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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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H9408-25UN

$418.00

H9408-50UN

$803.00

H9408-100UN

$1,250.00

$418.00


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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

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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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1 of 4

This Item
H8509L3888H1506
biological source

bacterial (Pseudomonas lemoignei)

biological source

-

biological source

bacterial (Lactobacillus leichmannii)

biological source

bacterial (Pseudomonas testosteroni)

specific activity

≥200 units/mg protein

specific activity

250-750 units/mg protein

specific activity

150-500 units/mg protein

specific activity

≥15 units/mg protein

form

lyophilized powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized solid

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

foreign activity

lactic dehydrogenase ≤0.05%, malic dehydrogenase ≤0.1%

foreign activity

lactate dehydrogenase ≤0.05%, malate dehydrogenase ≤0.1%

foreign activity

Malic dehydrogenase <0.5% of base activity

foreign activity

β-hydroxysteroid dehydrogenase ≤0.5%, alcohol dehydrogenase ≤0.05%

purified by

chromatography

purified by

chromatography

purified by

-

purified by

chromatography

General description

D-β-hydroxybutyrate dehydrogenase (BDH) is a membrane bound lipid-requiring enzyme.[1]

Application

β-Hydroxybutyrate Dehydrogenase from Pseudomonas lemoignei has been used in coupled assay to confirm the formation of acetoacetate.[2]
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.[3]
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_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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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)
The specific molecular architecture of plant 3-hydroxy-3-methylglutaryl-CoA lyase
Hemmerlin A, et al.
The Journal of biological chemistry, 80(3) (2019)
Tina D Shah et al.
Molecular and biochemical parasitology, 179(2), 100-106 (2011-07-20)
A putative β-hydroxybutyrate dehydrogenase (βHBDH) ortholog was identified in Trypanosoma brucei, the unicellular eukaryotic parasite responsible for causing African Sleeping Sickness. The trypanosome enzyme has greater sequence similarity to bacterial sources of soluble βHBDH than to membrane-bound Type I βHBDH
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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