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(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 + NAD+
acetoacetate + NADH
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
(R)-3-hydroxybutanoate + NADH + H+
acetoacetate + NAD+
(R)-3-hydroxybutanoate + NADP+
acetoacetate + NADPH
activity with NADP+ is 2% of the activity with NAD+
-
-
?
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
2-hydroxypropansulfonate + NAD+
acetonylsulfonate + NADH
-
-
-
r
2-methyl-3-hydroxybutyrate + NAD+
2-methylacetoacetate + NADH
-
-
-
r
3-hydroxyvalerate + NAD+
3-oxovalerate + NADH + H+
4-hydroxybutanoate + NAD+
acetoacetate + NADH
-
isoenzyme from heavy mitochondria shows 40% lower activity than enzyme fromlight mitochondria
-
-
?
acetoacetate + NADH + H+
(R)-3-hydroxybutanoate + NAD+
-
-
-
?
D-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
L-threonine + NAD+
?
-
-
-
?
levulinic acid + NADH + H+
4-hydroxyvaleric acid + NAD+
poly-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
additional information
?
-
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(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
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
-
?
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
-
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)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
-
r
(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 + NAD+
acetoacetate + NADH + H+
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
-
r
(R)-3-hydroxybutanoate + NAD+
acetoacetate + NADH + H+
-
-
-
-
r
(R)-3-hydroxybutanoate + NADH + H+
acetoacetate + NAD+
-
-
-
-
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+
-
-
-
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+
-
-
-
-
r
(R)-3-hydroxybutyrate + NAD+
acetoacetate + NADH + H+
-
-
-
-
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+
-
-
-
-
?
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+
-
-
-
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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(DL)-2-hydroxybutyrate
-
5 mM, pH 8.5, 25°, 69% inhibition
(DL)-lactate
-
5 mM, pH 8.5, 25°C, 65% inhibition
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
2-Hydroxybutyrate
-
10 mM, 57% inhibition
2-oxobutyrate
-
10 mM, 29% inhibition
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
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.15 mM, 63% inhibition
acetoacetyl-CoA
-
1 mM, 29% inhibition
acetyl-CoA
-
1 mM, 82% inhibition
acetylphosphonate
-
16.7 mM, pH 7, 28% inhibition
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
crotonate
-
10 mM, 20% inhibition
CuSO4
-
1 mM, 81% inhibition
D-lactate
-
5 mM, pH 8.5, 25°, 85% inhibition, uncompetitive vs. coenzyme, competitive vs. substrate
diazenedicarboxylic acid bis(dimethylamide)
dimethyl phosphate
-
16.7 mM, pH 7, 12% inhibition
dimethyloxyphosphinylacetate
-
competitive inhibitor vs. acetoacetate
EDTA
inhibition and destabilization of the enzyme at 10 mM
glucose
inhibits the enzyme when contained in the growth medium
Hg2+
inhibition at 1 mM, and destabilization at 10 mM
KCl
-
80-100 mM, 50% inhibition
LiCl
-
80-100 mM, 50% inhibition
methanephosphonic acid
-
3.3 mM, pH 7, 11% inhibition
methyl methylphosphonate
-
3.3 mM, pH 7, 13% inhibition
methyl phosphate
-
16.7 mM, pH 7, 21% inhibition
Methyl-2-methoxyphosphinylacetate
-
competitive inhibitor vs. acetoacetate
MnCl2
-
1 mM, 50% inhibition
NaCl
-
80-100 mM, 50% inhibition
NAD+
-
substrate inhibition, high concentrations, noncompetitive vs. beta-hydroxybutyrate
NH4Cl
-
80-100 mM, 50% inhibition
oxalate
-
16.7 mM, pH 7, 9% inhibition
Phenylarsine oxide
-
NAD+ and NADH protect against inhibition
propionate
-
5 mM, pH 8.5, 25°C, 9% inhibition
sodium acetonylphosphonate
-
3.3 mM, pH 7, 21% inhibition
sodium monomethyl acetylphosphonate
-
16.7 mM, pH 7, 60% inhibition
sodium monomethylacetonylphosphate
-
16.7 mM, pH 7, 30% inhibition
Sodium sulfide
-
competitive vs. beta-hydroxybutyrate
sodium sulfite
-
uncompetitive vs. NAD+ and acetoacetate, competitive vs. beta-hydroxybutyrate
succinate
-
10 mM, 12% inhibition
Zn2+
inhibition and destabilization of the enzyme at 10 mM
acetoacetate
-
substrate inhibition, above 5 mM, noncompetitive vs. NADH
acetoacetate
-
inhibition above 1 mM, 2 mM, 89% inhibition
bromomalonate
-
-
Butyrate
-
5 mM, pH 8.5, 25°C, 22% inhibition
Butyrate
-
10 mM, 20% inhibition
chloromalonate
-
-
diazenedicarboxylic acid bis(dimethylamide)
-
0.20 mM, activity can be recovered with dithiothreitol, enzyme contains a vicinal dithiol that is oxidized by diamide
diazenedicarboxylic acid bis(dimethylamide)
-
NAD+ protects against inhibition
dimethylmalonate
-
15.3 mM, 50% inhibition, oxidation, 11.3% reduction
dimethylmalonate
-
7.6 mM, 50% inhibition, oxidation, 8.5 mM, reduction
HgCl2
-
enzyme extremely sensitive, NADH and Ca2+ protect
HgCl2
-
0.1 mM, 100% inhibition
Hydroxymalonate
-
4.8 mM, 50% inhibition, oxidation, 7.8 reduction
Hydroxymalonate
-
1.8 mM, 50% inhibition, oxidation, 6.0 mM, reduction
L-3-hydroxybutyrate
-
5 mM, pH 8.5, 25°C, 23% inhibition; 5 mM, pH 8.5, 25°C, 32% inhibition
L-3-hydroxybutyrate
is a competitive inhibitor
L-3-hydroxybutyrate
-
5 mM, 73% inhibition
malonate
-
malonate
-
9.5 mM, 50% inhibition, oxidation, 8.2 mM
malonate
-
3.7 mM, 50% inhibition, oxidation
malonate
-
10 mM, 66% inhibition, oxidation
mesoxalate
-
-
methylmalonate
-
methylmalonate
-
2.1 mM, 50% inhibition, oxidation
methylmalonate
-
1.4 mM, 50% inhibition, oxidation, 0.8 mM reduction
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
N-ethylmaleimide
-
irreversible inhibition
N-ethylmaleimide
-
NAD+ protects against inhibition
NADH
-
competitive vs. NAD+
NADH
-
substrate inhibition, above 0.1 mM, competitive vs. acetoacetate
NADH
-
0.15 mM, 48% inhibition
p-chloromercuribenzoate
-
0.001 mM, extremely rapid inhibition, NAD+ and NADH protect against inhibition
p-chloromercuribenzoate
-
enzyme extremely sensitive, NADH and Ca2+ protect
p-chloromercuribenzoate
-
0.1 mM, 100% inhibition
Phenylglyoxal
-
extremely rapid inhibition
pyruvate
-
16.7 mM, pH 7.0, 22% inhibition
pyruvate
-
4 mM, 5% inhibition
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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.
Iron Deficiencies
3-Hydroxybutyrate dehydrogenase-2 and ferritin-H synergistically regulate intracellular iron.
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
Beta-hydroxybutyrate dehydrogenase activity in liver and liver tumors.
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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0.0391 - 290
(R)-3-hydroxybutanoate
0.45 - 2
(R)-3-hydroxybutyrate
0.28
3-acetylpyridine adenine dinucleotide
-
-
0.00547 - 32
acetoacetate
0.34 - 100
D-3-hydroxybutyrate
0.63 - 42.1
levulinic acid
additional information
additional information
-
0.0391
(R)-3-hydroxybutanoate
-
-
0.32
(R)-3-hydroxybutanoate
-
-
0.34
(R)-3-hydroxybutanoate
30°C
0.49
(R)-3-hydroxybutanoate
30°C
0.59
(R)-3-hydroxybutanoate
-
submitochondrial vesicles
0.6
(R)-3-hydroxybutanoate
wild type enzyme
0.71
(R)-3-hydroxybutanoate
-
enzyme expressed in SF9 cells
0.8
(R)-3-hydroxybutanoate
-
-
0.866
(R)-3-hydroxybutanoate
-
liver, soluble enzyme
0.866
(R)-3-hydroxybutanoate
-
liver-soluble enzyme, at pH 8.1 and 30°C
1.05
(R)-3-hydroxybutanoate
-
heart 3-hydroxybutyrate dehydrogenase
1.2
(R)-3-hydroxybutanoate
-
1.32
(R)-3-hydroxybutanoate
-
liver 3-hydroxybutyrate dehydrogenase
1.5
(R)-3-hydroxybutanoate
23°C, pH 8.0, wild-type enzyme
1.586
(R)-3-hydroxybutanoate
-
heart, soluble enzyme
1.586
(R)-3-hydroxybutanoate
-
heart-soluble enzyme, at pH 8.1 and 30°C
1.6
(R)-3-hydroxybutanoate
-
pH 8.0, 25°C
1.6
(R)-3-hydroxybutanoate
-
isoenzyme from heavy mitochondria
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
2.3
(R)-3-hydroxybutanoate
-
-
2.3
(R)-3-hydroxybutanoate
-
-
3.36
(R)-3-hydroxybutanoate
-
isoenzyme from light mitochondria
4
(R)-3-hydroxybutanoate
mutant enzyme H141A
7.4
(R)-3-hydroxybutanoate
-
-
9.1
(R)-3-hydroxybutanoate
-
30°C, pH 9.0
10
(R)-3-hydroxybutanoate
-
enzyme expressed in SF9 cells, C242S mutant, C242 important for substrate binding
10.5
(R)-3-hydroxybutanoate
-
25°C, pH 9.0
12.6
(R)-3-hydroxybutanoate
-
25°C, pH 7.5
21
(R)-3-hydroxybutanoate
-
cyanylated enzyme
35
(R)-3-hydroxybutanoate
23°C, pH 8.0, mutant enzyme H141A
51
(R)-3-hydroxybutanoate
mutant enzyme Q91A
70
(R)-3-hydroxybutanoate
mutant enzyme Q133A
78
(R)-3-hydroxybutanoate
23°C, pH 8.0, mutant enzyme K149R
96
(R)-3-hydroxybutanoate
23°C, pH 8.0, mutant enzyme Q193A
131
(R)-3-hydroxybutanoate
23°C, pH 8.0, mutant enzyme Q91A
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
0.45
(R)-3-hydroxybutyrate
oxidation reaction, pH 8.5, 55°C
0.633
(R)-3-hydroxybutyrate
-
euthermic state, liver
1.07
(R)-3-hydroxybutyrate
-
pH 8.1, 37°C
2
(R)-3-hydroxybutyrate
-
euthermic state, brain
0.00547
acetoacetate
-
-
0.146
acetoacetate
-
euthermic state, brain
0.149
acetoacetate
-
liver, soluble enzyme
0.15
acetoacetate
-
euthermic state, liver
0.17
acetoacetate
recombinant enzyme with N-terminal His-tag, at pH 6.5 and 30°C
0.24
acetoacetate
reduction reaction, pH 5.0, 55°C
0.29
acetoacetate
-
pH 7.0, 37°C
0.312
acetoacetate
-
heart, soluble enzyme
0.37
acetoacetate
wild-type
1.1
acetoacetate
mutant T190S
1.3
acetoacetate
mutant L215V
7.7
acetoacetate
mutant T190C
8.3
acetoacetate
mutant L215A
8.7
acetoacetate
-
cyanylated enzyme
10.47
acetoacetate
recombinant enzyme with C-terminal His-tag, at pH 6.5 and 30°C
32
acetoacetate
mutant T190A
0.34
D-3-hydroxybutyrate
-
0.49
D-3-hydroxybutyrate
-
0.5
D-3-hydroxybutyrate
-
0.8
D-3-hydroxybutyrate
wild-type
0.88
D-3-hydroxybutyrate
H6-HBDH
1.2
D-3-hydroxybutyrate
mutant H6-W187Y
1.3
D-3-hydroxybutyrate
mutant H6-W187F
3.4
D-3-hydroxybutyrate
mutant L215V
3.7
D-3-hydroxybutyrate
mutant T190S
9.2
D-3-hydroxybutyrate
mutant L215A
25
D-3-hydroxybutyrate
mutant H6-H144A
25
D-3-hydroxybutyrate
mutant T190A
30
D-3-hydroxybutyrate
mutant H6-Q94A
31
D-3-hydroxybutyrate
mutant H6-K152R
36
D-3-hydroxybutyrate
mutant T190C
47
D-3-hydroxybutyrate
mutant H6-Q196A
51
D-3-hydroxybutyrate
mutant H6-Q196N
61
D-3-hydroxybutyrate
mutant H6-W257A
65
D-3-hydroxybutyrate
mutant H6-W257Y
83
D-3-hydroxybutyrate
mutant H6-Q196E
83
D-3-hydroxybutyrate
mutant H6-W257F
84
D-3-hydroxybutyrate
mutant H6-W187T
100
D-3-hydroxybutyrate
mutant H6-W187A
0.63
levulinic acid
mutant enzyme H144L/W187L, at pH 6.5 and 30°C
0.63
levulinic acid
mutant enzyme W187F, 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
wild type enzyme, 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
mutant enzyme H144L, 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
1.72
levulinic acid
mutant enzyme H144F, at pH 6.5 and 30°C
2.81
levulinic acid
mutant enzyme H144I, at pH 6.5 and 30°C
3.84
levulinic acid
mutant enzyme H144V, at pH 6.5 and 30°C
4 - 5.4
levulinic acid
mutant enzyme W187I, 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
9.87
levulinic acid
mutant enzyme H144A, at pH 6.5 and 30°C
13.03
levulinic acid
mutant enzyme H144L/W187A, at pH 6.5 and 30°C
13.49
levulinic acid
mutant enzyme W187L, 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
36.83
levulinic acid
mutant enzyme W187A, at pH 6.5 and 30°C
42.1
levulinic acid
mutant enzyme W187V, at pH 6.5 and 30°C
0.000445
NAD+
-
-
0.0598
NAD+
-
25°C, pH 9.0
0.067
NAD+
-
heart, soluble enzyme
0.071
NAD+
-
liver, soluble enzyme
0.089
NAD+
oxidation reaction, pH 8.5, 55°C
0.12
NAD+
mutant H6-K152R
0.12
NAD+
mutant H6-Q196A
0.12
NAD+
mutant H6-Q196E
0.18
NAD+
23°C, pH 8.0, wild-type enzyme
0.21
NAD+
-
isoenzyme from heavy mitochondria
0.21
NAD+
mutant H6-W187Y
0.238
NAD+
-
euthermic state, liver
0.24
NAD+
-
liver 3-hydroxybutyrate dehydrogenase
0.24
NAD+
mutant H6-W187F
0.27
NAD+
-
240 mM Na+, purified enzyme, reconstituted with total mitochondrial phospholipids
0.27
NAD+
23°C, pH 8.0, mutant enzyme Q193A
0.28
NAD+
23°C, pH 8.0, mutant enzyme H141A
0.35
NAD+
mutant H6-H144A
0.36
NAD+
-
heart 3-hydroxybutyrate dehydrogenase
0.38
NAD+
23°C, pH 8.0, mutant enzyme K149R
0.39
NAD+
-
isoenzyme from light mitochondria
0.49
NAD+
mutant H6-W257F
0.51
NAD+
23°C, pH 8.0, mutant enzyme Q91A
0.53
NAD+
-
enzyme expressed in SF9 cells
0.74
NAD+
mutant H6-W257Y
0.76
NAD+
mutant H6-W187A
0.8
NAD+
-
enzyme expressed in SF9 cells, C242S mutant
0.88
NAD+
mutant H6-W187T
0.902
NAD+
-
cyanylated enzyme
0.95
NAD+
-
submitochondrial vesicles
0.95
NAD+
mutant H6-W257A
1.187
NAD+
-
euthermic state, brain
0.00102
NADH
-
-
0.014
NADH
-
liver, soluble enzyme
0.029
NADH
-
heart, soluble enzyme
0.029
NADH
reduction reaction, pH 5.0, 55°C
0.058
NADH
-
euthermic state, brain
0.074
NADH
-
euthermic state, liver
0.164
NADH
-
cyanylated enzyme
additional information
additional information
-
dissociation constants
-
additional information
additional information
-
dissociation constants for the cofactors and reaction kinetics at different physiological states in liver and brain
-
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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/W187A
the mutant shows reduced catalytic efficiency with levulinic acid compared to the wild type enzyme
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
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
C242S
-
PCR derived cDNA clone
M92V
-
PCR derived cDNA clone
S24T
-
PCR derived cDNA clone
H144A
catalytic efficiency (kcat/Km) is 0.2% of the activity of wild-type HBDH
K152R
retains a significant level of activity
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
Q196A
kcat/Km value is 0.6% that of the wild-type
Q196E
substantially reduced activity
Q196N
substantially reduced activity
Q94A
catalytic efficiency (kcat/Km) is 1.4% of the activity of wild-type HBDH
T190A
activity decreases to 0.1% that of the wild-type enzyme
T190S
retains 37% of the activity
W187F
shows significant activity levels, 65% that of the wild-type enzyme
W187T
shows faint activity
W187Y
shows significant activity levels, 41% that of the wild-type enzyme
W257F
shows low activity levels, 2% that of the wild-type enzyme
W257Y
shows low activity levels, 1% that of the wild-type enzyme
K149A
inactive mutant enzyme
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
H144L
the mutant shows activity with levulinic acid
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 activity with levulinic acid
H144L/W187F
the mutant shows strongly increased catalytic efficiency with levulinic acid compared to the wild type enzyme
W187F
the mutant shows activity with levulinic acid
W187F
the mutant shows increased catalytic efficiency with levulinic acid compared to the wild type enzyme
H141A
strongly decreased activity
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
decreased activity
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
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 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
-
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Loeb-Hennard, C.; McIntyre, J.O.
(R)-3-Hydroxybutyrate dehydrogenase: selective phosphatidylcholine binding by the C-terminal domain
Biochemistry
39
11929-11938
2000
Homo sapiens
-
brenda
Green, D.; Marks, a.R.; Fleischer, S.; McIntyre, J.O.
Wild type and mutant human heart (R)-3-hydroxybutyrate dehydrogenase expressed in insect cells
Biochemistry
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1996
Bos taurus, Homo sapiens
brenda
Klein, K.; Rudy, B.; McIntyre, J.O.; Fleischer, S.; Trommer, W.E.
Specific interaction of(R)-3-hydroxybutyrate dehydrogenase with membrane phosphatidylcholine as studied by ESR spectroscopy in oriented phospholipid multilayers: coenzyme binding enhances the interaction with phosphatidylcholine
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1996
Bos taurus
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Szewczyk, E.; Rozolska, M.
Occurence, purification and properties of the staphylococcal beta-hydroxybutyrate dehydrogenase
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1994
Staphylococcus xylosus
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Adam, Pascal; Duncan, T.M.; McIntyre, J.O.; Carter, C.E.; Fu, C.; Melin, M.; Latruffe, N.; Fleischer, S.
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Bos taurus
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Dutra, J.C.; Dutra-Filho, C.S.; Cardozo, S.E.C.; Wannmacher, C.M.D.; Sarkis, J.J.F.; Wajner, M.
Inhibition of succinate dehydrogenase and beta-hydroxybutyrate dehydrogenase activities by methylmalonate in brain and liver of developing rats
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Molecular cloning and characterization of (R)3-hydroxybutyrate dehydrogenase from human heart
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Homo sapiens
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Bailly, A.; Lone, Y.C.; Latruffe, N.
Post-transcriptional analysis of rat mitochondrial D-3-hydroxybutyrate dehydrogenase control through development and physiological stages
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Rattus norvegicus
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McIntyre, J.O.; Latruffe, N.; Brenner, S.C.; Fleischer, S.
Comparison of 3-hydroxybutyrate dehydrogenase from bovine heart and rat liver mitochondria
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262
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1988
Bos taurus, Rattus norvegicus
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Cortese, J.D.; Fleischer, S.
Noncooperative vs. cooperative reactivation of D-beta-hydroxybutyrate dehydrogenase: multiple equilibria for lecithin binding are determined by the physical state (soluble vs. bilayer) and composition of the phospholipids
Biochemistry
26
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1987
Bos taurus, Rattus norvegicus
brenda
Worral, E.B.; Gassain, S.; Cox, D.J.; Sugden, M.C.; Palmer, T.N.
3-Hydroxyisobutyrate dehydrogenase, an impurity in commercial 3-hydroxybutyrate dehydrogenase
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1987
Cereibacter sphaeroides
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Kovar, J.; Matyskova, I.; Matyska, L.
Kinetics of D-3-hydroxybutyrate dehydrogenase from Paracoccus denitrificans
Biochim. Biophys. Acta
871
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1986
Paracoccus denitrificans
-
brenda
Dubois, H.; Fritsche, T.M.; Trommer, W.E.; McIntyre, J.O.; Fleischer, S.
Cyanylation of 3-hydroxybutyrate dehydrogenase
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367
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1986
Bos taurus
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Matyskova I.; Kovar, J.; Racek, P.
Purification and properties of D-3-hydroxybutyrate dehydrogenase from Paracoccus denitrificans
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Paracoccus denitrificans
-
brenda
Burnett, B.K.; Khorana, H.G.
A rapid and efficient procedure for the purification of mitochondrial beta-hydroxybutyrate dehydrogenase
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Bos taurus
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Phelps, D.C.; Hatefi, Y.
Inhibition of D(-)-beta-hydroxybutyrate dehydrogenase by butanedione, phenylglyoxal, and diethyl pyrocarbonate
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20
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1981
Bos taurus
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MacGill, A.K.; Anderson, N.G.; Trotman, C.N.A.; Carrington, J.M.; Hanson, P.J.
D-3-Hydroxybutyrate dehydrogenase and metabolism of ketone bodies by rat stomach
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-
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Target size of D-beta-hydroxybutyrate dehydrogenase
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258
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Bos taurus
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Scawen, M.D.; Darbyshire, J.; Harvey, M.J.; Atkinson, T.
The rapid purification of 3-hydroxybutyrate dehydrogenase and malate dehydrogenase on triazine dye affinity matrices
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203
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Cereibacter sphaeroides
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Kluger, R.; Tsui, W.C.
Inhibition of bacterial D-3-hydroxybutyrate dehydrogenase by substrates and substrate analogues
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59
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1981
Paucimonas lemoignei
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Miyahara, M.; Utsumi, K.; Deamer, D.W.
Selective interaction of D-beta-hydroxybutyrate dehydrogenase with intracellular membranes
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641
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1981
Rattus norvegicus
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Nakada T.; Fukui, T.; Saito, T.; Miki, K.; Oji, C.; Matsuda, S.; Ushijima, A.; Tomita, K.
Purification and properties of D-beta-hydroxybutyrate dehydrogenase from Zoogloea ramiger I-16-M
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89
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1981
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Phelps, D.C.; Hatefi, Y.
Inhibition of D(-)-beta-hydroxybutyrate dehydrogenase by modifiers of disulfides, thiols, and vicinal dithiols
Biochemistry
20
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1981
Bos taurus
brenda
Tucker, G.A.; Dawson, A.P.
The kinetics of rat liver and heart mitochondria beta-hydroxybutyrate dehydrogenase
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179
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1979
Rattus norvegicus
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Kluger, R.; Nakaoka, K.; Tsui, W.C.
Substrate analogue studies of the specificity and catalytic mechanism of D-3-hydroxybutyrate dehydrogenase
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100
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1978
Paucimonas lemoignei
-
brenda
McIntyre, J.O.; Bock, H.G.O.; Fleischer, S.
The orientation of D-beta-hydroxybutyrate dehydrogenase in the mitochondrial inner membrane
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1978
Bos taurus
brenda
Dhariwal, K.R.; Venkitasubramanian, T.A.
Purification and properties of beta-hydroxybutyrate dehydrogenase from Mycobacterium phlei ATCC354
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104
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1978
Mycolicibacterium phlei
brenda
Tan, A.W.H.; Smith, C.M.; Aogaichi, T.; Plaut, G.W.E.
Inhibition of D(-)-3-hydroxybutyrate dehydrogenase by malonate analoges
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166
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Koyappayil, A.; Chavan, S.; Mohammadniaei, M.; Go, A.; Hwang, S.; Lee, M.
beta-Hydroxybutyrate dehydrogenase decorated MXene nanosheets for the amperometric determination of beta-hydroxybutyrate
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Paucimonas lemoignei
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