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9031-02-1

9031-02-1 Structure

9031-02-1 Structure
IdentificationBack Directory
[Name]

ALPHA-KETOGLUTARATE DEHYDROGENASE
[CAS]

9031-02-1
[Synonyms]

α-Ketoglutarate Dehydrogenase
ALPHA-KETOGLUTARATE DEHYDROGENASE
A-ketoglutarate dehydrogenase from*porcine heart
multienzyme 2-oxoglutarate dehydrogenase complex
α-ketoglutarate dehydrogenase from porcine heart
α-Ketoglutarate Dehydrogenase, from porcine heart
alpha-Ketoglutarate Dehydrogenase from porcine heart
MULTIENZYME 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, (1) INCLUDING EC 1.2.4.2
[MDL Number]

MFCD00130490
Chemical PropertiesBack Directory
[storage temp. ]

-20°C
[form ]

buffered aqueous glycerol solution
Safety DataBack Directory
[Hazard statements ]

H412
[Precautionary statements ]

P273-P501
[WGK Germany ]

3
Hazard InformationBack Directory
[Uses]

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

[General Description]

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).
[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.
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