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Key Documents

K1502

Sigma-Aldrich

α-Ketoglutarate Dehydrogenase from porcine heart

buffered aqueous glycerol solution, 0.1-1.0 units/mg protein (Lowry)

Synonyme(s) :

Multienzyme 2-oxoglutarate dehydrogenase complex

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Forme

buffered aqueous glycerol solution

Niveau de qualité

Activité spécifique

0.1-1.0 units/mg protein (Lowry)

Activité étrangère

pyruvate dehydrogenase ≤20%

Conditions d'expédition

dry ice

Température de stockage

−20°C

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Description générale

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

Actions biochimiques/physiologiques

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.

Qualité

May contain traces of polyethylene glycol.

Définition de l'unité

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.

Forme physique

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.

Informations légales

Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow

Mentions de danger

Conseils de prudence

Classification des risques

Aquatic Chronic 3

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

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


Listes réglementaires

Les listes réglementaires sont principalement fournies pour les produits chimiques. Seules des informations limitées peuvent être fournies ici pour les produits non chimiques. L'absence d'indication signifie qu'aucun des composants n'est répertorié. Il incombe à l'utilisateur de s'assurer de l'utilisation sûre et légale du produit.

EU REACH SVHC Candidate List

CAS No.

EU REACH Annex XIV (Authorisation List)

CAS No.

Certificats d'analyse (COA)

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Les clients ont également consulté

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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
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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