remaining activity after 40 min at 37°C, oxidation reaction
0 - 45
-
stable at 0°C and 25°C for 90 min, 18% activity after 90 min at 45°C, activity restored after 60 min at 37°C, loss of activity at 60°C
37
37
-
loss of 70% activity after 15 min, 0.24 mg protein/ml, Ca2+ and Mn2+ stabilize enzyme
37
-
75% activity after 30 min in buffer containing 1 mM Ca2+, 46% with 1 mM MnCl2
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme with an N-terminal His-tag has approximately 1200fold higher catalytic efficiency than its C-terminal counterpart and exhibits higher catalytic efficiency for levulinic acid than the C-terminal
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 mg enzyme/ml, 0.2 mM potassium phosphate pH 8.0, 10% glycerol, 10 mM 2-mercaptoethanol, 6 months, 0% inactivation, 0°C, 0.1 mg enzyme/ml, 1 day, 50% inactivation
-
-20°C, 20 mM phosphate buffer, pH 7.0, 20% glycerol
-20°C, crude extract, partially purified enzyme, several weeks, 0% inactivation
-
-20°C, several months, 0%, 4°C, lyophilized, 2 month, 0% inactivation, 4°C, 0.1 M sodium phosphate buffer pH 7-8, 5 days, 50% inactivation, stability increases in the presence of 1-10 mM EDTA
-
4°C, Tris-HCl buffer, 50-100 mM Mg2+, Mn2+, Ba2+, or Ca2+, enzyme loses all activity in the presence of phosphate buffer or EDTA within 2 min
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
about 1000fold, to homogeneity from liver mitochondrial membranes by solubilization with Triton X-100, DEAE-ion-exchange chromatography and phenyl-resin chromatography
-
ammonium sulfate, DEAE-Sepharose, 60°C, 10 min, hydroxylapatite, octyl-Sepharose, Sephadex G-200, DEAE-Sepharose
-
BDH3 partially purified from bdh2 mutant by three steps of column chromatography. Gene product of bdh3 expressed in Escherichia coli purified with 100% yield by two steps of column chromatography
charge-controlled hydrophobic chromatography and Sephadex G-100 gel filtration
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DEAE-cellulose, Matrex gel blue A, Sephadex G-200, chromatofocusing
-
native by 3 chromatographic steps, recombinant from Escherichia coli in 2chromatographic steps
native enzyme by ammonium sulfate fractionation and affinity chromatography
-
phospholipase A2 treatment, controlled-pore glass beads
protamine sulfate precipitation, Sephacryl S-400, S200, DEAE-Sepharose
-
recombinant C-terminally His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
-
recombinant enzyme from Escherichia coli strain DH1 by anion exchange chromatography, hydrophobic interaction chromatography using a gradient of 1-20% ammonium sulfate, and ultrafiltration
-
wild-type and mutants purified by metal chelating affinity chromatography followed by ion-exchange chromatography
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
BDH3 expressed in Escherichia coli BLR (DE3)/pLysS harboring pETT13
DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21(DE3)
enzyme expression in Escherichia coli strain XL-1 Blue; expressed in Escherichia coli XL1-Blue cells
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli; expression in Escherichia coli
expression of C-terminally His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
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functional co-expression with acetoacetyl-CoA thiolase and PHB synthase in Escherichia coli, recombinant production of poly(3-hydroxybutanoate) granules, overview
-
wild-type and mutants expressed in Escherichia coli XL1Blue harbouring pHBDH11. Wild-type HBDH and mutants containing an N-terminal His-tag expressed in Escherichia coli XL1Blue using pQE30 as a vector
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H144A
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144F
-
the mutant shows increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H144I
-
the mutant shows increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L
H144L/W187A
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L/W187F
H144L/W187I
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L/W187L
-
the mutant shows strongly increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L/W187V
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144V
-
the mutant shows wild type catalytic efficiency with levulinic acid
W187A
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
W187F
W187I
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
W187L
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
W187V
-
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
H144A
-
catalytic efficiency (kcat/Km) is 0.2% of the activity of wild-type HBDH
L215A
-
both Km and kcat values are largely affected and the catalytic efficiency (kcat/Km) is less than 3% that of the wild-type enzyme
L215V
-
Km values increase 3.5- and 4.3fold and the kcat values are 73-118% those of the wild-type toward D-3-hydroxybutyrate and acetoacetate, respectively. Mutation does not significantly change Km and kcat toward NAD+ and NADH
Q94A
-
catalytic efficiency (kcat/Km) is 1.4% of the activity of wild-type HBDH
W187F
-
shows significant activity levels, 65% that of the wild-type enzyme
W187Y
-
shows significant activity levels, 41% that of the wild-type enzyme
H141A
K149R
-
kcat/KM for (R)-3-hydroxybutanoate is 184.2fold lower than wild-type value, kcat/Km for NAD+ is 7.2fold lower than wild-type enzyme
Q193A
-
kcat/KM for (R)-3-hydroxybutanoate is 307fold lower than wild-type value, kcat/Km for NAD+ is 6.2fold lower than wild-type enzyme
Q91A
additional information
H144L
-
the mutant shows increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H144L/W187F
-
site-directed mutagenesis, the mutant shows activity with levulinnic acid, in contrast to the wild-type enzyme, and is engineered for production of 4-hydroxyvaleric acid, molecular docking simulation, overview
H144L/W187F
-
the mutant shows strongly increased catalytic efficiency with levulinic acid compared to the wild type enzyme
W187F
-
the mutant shows increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H141A
-
kcat/KM for (R)-3-hydroxybutanoate is 184.2fold lower than wild-type value, kcat/Km for NAD+ is 12.9fold lower than wild-type enzyme
Q91A
-
kcat/KM for (R)-3-hydroxybutanoate is 83.7fold lower than wild-type value, kcat/Km for NAD+ is 2.8fold lower than wild-type enzyme
additional information
the bdh1 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH1 causes a decline in the capacity to neutralize the stress; the bdh2 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH2 causes a decline in the capacity to neutralize the stress
additional information
the bdh1 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH1 causes a decline in the capacity to neutralize the stress; the bdh2 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH2 causes a decline in the capacity to neutralize the stress
additional information
the bdh1 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH1 causes a decline in the capacity to neutralize the stress; the bdh2 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH2 causes a decline in the capacity to neutralize the stress
additional information
-
the bdh1 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH1 causes a decline in the capacity to neutralize the stress; the bdh2 mutant lags behind the wild-type in growth rates when the cells are cultured with 3-hydroxybutyrate, citrate, succinate, or nutrient broth. A test of sensitivity to diamide as an oxidative stress reveals that the lack of BDH2 causes a decline in the capacity to neutralize the stress
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
the enzyme is a useful marker in the assay of diabetes mellitus and/or ketoacidosis
synthesis
-
the engineered enzyme mutant H144L/W187F is used for production of 4-hydroxyvaleric acid, a monomer of bio-polyester and a precursor of bio-fuels, from levulinic acid
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