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Literature summary extracted from

  • Bunik, V.; Brand, M.
    Generation of superoxide and hydrogen peroxide by side reactions of mitochondrial 2-oxoacid dehydrogenase complexes in isolation and in cells (2018), Biol. Chem., 399, 407-420 .
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.2.1.25 mitochondrion
-
 Mus musculus 5739
-
1.2.1.25 mitochondrion
-
 Saccharomyces cerevisiae 5739
-
1.2.1.25 mitochondrion
-
 Bos taurus 5739
-
1.2.1.25 mitochondrion
-
 Homo sapiens 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.1.25 3-methyl-2-oxobutanoate + CoA + NAD+ Homo sapiens
-
 2-methylpropanoyl-CoA + CO2 + NADH
-
 ir
1.2.1.25 3-methyl-2-oxobutanoate + CoA + NAD+ Mus musculus
-
 2-methylpropanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 3-methyl-2-oxobutanoate + CoA + NAD+ Saccharomyces cerevisiae
-
 2-methylpropanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 3-methyl-2-oxobutanoate + CoA + NAD+ Bos taurus
-
 2-methylpropanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 3-methyl-2-oxopentanoate + CoA + NAD+ Homo sapiens
-
 2-methylbutanoyl-CoA + CO2 + NADH
-
 ir
1.2.1.25 3-methyl-2-oxopentanoate + CoA + NAD+ Mus musculus
-
 2-methylbutanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 3-methyl-2-oxopentanoate + CoA + NAD+ Saccharomyces cerevisiae
-
 2-methylbutanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 3-methyl-2-oxopentanoate + CoA + NAD+ Bos taurus
-
 2-methylbutanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 4-methyl-2-oxopentanoate + CoA + NAD+ Homo sapiens
-
 3-methylbutanoyl-CoA + CO2 + NADH
-
 ir
1.2.1.25 4-methyl-2-oxopentanoate + CoA + NAD+ Mus musculus
-
 3-methylbutanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 4-methyl-2-oxopentanoate + CoA + NAD+ Saccharomyces cerevisiae
-
 3-methylbutanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 4-methyl-2-oxopentanoate + CoA + NAD+ Bos taurus
-
 3-methylbutanoyl-CoA + CO2 + NADH + H+
-
 ir

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.25 Bos taurus
-
-
-
1.2.1.25 Homo sapiens P12694 AND P21953 alpha and beta subunits of complex component E1 (BCKD), a tetramer (alpha2beta2), cf. EC 1.2.4.4
-
1.2.1.25 Mus musculus
-
-
-
1.2.1.25 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.25 3-methyl-2-oxobutanoate + CoA + NAD+
-
 Homo sapiens 2-methylpropanoyl-CoA + CO2 + NADH
-
 ir
1.2.1.25 3-methyl-2-oxobutanoate + CoA + NAD+
-
 Mus musculus 2-methylpropanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 3-methyl-2-oxobutanoate + CoA + NAD+
-
 Saccharomyces cerevisiae 2-methylpropanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 3-methyl-2-oxobutanoate + CoA + NAD+
-
 Bos taurus 2-methylpropanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 3-methyl-2-oxopentanoate + CoA + NAD+
-
 Homo sapiens 2-methylbutanoyl-CoA + CO2 + NADH
-
 ir
1.2.1.25 3-methyl-2-oxopentanoate + CoA + NAD+
-
 Mus musculus 2-methylbutanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 3-methyl-2-oxopentanoate + CoA + NAD+
-
 Saccharomyces cerevisiae 2-methylbutanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 3-methyl-2-oxopentanoate + CoA + NAD+
-
 Bos taurus 2-methylbutanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 4-methyl-2-oxopentanoate + CoA + NAD+
-
 Homo sapiens 3-methylbutanoyl-CoA + CO2 + NADH
-
 ir
1.2.1.25 4-methyl-2-oxopentanoate + CoA + NAD+
-
 Mus musculus 3-methylbutanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 4-methyl-2-oxopentanoate + CoA + NAD+
-
 Saccharomyces cerevisiae 3-methylbutanoyl-CoA + CO2 + NADH + H+
-
 ir
1.2.1.25 4-methyl-2-oxopentanoate + CoA + NAD+
-
 Bos taurus 3-methylbutanoyl-CoA + CO2 + NADH + H+
-
 ir

Subunits

EC Number Subunits Comment Organism
1.2.1.25 More E2 components form oligomeric cores of the complexes, to which peripheral E1 and E3 bind Mus musculus
1.2.1.25 More E2 components form oligomeric cores of the complexes, to which peripheral E1 and E3 bind Saccharomyces cerevisiae
1.2.1.25 More E2 components form oligomeric cores of the complexes, to which peripheral E1 and E3 bind Bos taurus
1.2.1.25 More E2 components form oligomeric cores of the complexes, to which peripheral E1 and E3 bind Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.2.1.25 More cf. EC 1.2.4.4 Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.25 CoA
-
 Mus musculus
1.2.1.25 CoA
-
 Saccharomyces cerevisiae
1.2.1.25 CoA
-
 Bos taurus
1.2.1.25 CoA
-
 Homo sapiens
1.2.1.25 NAD+
-
 Mus musculus
1.2.1.25 NAD+
-
 Saccharomyces cerevisiae
1.2.1.25 NAD+
-
 Bos taurus
1.2.1.25 NAD+
-
 Homo sapiens
1.2.1.25 thiamine diphosphate active site bound Saccharomyces cerevisiae

General Information

EC Number General Information Comment Organism
1.2.1.25 additional information anaerobic radical intermediate of E1-bound active aldehyde has been trapped by 5,5-dimethyl-1-pyrroline N-oxide (DMPO), which can serve as an artificial substrate-acceptor in the reaction Mus musculus
1.2.1.25 additional information anaerobic radical intermediate of E1-bound active aldehyde has been trapped by 5,5-dimethyl-1-pyrroline N-oxide (DMPO), which can serve as an artificial substrate-acceptor in the reaction Saccharomyces cerevisiae
1.2.1.25 additional information anaerobic radical intermediate of E1-bound active aldehyde has been trapped by 5,5-dimethyl-1-pyrroline N-oxide (DMPO), which can serve as an artificial substrate-acceptor in the reaction Bos taurus
1.2.1.25 additional information anaerobic radical intermediate of E1-bound active aldehyde has been trapped by 5,5-dimethyl-1-pyrroline N-oxide (DMPO), which can serve as an artificial substrate-acceptor in the reaction Homo sapiens
1.2.1.25 physiological function mitochondrial 2-oxoacid dehydrogenase complexes oxidize 2-oxoglutarate, pyruvate, branched-chain 2-oxoacids and 2-oxoadipate to the corresponding acyl-CoAs and reduce NAD+ to NADH. The isolated enzyme complexes generate superoxide anion radical or hydrogen peroxide in defined reactions by leaking electrons to oxygen. But the 2-oxoacid dehydrogenase complexes contribute little to the production of superoxide or hydrogen peroxide relative to other mitochondrial sites at physiological steady-states. The contributions may increase under pathological conditions, in accordance with the high maximum capacities of superoxide or hydrogen peroxide-generating reactions of the complexes, established in isolated mitochondria. The complexes consist of multiple copies of three catalytic components (E1, E2 and E3). The first step of the overall complex reaction is catalyzed by the appropriate 2-oxoacid specific 2-oxoacid dehydrogenase (E1). Employing the diphosphorylated derivative of vitamin B1, ThDP, the E1 components decarboxylate 2-oxoacids to the first reaction product CO2 and ThDP-bound active aldehydes. The decarboxylation reaction is followed by the reductive acylation of the E1 substrate-acceptor, the lipoyl-comprising domain of the second component (E2) of the complexes. E1-catalyzed reaction releasing CO2 is irreversible, and has specific significance in the regulation of the overall process. Formation of the active aldehyde after decarboxylation of an adduct of a 2-oxoacid with thiamine diphosphate in the active site of E1 is a pre-requisite for the ROS-generating reactions by the E1 component and for the physiological reduction of the complex-bound dihydrolipoyl residues, participating in the forward direction of ROS generation by the complexes, overview. The dehydrogenase components E1 and E3 catalyze generation of superoxide and/or hydrogen peroxide in both the isolated and complex-bound state, albeit to different degrees Mus musculus
1.2.1.25 physiological function mitochondrial 2-oxoacid dehydrogenase complexes oxidize 2-oxoglutarate, pyruvate, branched-chain 2-oxoacids and 2-oxoadipate to the corresponding acyl-CoAs and reduce NAD+ to NADH. The isolated enzyme complexes generate superoxide anion radical or hydrogen peroxide in defined reactions by leaking electrons to oxygen. But the 2-oxoacid dehydrogenase complexes contribute little to the production of superoxide or hydrogen peroxide relative to other mitochondrial sites at physiological steady-states. The contributions may increase under pathological conditions, in accordance with the high maximum capacities of superoxide or hydrogen peroxide-generating reactions of the complexes, established in isolated mitochondria. The complexes consist of multiple copies of three catalytic components (E1, E2 and E3). The first step of the overall complex reaction is catalyzed by the appropriate 2-oxoacid specific 2-oxoacid dehydrogenase (E1). Employing the diphosphorylated derivative of vitamin B1, ThDP, the E1 components decarboxylate 2-oxoacids to the first reaction product CO2 and ThDP-bound active aldehydes. The decarboxylation reaction is followed by the reductive acylation of the E1 substrate-acceptor, the lipoyl-comprising domain of the second component (E2) of the complexes. E1-catalyzed reaction releasing CO2 is irreversible, and has specific significance in the regulation of the overall process. Formation of the active aldehyde after decarboxylation of an adduct of a 2-oxoacid with thiamine diphosphate in the active site of E1 is a pre-requisite for the ROS-generating reactions by the E1 component and for the physiological reduction of the complex-bound dihydrolipoyl residues, participating in the forward direction of ROS generation by the complexes, overview. The dehydrogenase components E1 and E3 catalyze generation of superoxide and/or hydrogen peroxide in both the isolated and complex-bound state, albeit to different degrees Saccharomyces cerevisiae
1.2.1.25 physiological function mitochondrial 2-oxoacid dehydrogenase complexes oxidize 2-oxoglutarate, pyruvate, branched-chain 2-oxoacids and 2-oxoadipate to the corresponding acyl-CoAs and reduce NAD+ to NADH. The isolated enzyme complexes generate superoxide anion radical or hydrogen peroxide in defined reactions by leaking electrons to oxygen. But the 2-oxoacid dehydrogenase complexes contribute little to the production of superoxide or hydrogen peroxide relative to other mitochondrial sites at physiological steady-states. The contributions may increase under pathological conditions, in accordance with the high maximum capacities of superoxide or hydrogen peroxide-generating reactions of the complexes, established in isolated mitochondria. The complexes consist of multiple copies of three catalytic components (E1, E2 and E3). The first step of the overall complex reaction is catalyzed by the appropriate 2-oxoacid specific 2-oxoacid dehydrogenase (E1). Employing the diphosphorylated derivative of vitamin B1, ThDP, the E1 components decarboxylate 2-oxoacids to the first reaction product CO2 and ThDP-bound active aldehydes. The decarboxylation reaction is followed by the reductive acylation of the E1 substrate-acceptor, the lipoyl-comprising domain of the second component (E2) of the complexes. E1-catalyzed reaction releasing CO2 is irreversible, and has specific significance in the regulation of the overall process. Formation of the active aldehyde after decarboxylation of an adduct of a 2-oxoacid with thiamine diphosphate in the active site of E1 is a pre-requisite for the ROS-generating reactions by the E1 component and for the physiological reduction of the complex-bound dihydrolipoyl residues, participating in the forward direction of ROS generation by the complexes, overview. The dehydrogenase components E1 and E3 catalyze generation of superoxide and/or hydrogen peroxide in both the isolated and complex-bound state, albeit to different degrees Bos taurus
1.2.1.25 physiological function mitochondrial 2-oxoacid dehydrogenase complexes oxidize 2-oxoglutarate, pyruvate, branched-chain 2-oxoacids and 2-oxoadipate to the corresponding acyl-CoAs and reduce NAD+ to NADH. The isolated enzyme complexes generate superoxide anion radical or hydrogen peroxide in defined reactions by leaking electrons to oxygen. But the 2-oxoacid dehydrogenase complexes contribute little to the production of superoxide or hydrogen peroxide relative to other mitochondrial sites at physiological steady-states. The contributions may increase under pathological conditions, in accordance with the high maximum capacities of superoxide or hydrogen peroxide-generating reactions of the complexes, established in isolated mitochondria. The complexes consist of multiple copies of three catalytic components (E1, E2 and E3). The first step of the overall complex reaction is catalyzed by the appropriate 2-oxoacid specific 2-oxoacid dehydrogenase (E1). Employing the diphosphorylated derivative of vitamin B1, ThDP, the E1 components decarboxylate 2-oxoacids to the first reaction product CO2 and ThDP-bound active aldehydes. The decarboxylation reaction is followed by the reductive acylation of the E1 substrate-acceptor, the lipoyl-comprising domain of the second component (E2) of the complexes. E1-catalyzed reaction releasing CO2 is irreversible, and has specific significance in the regulation of the overall process. Formation of the active aldehyde after decarboxylation of an adduct of a 2-oxoacid with thiamine diphosphate in the active site of E1 is a pre-requisite for the ROS-generating reactions by the E1 component and for the physiological reduction of the complex-bound dihydrolipoyl residues, participating in the forward direction of ROS generation by the complexes, overview. The dehydrogenase components E1 and E3 catalyze generation of superoxide and/or hydrogen peroxide in both the isolated and complex-bound state, albeit to different degrees Homo sapiens