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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
biological source
bacterial (Pseudomonas lemoignei)
Quality Level
form
lyophilized powder
specific activity
≥200 units/mg protein
purified by
chromatography
foreign activity
lactic dehydrogenase ≤0.05%
malic dehydrogenase ≤0.1%
storage temp.
−20°C
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General description
D-β-hydroxybutyrate dehydrogenase (BDH) is a membrane bound lipid-requiring enzyme.
Application
β-Hydroxybutyrate Dehydrogenase from Pseudomonas lemoignei has been used in coupled assay to confirm the formation of acetoacetate.
Suitable for the determination of acetoacetate and D(-)-3-hydroxybutyrate by the method of Williamson, D. H., and Mellanby, J., Methods of Enzymatic Analysis, Bergmeyer, H., ed., 2nd edition, 4, 1836 (1974).
Biochem/physiol Actions
In Paracoccus denitrificans, 3-hydroxybutyrate dehydrogenase plays a key role in the degradation of intracellular polyhydroxybutyrate and polyhydroxyvalerate.
In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle).
Physical form
lyophilized powder containing sucrose, β-NAD and Tris buffer salts
Other Notes
One unit will oxidize 1.0 μmole of D-β-hydroxybutyrate to acetoacetate per min at pH 7.8 at 37 °C.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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The specific molecular architecture of plant 3-hydroxy-3-methylglutaryl-CoA lyase
Hemmerlin A, et al.
The Journal of biological chemistry, 80(3) (2019)
D-beta-HYDROXYBUTYRATE DEHYDROGENASE: A MOLECULAR BIOLOGY APPROACH TO THE STUDY OF A LIPID-REQUIRING ENZYME
Structure and Function of Membrane Proteins, 283-300 (1983)
3-Hydroxybutyrate oligomer hydrolase and 3-hydroxybutyrate dehydrogenase participate in intracellular polyhydroxybutyrate and polyhydroxyvalerate degradation in Paracoccus denitrificans
Lu J, et al.
Applied and Environmental Microbiology, 80(3), 986-993 (2014)
W Hugo Ramos-Vera et al.
Journal of bacteriology, 193(5), 1201-1211 (2010-12-21)
Two autotrophic carbon fixation cycles have been identified in Crenarchaeota. The dicarboxylate/4-hydroxybutyrate cycle functions in anaerobic or microaerobic autotrophic members of the Thermoproteales and Desulfurococcales. The 3-hydroxypropionate/4-hydroxybutyrate cycle occurs in aerobic autotrophic Sulfolobales; a similar cycle may operate in autotrophic
J Nie et al.
Scandinavian journal of medicine & science in sports, 21(5), 625-629 (2010-05-13)
This study examined the response of serum biomarkers of cardiac and skeletal muscle damage at rest and after a routine workout of 21 km run in 12 male adolescent (16.2±0.6 years) long-distance runners. Biomarkers of cardiac [troponins (cTnT, cTnI), creatine
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