1.2.1.105: 2-oxoglutarate dehydrogenase system
This is an abbreviated version!
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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Metals Ions
Metals Ions on EC 1.2.1.105 - 2-oxoglutarate dehydrogenase system
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Ca2+
Mg2+
Mn2+
additional information
Ca2+
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Ca2+ and Mg2+ together synergistically reduce the Km-value for 2-oxoglutarate by over 10fold
Ca2+
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0.01 mM, decreases the concentration of 2-oxoglutarate required for half-maximal activity, inhibition at higher concentrations
Ca2+
K0.5 value in absence of NADH is 0.00013 mM, in presence of NADH is 0.00781 mM. Component E1 has two potential Ca2+ -binding sites, site 1 (D114ADLD) and site 2 (E139SDLD). A mutated form of E1, D114A, shows a 6-fold decrease in sensitivity for Ca2+ ,whereas variantx02site1 (sequence of site 1 is replaced by A114AALA) exhibits an almost complete loss of Ca2+ activation. A variant in site2 (sequence is replaced with A139SALA) shows no measurable change in Ca2+ sensitivity
Ca2+
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diminishes the Km value of the 2-oxoglutarate dehydrogenase complex for 2-oxoglutarate in the physiological range, maximal activation, 35%, with 0.004 mM Ca2+
Ca2+
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3.5 mol of Ca2+-binding sites per mol of 2-oxoglutarate dehydrogenase complex
additional information
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the enzyme shows an optimum activity at 0.1 M ionic strength. Increase in ionic strength from 0.1 M to 0.2 M results in a decrease of S0.5 for 2-oxoglutarate, and in an increase of S0.5 for NAD. Changes in ionic strength over the range of 0.05-0.2 M have little, if any, effect on S0.5 for CoA