H9408
β-Hydroxybutyrate Dehydrogenase from Pseudomonas lemoignei
lyophilized powder, ≥200 units/mg protein
Synonym(s):
(R)-3-Hydroxybutanoate:NAD+ oxidoreductase, 3-HBDH
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
≥200 units/mg protein
Biological source:
bacterial (Pseudomonas lemoignei)
biological source
bacterial (Pseudomonas lemoignei)
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
Quality Level
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
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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)
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)
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)
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
Michel A Sciotti et al.
Chimia, 64(11), 793-798 (2011-01-05)
Gamma hydroxybutyric acid (GHB) is a regulated therapeutic drug, which naturally occurs in mammalian brain tissues as an intermediate of the GABA (gamma aminobutyric acid) neurotransmitter metabolism. The increasing misuse of GHB as a narcotic or abusing drug in recent
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