K1502
α-Ketoglutarate Dehydrogenase from porcine heart
buffered aqueous glycerol solution, 0.1-1.0 units/mg protein (Lowry)
Sinónimos:
Multienzyme 2-oxoglutarate dehydrogenase complex
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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
Specific activity:
0.1-1.0 units/mg protein (Lowry)
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Permítanos ayudarleform
buffered aqueous glycerol solution
specific activity
0.1-1.0 units/mg protein (Lowry)
foreign activity
pyruvate dehydrogenase ≤20%
shipped in
dry ice
storage temp.
−20°C
Quality Level
General description
Research Area: Neuroscience
α-Ketoglutarate dehydrogenase (α-KGDH) is a multienzyme complex localized to the mitochondria. This integrated enzyme is made up of many units of thiamine pyrophosphate-dependent dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3), and dihydrolipoamide succinyl transferase (E2).
α-Ketoglutarate dehydrogenase (α-KGDH) is a multienzyme complex localized to the mitochondria. This integrated enzyme is made up of many units of thiamine pyrophosphate-dependent dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3), and dihydrolipoamide succinyl transferase (E2).
Application
α-Ketoglutarate Dehydrogenase from the porcine heart has been used:
- to study the reversal of nitration by glutathione (GSH) in peroxynitrite-treated cells
- to measure its activity by Spectramax M5 microplate spectrofluorimeter using heart mitochondria
- as a positive control to evaluate its activity in by Spectramax GEMINI EM fluorescence microplate reader using mice neurons
Biochem/physiol Actions
α-Ketoglutarate dehydrogenase (α-KGDH) is a key enzyme of bioenergetic processes and a controlling unit of metabolic flux through the Krebs cycle or tricarboxylic acid (TCA) cycle. It catalyzes the oxidative decarboxylation of α-ketoglutarate (KG) to succinyl-CoA by releasing reduced nicotinamide adenine dinucleotide (NADH). It is the rate-limiting reaction of the TCA cycle. This reaction contributes to the electrons of the respiratory chain and requires thiamine pyrophosphate as a cofactor. The reduction of NAD (nicotinamide adenine dinucleotide) is observed to determine its reaction rate. α-KGDH from porcine has an optimum pH range of 6.6–7.4. This enzyme is inhibited by oxidative stress and results in a metabolic deficiency. However, α-KGDH is also known to produce reactive oxygen species (ROS) leading to oxidative stress. Defective or limited levels of α-KGDH cause several neurodegenerative diseases such as Alzheimer′s disease.
α-Ketoglutarate dehydrogenase is most responsive to alterations in the tumor microenvironment and contributes to the adaptive metabolic response in cancer. Inhibiting α-ketoglutarate dehydrogenase counteracts lung metastasis associated with breast cancer.
Physical form
Supplied as a 50% glycerol solution containing ~9 mg per mL bovine serum albumin, 30% sucrose, 1.5 mM EDTA, 1.5 mM EGTA, 1.5 mM 2-mercaptoethanol, 0.3% TRITON™ X-100, 0.003% sodium azide, and 15 mM potassium phosphate, pH 6.8.
Analysis Note
May contain traces of polyethylene glycol.
Other Notes
One unit will convert 1.0 μmole of β-NAD to β-NADH per min at pH 7.4 at 30 °C in the presence of saturating levels of coenzyme A.
Legal Information
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow
hcodes
pcodes
Hazard Classifications
Aquatic Chronic 3
Clase de almacenamiento
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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alpha-ketoglutarate dehydrogenase inhibition counteracts breast cancer-associated lung metastasis
Atlante S, et al.
Cell Death & Disease, 9(7), 756-756 (2018)
Shuyi Zhang et al.
Science (New York, N.Y.), 334(6062), 1551-1553 (2011-12-17)
It is generally accepted that cyanobacteria have an incomplete tricarboxylic acid (TCA) cycle because they lack 2-oxoglutarate dehydrogenase and thus cannot convert 2-oxoglutarate to succinyl-coenzyme A (CoA). Genes encoding a novel 2-oxoglutarate decarboxylase and succinic semialdehyde dehydrogenase were identified in
Wagner L Araújo et al.
The Plant cell, 24(6), 2328-2351 (2012-07-04)
Transgenic tomato (Solanum lycopersicum) plants expressing a fragment of the gene encoding the E1 subunit of the 2-oxoglutarate dehydrogenase complex in the antisense orientation and exhibiting substantial reductions in the activity of this enzyme exhibit a considerably reduced rate of
Qingli Shi et al.
The Journal of biological chemistry, 286(20), 17640-17648 (2011-04-02)
Reduced brain metabolism is an invariant feature of Alzheimer Disease (AD) that is highly correlated to the decline in brain functions. Decreased activities of key tricarboxylic acid cycle (TCA) cycle enzymes may underlie this abnormality and are highly correlated to
João Leandro et al.
ACS chemical biology, 15(8), 2041-2047 (2020-07-08)
DHTKD1 is the E1 component of the 2-oxoadipate dehydrogenase complex, which is an enzyme involved in the catabolism of (hydroxy-)lysine and tryptophan. Mutations in DHTKD1 have been associated with 2-aminoadipic and 2-oxoadipic aciduria, Charcot-Marie-Tooth disease type 2Q and eosinophilic esophagitis
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