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Information on EC 1.1.1.30 - 3-hydroxybutyrate dehydrogenase
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1.1.1.30 3-hydroxybutyrate dehydrogenaseIUBMB Comments
Also oxidizes other 3-hydroxymonocarboxylic acids.
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Word Map
- 1.1.1.30
- ketone
- succinate
- acetoacetate
-
lipid-requiring
- lecithin
- acetoacetyl-coa
-
thiolase
-
coa-transferase
- alpha-glycerophosphate
-
submitochondrial
-
3-oxoacid
-
ketogenesis
-
ketogenic
-
enzyme-phospholipid
- synthesis
- diagnostics
The enzyme appears in viruses and cellular organisms
Synonyms
beta-hydroxybutyrate dehydrogenase, 3-hydroxybutyrate dehydrogenase, d-beta-hydroxybutyrate dehydrogenase, d-3-hydroxybutyrate dehydrogenase, beta-hydroxybutyric dehydrogenase, dhrs6, beta-hydroxybutyric acid dehydrogenase, 3-hbdh, 3-hydroxybutyrate dehydrogenase-2, 3hbdh, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3HBDH
BDH
BDH1
BDH2
BDH3
BdhA
beta-hydroxybutyrate dehydrogenase
D-(-)-3-hydroxybutyrate dehydrogenase
D-3-hydroxybutyrate dehydrogenase
D-beta-hydroxybutyrate dehydrogenase
HBD
HBDH
additional information
additional information
-
the enzyme belongs to the family of short-chain dehydrogenases/reductases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+
-
-
-
-
(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+
enzyme is completely dependent on the presence of phospholipid for activity
-
(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
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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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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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
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
-
?
acetoacetate + NADH + H+
(R)-3-hydroxybutanoate + NAD+
-
-
?
(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 SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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
acetoacetate + NADH + H+
(R)-3-hydroxybutanoate + NAD+
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
-
?
(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
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+
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
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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Mn2+
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INHIBITOR
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
-
-
286513, 286516, 286517, 286521, 286525, 286527, 286528, 286530, 286535, 286538, 286540, 286542, 286543
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
-
-
phosphatidylcholine
-
state of phosphatidylcholine determines nature of activation, noncooperative for soluble phosphatidylcholine, cooperative for bilayer 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
-
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
-
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
-
additional information
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
-
additional information
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
-
additional information
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
-
additional information
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
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
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Brain Neoplasms
The calorically restricted ketogenic diet, an effective alternative therapy for malignant brain cancer.
Carcinoma
Monitoring by alpha-hydroxybutyrate dehydrogenase of human ovarian carcinoma grown in nude mice.
Carcinoma, Hepatocellular
Immunochemical analysis of the membrane proteins of rat liver and Zajdela hepatoma mitochondria.
Carcinoma, Hepatocellular
Regulation of D-beta-hydroxybutyrate dehydrogenase in rat hepatoma cell lines.
Carcinoma, Hepatocellular
[Activity of the beta-hydroxybutyric dehydrogenase of mitochondria of ascitic hepatoma and of the normal rat liver.]
Cardiomegaly
Cardiac hypertrophy in spontaneously hypertensive rats. Ultrastructural cytochemistry of beta-hydroxybutyrate dehydrogenase [proceedings]
Cardiomegaly
Proceedings: Cardiac hypertrophy in spontaneously hypertensive rats. I. Chronological changes in the mitochondrial beta-hydroxybutyrate dehydrogenase activity in the myocardium.
Diabetes Mellitus
Metabolic control of the expression of mitochondrial D-beta-hydroxybutyrate dehydrogenase, a ketone body converting enzyme.
Diabetes Mellitus
The effect of spontaneous diabetes mellitus on fatty acid oxidation, beta-hydroxybutyrate dehydrogenase activity and respiratory coupling of hepatic mitochondria in the guinea-pig (Cavia porcellus).
Diabetes Mellitus
The structures of Alcaligenes faecalis D-3-hydroxybutyrate dehydrogenase before and after NAD+ and acetate binding suggest a dynamical reaction mechanism as a member of the SDR family.
Diabetes Mellitus, Experimental
Variations of specific mRNA and polypeptide contents of rat liver D-beta-hydroxybutyrate dehydrogenase during an experimental diabetes mellitus.
Fatty Liver
Deficiency of 3-hydroxybutyrate dehydrogenase (BDH1) in mice causes low ketone body levels and fatty liver during fasting.
Glioma
Differential utilization of ketone bodies by neurons and glioma cell lines: a rationale for ketogenic diet as experimental glioma therapy.
Heart Failure
[Histochemical study of the enzyme activity of the myocardium of sudden death victims with postinfarct cardiosclerosis]
Hutchinson's Melanotic Freckle
Histochemical findings in different types of malignant melanoma: biological and clinical significance.
Hyperthyroidism
Accelerated postnatal development of D(-)- -hydroxybutyrate dehydrogenase (EC 1.1.1.30) activity in the brain in hyperthyroidism.
Hyperthyroidism
Concerning the decreased D-3-hydroxybutyrate dehydrogenase activity in the liver and heart of hyperthyroid rats.
Hyperthyroidism
Differential action of thyroid hormones on the activity of certain enzymes in rat kidney and brain.
Hyperthyroidism
Ketone-body metabolism in hyperthyroid rats: reduced activity of D-3-hydroxybutyrate dehydrogenase in both liver and heart and of succinyl-coenzyme A: 3-oxoacid coenzyme A-transferase in heart.
Hypothyroidism
Mitochondrial oxidative enzyme activity in individual fibre types in hypo- and hyperthyroid rat skeletal muscles.
Hypothyroidism
[Enzymatic and immunologic study of the role of the thyroid hormone in the formation of the internal mitochondrial membrane during postnatal development of the rat]
Infections
Neisseria gonorrhoeae modulates iron-limiting innate immune defenses in macrophages.
Ketosis
Effect of prenatally-induced and postnatally-maintained ketosis on beta-hydroxybutyrate dehydrogenase and hexokinase levels in the developing rat brain.
Ketosis
The structures of Alcaligenes faecalis D-3-hydroxybutyrate dehydrogenase before and after NAD+ and acetate binding suggest a dynamical reaction mechanism as a member of the SDR family.
Melanoma
Histochemical findings in different types of malignant melanoma: biological and clinical significance.
Nasopharyngeal Carcinoma
Inactivation of 3-hydroxybutyrate dehydrogenase type 2 promotes proliferation and metastasis of nasopharyngeal carcinoma by iron retention.
Neoplasm Metastasis
Inactivation of 3-hydroxybutyrate dehydrogenase type 2 promotes proliferation and metastasis of nasopharyngeal carcinoma by iron retention.
Neoplasms
Fatty acid oxidation, substrate shuttles, and activity of the citric acid cycle in hepatocellular carcinomas of varying differentiation.
Neoplasms
Loss of acetoacetate coenzyme A transferase activity in tumours of peripheral tissues.
Neoplasms
Low ketolytic enzyme levels in tumors predict ketogenic diet responses in cancer cell lines in vitro and in vivo.
Neoplasms
Monitoring by alpha-hydroxybutyrate dehydrogenase of human ovarian carcinoma grown in nude mice.
Neoplasms
The calorically restricted ketogenic diet, an effective alternative therapy for malignant brain cancer.
Obesity
Treatment with the 5-HT3 antagonist tropisetron modulates glucose-induced obesity in mice.
Reperfusion Injury
[Transmural differences between damaged cardiomyocytes due to post-ischemic reperfusion and calcium paradox]
Starvation
Activities of some key enzymes of carbohydrate, ketone body, adenosine and glutamine metabolism in liver, and brown and white adipose tissues of the rat.
Starvation
Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.2
(R)-3-hydroxybutanoate
-
240 mM Na+, purified enzyme, reconstituted with total mitochondrial phospholipids
2.2
(R)-3-hydroxybutanoate
-
tetrameric enzyme (BDH-I) reconstituted with mitochondrial phospholipid vesicles, in the presence of 240 mM Na+, at pH 7.4 and 37°C
10
(R)-3-hydroxybutanoate
-
enzyme expressed in SF9 cells, C242S mutant, C242 important for substrate binding
200
(R)-3-hydroxybutanoate
-
240 mM Na+, purified enzyme, thiol group 1 modified with 1,1'-azobis(NN'-dimethylformamide), reconstituted with total mitochondrial phospholipids
200
(R)-3-hydroxybutanoate
-
enzyme form BDH-II, in the presence of 240 mM Na+, at pH 7.4 and 37°C
290
(R)-3-hydroxybutanoate
-
240 mM Na+, purified enzyme, thiol group 2 modified with 1,1'-azobis(NN'-dimethylformamide), reconstituted with total mitochondrial phospholipids
290
(R)-3-hydroxybutanoate
-
enzyme form BDH-III, in the presence of 240 mM Na+, at pH 7.4 and 37°C
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
0.63
levulinic acid
mutant enzyme H144L/W187L, at pH 6.5 and 30°C
0.63
levulinic acid
recombinant mutant enzyme W187F with N-terminal His-tag, at pH 6.5 and 30°C
0.64
levulinic acid
mutant enzyme H144L/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
13.03
levulinic acid
mutant enzyme H144L/W187A, 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
25.57
levulinic acid
mutant enzyme H144L/W187V, at pH 6.5 and 30°C
25.76
levulinic acid
mutant enzyme H144L/W187I, 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
0.00122
levulinic acid
mutant enzyme H144L/W187A, at pH 6.5 and 30°C
0.002
levulinic acid
mutant enzyme H144L/W187V, at pH 6.5 and 30°C
0.00289
levulinic acid
mutant enzyme H144L/W187I, 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
0.07107
levulinic acid
mutant enzyme H144L/W187L, 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
0.2565
levulinic acid
mutant enzyme H144L/W187F, 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
0.016
levulinic acid
mutant enzyme H144L/W187A, at pH 6.5 and 30°C
0.045
levulinic acid
mutant enzyme H144L/W187L, at pH 6.5 and 30°C
0.051
levulinic acid
mutant enzyme H144L/W187V, at pH 6.5 and 30°C
0.074
levulinic acid
mutant enzyme H144L/W187I, at pH 6.5 and 30°C
0.164
levulinic acid
mutant enzyme H144L/W187F, 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
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
145
-
heart 3-hydroxybutyrate dehydrogenase, reconstituted with mitochondrial phospholipids
91
-
liver 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
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
286513, 286514, 286516, 286517, 286521, 286522, 286525, 286527, 286528, 286530, 286535, 286538, 286540, 286542, 286543
-
-
brenda
-
-
-
brenda
enzyme shows hysteresis, lag phase in progress curve
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
-
brenda
additional information
-
the enzyme is localized in poly(3-hydroxybutyrate) granules, co-localization with acetoacetyl-CoA thiolase and PHB synthase, overview
brenda
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
brenda
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
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
-
brenda
-
located on the matrix face of the inner membrane
brenda
-
located on the matrix face of the inner membrane
brenda
-
beta-hydroxybutyrate dehydrogenase from heavy and light mitochondria are isoforms
brenda
-
light and heavy mitochondria, enzyme expression and activity is increased in heavy mitochondria in hibernating state, overview
brenda
-
located on the matrix face of the inner membrane
brenda
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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
enzyme inactivation in developing zebrafish embryo results in heme deficiency and delays erythrocyte maturation
malfunction
inhibiting expression of the 3-hydroxybutyrate dehydrogenase-2 gene results in abnormal accumulation of intracellular iron, increased oxidative stress, and mitochondrial iron deficiency
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
119000
-
reconstituted enzyme, radiation inactivation, irradiation leads to loss of activity and fragmentation
120000
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
additional information
?
x * 27600, calculated from amino acid sequence
?
-
x * 27600, calculated from amino acid sequence
tetramer
-
alpha4, 4 * 38000, preprotein, calculated from deduced amino acid sequence
tetramer
-
alpha4, 4 * 33117, mature protein, calculated from deduced amino acid sequence
additional information
secondary and tertiary enzyme structure analysis, overview
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
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
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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PROTEIN VARIANTS
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
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
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
additional information
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 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 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