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K1502
α-Ketoglutarate Dehydrogenase from porcine heart
buffered aqueous glycerol solution, 0.1-1.0 units/mg protein (Lowry)
Synonym(e):
Multienzyme 2-oxoglutarate dehydrogenase complex
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About This Item
CAS-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
NACRES:
NA.54
Empfohlene Produkte
Form
buffered aqueous glycerol solution
Spezifische Aktivität
0.1-1.0 units/mg protein (Lowry)
Fremdaktivität
pyruvate dehydrogenase ≤20%
Versandbedingung
dry ice
Lagertemp.
−20°C
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Allgemeine Beschreibung
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).
Anwendung
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. Wirkung
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.
Qualität
May contain traces of polyethylene glycol.
Einheitendefinition
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.
Physikalische 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.
Rechtliche Hinweise
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow
H-Sätze
P-Sätze
Gefahreneinstufungen
Aquatic Chronic 3
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Tristan Wagner et al.
Chemistry & biology, 18(8), 1011-1020 (2011-08-27)
The α-ketoglutarate dehydrogenase (KDH) complex is a major regulatory point of aerobic energy metabolism. Mycobacterium tuberculosis was reported to lack KDH activity, and the putative KDH E1o component, α-ketoglutarate decarboxylase (KGD), was instead assigned as a decarboxylase or carboligase. Here
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
Casey L Quinlan et al.
The Journal of biological chemistry, 289(12), 8312-8325 (2014-02-12)
Several flavin-dependent enzymes of the mitochondrial matrix utilize NAD(+) or NADH at about the same operating redox potential as the NADH/NAD(+) pool and comprise the NADH/NAD(+) isopotential enzyme group. Complex I (specifically the flavin, site IF) is often regarded as
Gary E Gibson et al.
Journal of neurochemistry, 134(1), 86-96 (2015-03-17)
Reversible post-translation modifications of proteins are common in all cells and appear to regulate many processes. Nevertheless, the enzyme(s) responsible for the alterations and the significance of the modification are largely unknown. Succinylation of proteins occurs and causes large changes
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