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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About This Item
Número de CAS:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
Productos recomendados
Formulario
buffered aqueous glycerol solution
Nivel de calidad
actividad específica
0.1-1.0 units/mg protein (Lowry)
actividad extraña
pyruvate dehydrogenase ≤20%
Condiciones de envío
dry ice
temp. de almacenamiento
−20°C
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Descripción general
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).
Aplicación
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
Acciones bioquímicas o fisiológicas
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.
Calidad
May contain traces of polyethylene glycol.
Definición de unidad
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.
Forma física
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.
Información legal
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow
Frases de peligro
Consejos de prudencia
Clasificaciones de peligro
Aquatic Chronic 3
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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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
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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
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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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