1.2.1.105: 2-oxoglutarate dehydrogenase system
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For detailed information about 2-oxoglutarate dehydrogenase system, go to the full flat file.
Word Map on EC 1.2.1.105
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1.2.1.105
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kgdhc
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dihydrolipoamide
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thiamin
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alpha-ketoacids
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2-oxoadipate
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transsuccinylase
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charcot-marie-tooth
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2-aminoadipic
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medicine
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thiokinase
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glutaryl-coa
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analysis
- 1.2.1.105
- kgdhc
- dihydrolipoamide
- thiamin
- alpha-ketoacids
- 2-oxoadipate
-
transsuccinylase
- charcot-marie-tooth
-
2-aminoadipic
- medicine
- thiokinase
- glutaryl-coa
- analysis
Reaction
Synonyms
2-OGDH2, 2-oxoglutarate dehydrogenase, 2-oxoglutarate dehydrogenase complex, alpha-KDE2, alpha-ketoglutarate dehydrogenase, alpha-ketoglutarate dehydrogenase complex, alpha-KGDH, At3g55410, At5g65750, DHTKD1, dihydrolipoyl succinyltransferase E2, E1a, E1k, E1o, E2, KGDH, KGDHC, More, MPA24.10, ODGH, ODGH1, ODGH2, ODH, OGDC, OGDH, OGDHC, OGDHL, OGHDC-E2, PDHC, SucA, SucB
ECTree
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Application on EC 1.2.1.105 - 2-oxoglutarate dehydrogenase system
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APPLICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
analysis
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sensitive and rapid assay procedures for human mitochondrial the pyruvate dehydrogenase (PDH) complex, the 2-oxoglutarate dehydrogenase (OGDH) complex and their 5 component enzymes, for use with crude tissue extracts
medicine
synthesis
expression of the structural genes for all three subunits of the Escherichia coli 2-oxoglutarate dehydrogenase complex in Saccharomyces cerevisiae. The Escherichia coli lipoic-acid scavenging enzyme is coexpressed to enable cytosolic lipoylation of the complex, which is required for its enzymatic activity. In vivo cytosolic activity of the complex is tested byconstructing a reporter strain in which the essential metabolite 5-aminolevulinic acid can only be synthetized from cytosolic, and not mitochondrial, succinyl-CoA. In the resulting strain, complementation of 5-aminolevulinic acid auxotrophy depends on activation of the 2-oxoglutarate dehydrogenase complex by lipoic acid addition
additional information
medicine
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altered in the post-mortem substantia nigra samples from patients suffering from Parkinson's disease, decreased activity in the brain of Alzheimer's disease patients, involving regions affected by the disease as well as regions that remain normal, reduced activity or increased vulnerability to oxidative stress in fibroblasts from patients with presenlilin-1 mutation
medicine
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hypochlorous acid and chloramines have the potential to inactivate KGDHC, a major target in neurodegeneration
medicine
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hypochlorous acid and chloramines have the potential to inactivate KGDHC, a major target in neurodegeneration, without significant loss of cellular viability
medicine
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key regulatory branch points of mitochondrial metabolism are targets of a cellular derivative of phytanic acid, decreased activity of the complexes may contribute to neurological symptoms upon accumulation of phytanic acid in Refsum disease
medicine
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KGDHC is diminished in brains from patients with Alzheimers's disease, Parkinson's disease, Huntington's disease, Wernicke-Korskoff disease, and progressive supranuclear palsy, not diminished in brains of patients that died with schizophrenia, reduced KDGDHC may be a better indicator of the primary reactive oxygen species action than commonly used measures of oxidative stress
medicine
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loss of KGDHC activity resulting from the lack of thiamine diphosphate coenzyme may lead to oxidative stress and to neuronal death both directly and by predisposing to other insults
medicine
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potential of succinyl phosphonate esters for modeling the biochemical and pathophysiological consequences of reduced KGDHC activity in brain diseases
medicine
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succinyl phosphonate and its esters may be useful in studying the effects of reduced KGDHC activity on neuronal and brain function
medicine
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succinyl phosphonate and its esters may be useful in studying the effects of reduced KGDHC activity on neuronal and brain function
medicine
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susceptibility of KGDHC to inactivation in kidney cells exposed to cisplatin metabolites my be due to the proximity of mitochondrial aspartate aminotransferase to KGDHC in mitochondria, mitochondrial aspartate aminotransferase may catalyze a beta-lyase reaction with the cisplatin-cysteine S-conjugate, converting cisplatin to a toxicant
additional information
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alpha-ketoglutarate-involving reactions belong to the backbone of high-flux reactions, which is rather conserved in evolution
additional information
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in post-mortem mice brain samples the activity is quickly lost, whereas the activity of another TPP-dependent enzyme, PDH, remains unalterd for at least 24 h
