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2-oxo-3-methylvalerate + CoA + NAD+
?
2-oxo-4-methylthiobutanoate + NAD+ + CoA
3-methylthiopropionyl-CoA + NADH + CO2
2-oxo-isocaproate + acyl-CoA + NAD+
?
2-oxo-isocaproate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
2-oxo-isocaproate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
?
-
overall reaction of the recombinant branched-chain alpha-keto acid dehydrogenase multienzyme complex BCKADH
-
-
?
2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(propanoyl)dihydrolipoyllysine + CO2
2-oxoglutarate + CoA + NAD+
3-carboxypropionyl-CoA + NADH + CO2
-
-
-
-
?
2-oxoglutarate + NAD+ + CoA
3-carboxypropionyl-CoA + NADH + CO2
2-oxoisocaproate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH + H+
-
-
-
-
?
2-oxoisovalerate + 2,6-dichlorophenol indophenol
? + CO2
-
-
-
-
?
2-oxoisovalerate + 2,6-dichlorophenolindophenol + CoA
? + CO2 + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
2-oxoisovalerate + acyl-CoA + NAD+
isobutyrate + CO2 + CoA + NADH + H+
2-oxoisovalerate + NAD+
?
-
-
-
-
?
2-oxoisovalerate + NAD+
? + NADH
-
-
-
-
?
2-oxoisovalerate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase] lipoyllysine
?
-
-
-
-
?
2-oxoisovalerate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
?
-
overall reaction of the recombinant branched-chain alpha-keto acid dehydrogenase multienzyme complex BCKADH
-
-
?
2-oxoisovalerate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
? + CO2
-
-
-
-
?
2-oxoisovalerate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-butanoyl-dihydrolipoyllysine + CO2
-
overall reaction of the branched-chain alpha-keto acid dehydrogenase multienzyme complex BCKADH
-
-
?
2-oxopentanoate + NAD+ + CoA
butanoyl-CoA + CO2 + NADH
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
4-methyl-2-oxopentanoate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH
4-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(3-methylbutanoyl)dihydrolipoyllysine + CO2
acyl-E1b-thiamine diphosphate + lipoyl-[lipoic acid-bearing domain]
2-oxo-acyl-S-lipoyl-[lipoic acid-bearing domain] + E1b-thiamine diphosphate
-
reductive acylation of lipoyl-LBD
-
-
?
alpha-keto-beta-methylvaleric acid + NADH
?
-
-
-
-
?
alpha-ketoisocaproic acid + NADH
?
-
-
-
-
?
alpha-ketoisovaleric acid + NADH
?
-
-
-
-
?
E1b-thiamine diphosphate + 2-oxo-acid
E1b-thiamine diphosphate-acyl + CO2
-
decarboxylation, His146beta' and His291alpha are involved
-
-
?
lipoic acid + CoA + NAD+
?
-
-
-
-
?
pyruvate + NAD+ + CoA
acetyl-CoA + CO2 + NADH
additional information
?
-
2-oxo-3-methylvalerate + CoA + NAD+
?
-
-
-
-
?
2-oxo-3-methylvalerate + CoA + NAD+
?
-
-
-
-
?
2-oxo-4-methylthiobutanoate + NAD+ + CoA
3-methylthiopropionyl-CoA + NADH + CO2
-
-
-
-
?
2-oxo-4-methylthiobutanoate + NAD+ + CoA
3-methylthiopropionyl-CoA + NADH + CO2
-
-
-
-
?
2-oxo-4-methylthiobutanoate + NAD+ + CoA
3-methylthiopropionyl-CoA + NADH + CO2
-
38% of the activity with 3-methyl-2-oxobutanoate
-
-
?
2-oxo-isocaproate + acyl-CoA + NAD+
?
-
-
-
-
?
2-oxo-isocaproate + acyl-CoA + NAD+
?
-
-
-
-
?
2-oxo-isocaproate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
2-oxo-isocaproate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(propanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(propanoyl)dihydrolipoyllysine + CO2
-
50% of the activity with 3-methyl-2-oxobutanoate
-
-
?
2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(propanoyl)dihydrolipoyllysine + CO2
-
2-oxobutanoate
-
-
?
2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(propanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(propanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(propanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(propanoyl)dihydrolipoyllysine + CO2
-
20% of the activity with 3-methyl-2-oxobutanoate
-
-
?
2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(propanoyl)dihydrolipoyllysine + CO2
-
2-oxobutanoate
-
-
?
2-oxoglutarate + NAD+ + CoA
3-carboxypropionyl-CoA + NADH + CO2
-
poor substrate
-
-
?
2-oxoglutarate + NAD+ + CoA
3-carboxypropionyl-CoA + NADH + CO2
-
no activity
-
-
?
2-oxoglutarate + NAD+ + CoA
3-carboxypropionyl-CoA + NADH + CO2
-
-
-
-
?
2-oxoisovalerate + acyl-CoA + NAD+
isobutyrate + CO2 + CoA + NADH + H+
-
-
-
-
?
2-oxoisovalerate + acyl-CoA + NAD+
isobutyrate + CO2 + CoA + NADH + H+
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
r
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
-
-
-
-
r
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
D-3-methyl-2-oxopentanoate and L-3-methyl-2-oxopentanoate
-
-
?
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
38% of the activity with 3-methyl-2-oxobutanoate
-
-
?
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
?
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
r
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
r
4-methyl-2-oxopentanoate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH
-
-
-
-
?
4-methyl-2-oxopentanoate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH
-
-
-
?
4-methyl-2-oxopentanoate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH
-
-
-
-
?
4-methyl-2-oxopentanoate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH
-
-
-
-
?
4-methyl-2-oxopentanoate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH
-
-
-
-
?
4-methyl-2-oxopentanoate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH
-
-
-
-
?
4-methyl-2-oxopentanoate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH
-
38% of the activity with 3-methyl-2-oxobutanoate
-
-
?
4-methyl-2-oxopentanoate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH
-
-
-
-
?
4-methyl-2-oxopentanoate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH
-
-
-
?
4-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(3-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
r
4-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue(2-methylpropanoyl)transferase]-lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(3-methylbutanoyl)dihydrolipoyllysine + CO2
-
-
-
-
r
pyruvate + NAD+ + CoA
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + NAD+ + CoA
acetyl-CoA + CO2 + NADH
-
20% of the activity with 3-methyl-2-oxobutanoate
-
-
?
pyruvate + NAD+ + CoA
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + NAD+ + CoA
acetyl-CoA + CO2 + NADH
-
poor substrate
-
-
?
pyruvate + NAD+ + CoA
acetyl-CoA + CO2 + NADH
-
no activity
-
-
?
pyruvate + NAD+ + CoA
acetyl-CoA + CO2 + NADH
-
-
-
-
?
pyruvate + NAD+ + CoA
acetyl-CoA + CO2 + NADH
-
-
-
-
?
additional information
?
-
-
enzyme probably is identical with EC 1.2.1.25
-
-
?
additional information
?
-
-
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1(thiamine diphosphate)-C(OH)CHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
-
-
?
additional information
?
-
-
the enzyme complex is regulated by reversible phosphorylation, complex is inactive in the phosphorylated form and active in the dephosphorylated form
-
-
?
additional information
?
-
-
regulation of the enzyme complex by phosphorylation and dephosphorylation
-
-
?
additional information
?
-
-
the activity of the multienzyme complex is regulated by reversible phosphorylation of the alpha-subunit of the E1 component, EC 1.2.4.4.
-
-
?
additional information
?
-
-
regulation by phosphorylation-dephosphorylation
-
-
?
additional information
?
-
-
enzyme is involved in the catabolism of branched-chain 2-oxo acids
-
-
?
additional information
?
-
-
patients with type IA maple syrup urine disease show missense mutations in the E1 alpha-subunit resulting in the loss of E1 and branched-chain ketoacid dehydrogenase activity
-
-
?
additional information
?
-
-
thiamine increases the specific activity of the human liver enzyme complex
-
-
?
additional information
?
-
-
branched-chain alpha-ketoacid dehydrogenase multienzyme complex BCKDC which is regulated by phosphorylation of component E1b, residue Ser292 of the alpha-domain, in response to hormone and dietary stimuli, phosphorylation induces a conformational change of E1b phosphorylation loop which prevents binding of the E2b component, thiamine diphosphate and His291alpha are involved, overview
-
-
?
additional information
?
-
-
enzyme-deficiency leads to inherited marple syrup urine disease MSUD
-
-
?
additional information
?
-
-
the lipoic acid-bearing domain of enzyme complex component E2 plays a central role in substrate channeling in the mitochondrial multienzyme complex
-
-
?
additional information
?
-
-
E1 and E2 components of the complex act in tandem, the lipoic acid-bearing domain plays an important role in substrate channeling in oxidative decarboxylation of the branched chain alpha-ketoacids within the dehydrogenase multienzyme complex
-
-
?
additional information
?
-
-
multistep reaction of the enzyme complex, overview
-
-
?
additional information
?
-
-
overall reaction
-
-
?
additional information
?
-
-
the overall reaction proceeds in several steps of the components E1, E2, and E3, overview, conformation of the conserved phosphorylation loop, carrying 2 phosphorylation sites Ser292alpha andSer302alpha, is essential for recognition of lipoylated LBD to initiate E1b-catalyzed reductive acylation, E1b is regulated by reversible phosphorylation through the kinase of the multienzyme complex
-
-
?
additional information
?
-
-
flux-generating step for branched-chain amino acid catabolism
-
-
?
additional information
?
-
-
branched-chain alpha-keto acid dehydrogenase complex is essentially devoid of the constituent dihydrolipoamide dehydrogenase component (E3). The absence of E3 is associated with the low affinity of the subunit-binding domain of human BCKDC for hE3
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
enzyme probably is identical with EC 1.2.1.25
-
-
?
additional information
?
-
-
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1(thiamine diphosphate)-C(OH)CHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
-
-
?
additional information
?
-
-
regulation by phosphorylation-dephosphorylation
-
-
?
additional information
?
-
-
starvation causes a significant decrease in activity in maternal tissues
-
-
?
additional information
?
-
-
enzyme complex is induced by growth on branched-chain amino acid or keto acid and repressed by growth in the presence of glucose or ammonium ion
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
enzyme probably is identical with EC 1.2.1.25
-
-
?
additional information
?
-
-
the multienzyme complex catalyzes a thiamine diphosphate- and Mg2+-dependent oxidative decarboxylation of branched-chain keto acids with the formation of branched-chain acyl-CoA and reduction of NAD+ to NADH: R1R2CHCOCOOH + NAD+ + CoASH = R1R2CHCO-S-CoA + NADH + CO2, component E1 (EC 1.2.4.4, branched-chain keto acid dehydrogenase), component E2 (no EC number, branched-chain acyltransferase), component E3 (EC 1.8.1.4, dihydrolipoamide dehydrogenase), partial reactions catalyzed by the multienzyme complex: 1. R1R2CHCOCOOH + E1-(thiamine diphosphate) = E1-(thiamine diphosphate)-COHCHR1R2 + CO2, 2. E1(thiamine diphosphate)-C(OH)CHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
-
-
?
additional information
?
-
-
the intramitochondrial pyruvate dehydrogenase complex and the branched-chain 2-oxo acid dehydrogenase complex are responsible for the oxidative decarboxylation of 2-oxobutanoate, the branched-chain 2-oxo acid dehydrogenase complex is probably the more important complex
-
-
?
additional information
?
-
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the enzyme can be regulated by an endogenous protein kinase
-
-
?
additional information
?
-
-
high-protein diet increases the enzyme concentration in rat liver, protein-free diet decreases enzyme concentration in rat liver
-
-
?
additional information
?
-
-
enzyme regulates the catabolism of branched-chain amino acids, and is regulated by phosphorylation-dephosphorylation
-
-
?
additional information
?
-
does not interact with human mitochondrial branched-chain aminotransferase isozymes
-
-
?
additional information
?
-
-
the enzyme catalyzes a reaction of branched-chain amino acid catabolism which constitutes a crucial step to provide fatty acid precursors for antibiotic biosynthesis
-
-
?
additional information
?
-
-
decarboxylation and acylation reaction proceeds in 4 reaction steps in the enzyme complex, involving the cofactor thiamine diphosphate and the lipoic acid-bearing domain of component E2, E1 undergoes an open-closed conformational change upon formation of the enzyme-substrate complex, overview
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?
additional information
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the 2-oxoisovalerate dehydrogenase alpha subunit interacts directly with the superoxid dismutase of Thermus thermophilus
-
-
?
additional information
?
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-
the 2-oxoisovalerate dehydrogenase alpha subunit interacts directly with the superoxid dismutase of Thermus thermophilus
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-
?
additional information
?
-
the 2-oxoisovalerate dehydrogenase alpha subunit interacts directly with the superoxid dismutase of Thermus thermophilus
-
-
?
additional information
?
-
-
decarboxylation and acylation reaction proceeds in 4 reaction steps in the enzyme complex, involving the cofactor thiamine diphosphate and the lipoic acid-bearing domain of component E2, E1 undergoes an open-closed conformational change upon formation of the enzyme-substrate complex, overview
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-
?
additional information
?
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the multienzyme complex is able to activate the branched fatty acids which are formed by transamination of Leu, Val, and Ile
-
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?
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D108N
-
less thermostable than wild type enzyme
D200A
-
less thermostable than wild type enzyme
D200A/D108N
-
the mutant is defective in folding and assembly and as no detectable overall activity
D200N
-
less thermostable than wild type enzyme
D295A
-
site-directed mutagenesis of an alpha-subunit residue of component E1b, increased activity compared to the wild-type
E198Q/D200N
-
the mutant is defective in folding and assembly and as no detectable overall activity
F364C
-
E1alpha-missense mutation in type IA maple syrup urine disease that causes the occurence of exclusively alpha,beta dimers
H146A
-
site-directed mutagenesis, mutation of a beta'-subunit residue, no reductive acylation activity, low decarboxylation activity
H147N
-
site-directed mutagenesis, mutation of a beta'-subunit residue, no reductive acylation activity, low decarboxylation activity
H291A
-
site-directed mutagenesis, mutation of a alpha-subunit residue, highly reduced activity compared to the wild-type E1b component
H291N
-
site-directed mutagenesis, mutation of a alpha-subunit residue, highly reduced activity compared to the wild-type E1b component
H291Q
-
site-directed mutagenesis, mutation of a alpha-subunit residue, highly reduced activity compared to the wild-type E1b component
R287A
-
site-directed mutagenesis of an alpha-subunit residue of component E1b, highly increased Km and reduced activity compared to the wild-type
R301A
-
site-directed mutagenesis of an alpha-subunit residue of component E1b, increased Km and reduced activity compared to the wild-type
S292D
-
site-directed mutagenesis, mutation of a alpha-subunit residue of complex component E1b, reduced activity compared to the wild-type E1b component
S292E
-
site-directed mutagenesis, mutation of a alpha-subunit residue of complex component E1b, highly reduced activity compared to the wild-type E1b component
S292N
-
site-directed mutagenesis, mutation of a alpha-subunit residue of complex component E1b, reduced activity compared to the wild-type E1b component
S302A
-
site-directed mutagenesis, mutation of a alpha-subunit residue of complex component E1b, increased activity compared to the wild-type E1b component
T265R
-
missense mutation in type IA maple syrup urine disease that causes the occurence of both alpha2beta2 tetramers and lower molecular weight species
Y300A
-
site-directed mutagenesis of an alpha-subunit residue of component E1b, increased Km and reduced activity compared to the wild-type
Y300F
-
site-directed mutagenesis of an alpha-subunit residue of component E1b, increased Km and reduced activity compared to the wild-type
Y368C
-
missense mutation in type IA maple syrup urine disease that causes the occurence of both alpha2beta2 tetramers and lower molecular weight species
Y393N
-
E1alpha-missense mutation in type IA maple syrup urine disease that causes the occurence of exclusively alpha,beta dimers
S313A
-
twofold increase in Km-value but no change in turnover-number
S315A
-
mutation has no effect on Km-value or turnover-number
S319A
-
mutation has no effect on Km-value or turnover-number
D296A
-
inactive enzyme, no ability of component E1 apoenzyme to reconstitute with thiamine diphosphate
H292A
-
inactive enzyme, no binding of thiamine diphosphate
R288A
-
inactive enzyme, no detectable phosphorylation
S293E/S303E
-
mutation in the alpha-subunit, no activity
S303A
-
mutation in the alpha-subunit, no effect upon enzyme activity
S303E
-
mutation in the alpha-subunit, no effect upon enzyme activity
S292Q
-
no activity
S292Q
-
site-directed mutagenesis, mutation of a alpha-subunit residue of complex component E1b, inactive mutant
S293A
-
mutation in the alpha-subunit, nearly 12fold increase in Km-value, no inactivation after incubation with ATP
S293A
-
10fold increased Km-value for 3-methyl-2-oxobutanoate, 2.8fold increased Km-value for 4-methyl-2-oxopentanoate, no change in Km-value for thiamine diphosphate
S293E
-
mutation in the alpha-subunit, completely inactive enzyme
S293E
-
no ability of the E1 apoenzyme to reconstitute with thiamine diphosphate
additional information
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missense mutation in E1b subunits that cause maple syrup urine disease: R114W-alpha, T166M-alpha, R220W-alpha. N222S-alpha. M64T-alpha. G204S-alpha. A208T-alpha. T265R-alpha, I281T-alpha, N126Y-beta, Q145K-alpha, H156R-beta, A209D-alpha, A240P-alpha. G245R-alpha, R252H-alpha, F364C-alpha, Y368C-alpha and Y393N-alpha
additional information
-
enzyme complex regulation by reversible phosphorylation is impaired in component E1b S292 and S302 mutants, no or residual acylation of the lipoic acid-bearing domain of component E2b, overview
additional information
-
hE1b-Tyr113Phe mutant, specifically affects the decarboxylation reaction, thiamine diphosphate appears hyperactive, is prone to paracatalytic inactivation
additional information
-
the hybrid E1b heterotetramer carrying one wild type, one S292Qalpha subunit, and two wild type beta subunits contains only one functional active site and exhibits nearly 40% of the wild type activity
additional information
-
construction of transgenic Arabidopsis thaliana plants overexpressing the branched-chain alpha-keto acid dehydrogenase multienzyme complex BCKDC in chloroplasts via Agrobacterium tumefaciens transformation under control of the CaMV 35S promotor, accumulation of branched-chain acyl-CoAs and alteration of free amino acid composition in seeds, overview
additional information
-
complete deletion of the bkdR open reading frame, produces fewer spores or the spores have reduced viability, is apparently not complemented in trans by the wild-type allele, is able to utilize leucine as sole carbon source and has no detectable growth defect, bkdR gene product acts as a repressor, rather than an activator of transcription
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Reed, L.J.; Damuni, Z.; Merryfield, M.L.
Regulation of mammalian pyruvate and branched-chain alpha-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation
Curr. Top. Cell. Regul.
27
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1985
Bos taurus
brenda
Aevarsson, A.; Chuang, J.L.; Wynn, R.M.; Turley, S.; Chuang, D.T.; Hol, W.G.J.
Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease
Structure
8
277-291
2000
Homo sapiens
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Randle, P.J.; Patston, P.A.; Espinal, J.
Branched-chain ketoacid dehydrogenase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
18
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1987
Bos taurus, Oryctolagus cuniculus, Rattus norvegicus
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Sykes, P.J.; Burns, G.; Menard, J.; Hatter, K.; Sokatch, J.R.
Molecular cloning of genes encoding branched-chain keto acid dehydrogenase of Pseudomonas putida
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Cloning of genes for branched-chain keto acid dehydrogenase in Pseudomonas putida
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Molecular cloning of the mature E1b-beta subunit of human branched-chain alpha-keto acid dehydrogenase complex
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Nobukuni, Y.; Mitsubuchi, H.; Endo, F.; Asaka, J.; Oyama, R.; Titani, K.; Matsuda, I.
Isolation and characterization of a complementary DNA clone coding for the E1 beta subunit of the bovine branched-chain alpha-ketoacid dehydrogenase complex: complete amino acid sequence of the precursor protein and its proteolytic processing
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1990
Bos taurus
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Lau, K.S.; Cooper, A.J.L.; Chuang, D.T.
Inhibition of the bovine branched-chain 2-oxo acid dehydrogenase complex and its kinase by arylidenepyruvates
Biochim. Biophys. Acta
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1990
Bos taurus
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Harris, R.A.; Kuntz, M.J.; Simpson, R.
Inhibition of branched-chain alpha-keto acid dehydrogenase kinase by alpha-chloroisocaproate
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Rattus norvegicus
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Oxidation of branched-chain amino acids in tumor-bearing rats
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Purification of branched-chain keto acid dehydrogenase and lipoamide dehydrogenase-valine from Pseudomonas
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1988
Pseudomonas aeruginosa, Pseudomonas putida
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Assays for E1 and E2 components of the branched-chain keto acid dehydrogenase complex
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1988
Bos taurus
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Branched-chain alpha-keto acid dehydrogenase and its kinase from rabbit liver and heart
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Oryctolagus cuniculus
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Pettit, F.H.; Reed, L.J.
Branched-chain alpha-keto acid dehydrogenase complex from bovine kidney
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166
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1988
Bos taurus
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Purification, resolution, and reconstitution of branched-chain 2-keto acid dehydrogenase complex from bovine kidney
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1988
Bos taurus
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Isolation of branched-chain alpha-keto acid dehydrogenase as active complex from bovine liver
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1988
Bos taurus
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Activity of branched-chain 2-oxo acid dehydrogenase complex in rat liver mitochondria and in rat liver
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256
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Rattus norvegicus
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Cellular localization and characterization of bovine liver branched-chain -keto acid dehydrogenases
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Bos taurus
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Partial purification and properties of branched-chain 2-oxo acid dehydrogenase of ox liver
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171
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Bos taurus
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Pettit, F.H.; Yeaman, S.J.; Reed, L.J.
Purification and characterization of branched chain alpha-keto acid dehydrogenase complex of bovine kidney
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75
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1978
Bos taurus
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Purification and characterization of branched chain alpha-ketoacid dehydrogenase from bovine liver mitochondria
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254
5522-5526
1979
Bos taurus
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Sokatch, J.R.; McCully, V.; Roberts, C.M.
Purification of a branched-chain keto acid dehydrogenase from Pseudomonas putida
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1981
Pseudomonas putida
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Purification, resolution, and reconstitution of rat liver branched-chain alpha-keto acid dehydrogenase complex
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Rattus norvegicus
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Purification of branched chain alpha-ketoacid dehydrogenase complex from rat liver
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Rattus norvegicus
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242
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Ovis aries
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Role of branched-chain 2-oxo acid dehydrogenase and pyruvate dehydrogenase in 2-oxobutyrate metabolism
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234
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1986
Rattus norvegicus
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McCully, V.; Burns, G.; Sokatch, J.R.
Resolution of branched-chain oxo acid dehydrogenase complex of Pseudomonas aeruginosa PAO
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Pseudomonas aeruginosa
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Morrison, E.Y.S.A.; Mullings, K.
Isolation of a branched chain alpha-keto acid dehydrogenase from rabbit liver
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Oryctolagus cuniculus
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Isolation of rabbit liver branched chain alpha-ketoacid dehydrogenase and regulation by phosphorylation
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Oryctolagus cuniculus
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Activation of hepatic branched chain alpha-keto acid dehydrogenase by a skeletal muscle factor
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1982
Rattus norvegicus
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Stabilization of mammalian liver branched-chain alpha-ketoacid dehydrogenase by thiamin pyrophosphate
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202
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1980
Bos taurus
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Gerbling, H.; Gerhardt, B.
Oxidative decarboxylation of branched-chain 2-oxo fatty acids by higher plant peroxisomes
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Vigna radiata
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Parker, P.J.; Randle, P.J.
Inactivation of rat heart branched-chain 2-oxoacid dehydrogenase complex by adenosine triphosphate
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Rattus norvegicus
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Danner, D.J.; Davidson, E.D.; Elsas, L.J.
Thiamine increases the specific activity of human liver branched chain alpha-ketoacid dehydrogenase
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Homo sapiens
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Parker, P.J.; Randle, P.J.
Branched chain 2-oxo-acid dehydrogenase complex of rat liver
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Rattus norvegicus
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Sinclair, D.A.; Dawes, I.W.; Dickinson, J.R.
Purification and characterization of the branched chain alpha-ketoacid dehydrogenase complex from Saccharomyces cerevisiae
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31
911-922
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Saccharomyces cerevisiae
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Dickinson, J.R.
Branched-chain keto acid dehydrogenase of yeast
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Saccharomyces cerevisiae
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Hester, K.L.; Luo, J.; Sokatch, J.R.
Purification of Pseudomonas putida branched-chain keto acid dehydrogenase E1 component
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A second branched-chain alpha-keto acid dehydrogenase gene cluster (bkdFGH) from Streptomyces avermitilis: its relationship to avermectin biosynthesis and the construction of a bkdF mutant suitable for the production of novel antiparasitic avermectins
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177
3504-3511
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Site-directed mutagenesis of phosphorylation sites of the branched chain alpha-ketoacid dehydrogenase complex
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Isolation and characterization of cDNA clones for the E1beta and E2 subunits of the branched-chain alpha-ketoacid dehydrogenase complex in Arabidopsis
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Arabidopsis thaliana
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Purification of rat kidney branched-chain oxo acid dehydrogenase complex with endogenous kinase activity
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Activation of hepatic branched-chain alpha-keto acid dehydrogenase complex by tumor necrosis factor-alpha in rats
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Rattus norvegicus
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Folding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase complex
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Homo sapiens
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Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase: refined phosphorylation loop structure in the active site
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278
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Homo sapiens
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Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain alpha-keto acid decarboxylase/dehydrogenase
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279
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Homo sapiens
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337
1011-1033
2004
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Li, L.; Thipyapong, P.; Breeden, D.C.; Steffens, J.C.
Overexpression of a bacterial branched-chain alpha-keto acid dehydrogenase complex in Arabidopsis results in accumulation of branched-chain acyl-CoAs and alteration of free amino acid composition in seeds
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165
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Homo sapiens
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Molecular mechanism for regulation of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex by phosphorylation
Structure
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2004
Homo sapiens
brenda
Murakami, T.; Matsuo, M.; Shimizu, A.; Shimomura, Y.
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Rattus norvegicus
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Nakai, N.; Shimomura, Y.; Tamura, T.; Tamura, N.; Hamada, K.; Kawano, F.; Ohira, Y.
Leucine-induced activation of translational initiation is partly regulated by the branched-chain alpha-keto acid dehydrogenase complex in C2C12 cells
Biochem. Biophys. Res. Commun.
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Mus musculus
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Mersey, B.D.; Jin, P.; Danner, D.J.
Human microRNA (miR29b) expression controls the amount of branched chain alpha-ketoacid dehydrogenase complex in a cell
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Homo sapiens
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Sprusansky, O.; Stirrett, K.; Skinner, D.; Denoya, C.; Westpheling, J.
The bkdR gene of Streptomyces coelicolor is required for morphogenesis and antibiotic production and encodes a transcriptional regulator of a branched-chain amino acid dehydrogenase complex
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Streptomyces coelicolor
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Homo sapiens
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Brosnan, J.T.; Brosnan, M.E.
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Homo sapiens
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Homo sapiens, Rattus norvegicus
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Machius, M.; Wynn, R.M.; Chuang, J.L.; Li, J.; Kluger, R.; Yu, D.; Tomchick, D.R.; Brautigam, C.A.; Chuang, D.T.
A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase
Structure
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Homo sapiens
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Purification of branched-chain keto acid dehydrogenase regulator from Pseudomonas putida
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Pseudomonas putida
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Al-Mailem, D.M.; Hough, D.W.; Danson, M.J.
The 2-oxoacid dehydrogenase multienzyme complex of Haloferax volcanii
Extremophiles
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Haloferax volcanii
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Heath, C.; Posner, M.G.; Aass, H.C.; Upadhyay, A.; Scott, D.J.; Hough, D.W.; Danson, M.J.
The 2-oxoacid dehydrogenase multi-enzyme complex of the archaeon Thermoplasma acidophilum - recombinant expression, assembly and characterization
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Thermoplasma acidophilum
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Kang, H.; Lee, S.K.; Cho, S.W.; Lee, S.H.; Kwack, K.
Branched chain alpha-keto acid dehydrogenase, E1-beta subunit gene is associated with premature ovarian failure
Fertil. Steril.
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2008
Homo sapiens
brenda
Nakai, T.; Kuramitsu, S.; Kamiya, N.
Structural bases for the specific interactions between the E2 and E3 components of the Thermus thermophilus 2-oxo acid dehydrogenase complexes
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Thermus thermophilus
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Islam, M.M.; Wallin, R.; Wynn, R.M.; Conway, M.; Fujii, H.; Mobley, J.A.; Chuang, D.T.; Hutson, S.M.
A novel branched-chain amino acid metabolon. Protein-protein interactions in a supramolecular complex
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Rattus norvegicus (P35738)
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Li, J.; Machius, M.; Chuang, J.L.; Wynn, R.M.; Chuang, D.T.
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Homo sapiens
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Matsumoto, H.; Akita, K.; Sakai, R.; Shimomura, Y.
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Mus musculus
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Decreased enzyme activity and contents of hepatic branched-chain alpha-keto acid dehydrogenase complex subunits in a rat model for type 2 diabetes mellitus
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Rattus norvegicus
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Mus musculus
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Knapik-Czajka, M.
Stimulation of rat liver branched-chain alpha-keto acid dehydrogenase activity by low doses of bezafibrate
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Rattus norvegicus
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Cole, J.T.; Sweatt, A.J.; Hutson, S.M.
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Rattus norvegicus
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Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex
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Homo sapiens
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Knapik-Czajka, M.
Simvastatin increases liver branched-chain alpha-ketoacid dehydrogenase activity in rats fed with low protein diet
Toxicology
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2014
Rattus norvegicus
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Tso, S.C.; Qi, X.; Gui, W.J.; Chuang, J.L.; Morlock, L.K.; Wallace, A.L.; Ahmed, K.; Laxman, S.; Campeau, P.M.; Lee, B.H.; Hutson, S.M.; Tu, B.P.; Williams, N.S.; Tambar, U.K.; Wynn, R.M.; Chuang, D.T.
Structure-based design and mechanisms of allosteric inhibitors for mitochondrial branched-chain alpha-ketoacid dehydrogenase kinase
Proc. Natl. Acad. Sci. USA
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Mus musculus
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Jia, F.; Cui, M.; Than, M.T.; Han, M.
Developmental defects of Caenorhabditis elegans lacking branched-chain alpha-ketoacid dehydrogenase are mainly caused by monomethyl branched-chain fatty acid deficiency
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Caenorhabditis elegans
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Lee, D.W.; Ng, B.G.; Kim, B.S.
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Streptomyces sp., Streptomyces sp. M10
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Kumaran, S.; Patel, M.S.; Jordan, F.
Nuclear magnetic resonance approaches in the study of 2-oxo acid dehydrogenase multienzyme complexes - a literature review
Molecules
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Escherichia coli
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Kadota, Y.; Toyoda, T.; Kitaura, Y.; Adams, S.H.; Shimomura, Y.
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Rattus norvegicus
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The impact of the branched-chain ketoacid dehydrogenase complex on amino acid homeostasis in Arabidopsis
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Arabidopsis thaliana
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Song, C.; Li, H.; Sheng, L.; Zhang, X.
Characterization of the interaction between superoxide dismutase and 2-oxoisovalerate dehydrogenase
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Thermus thermophilus (Q72GU1), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q72GU1)
brenda
Cui, Q.; Zhou, F.; Liu, W.; Tao, Y.
Avermectin biosynthesis stable functional expression of branched chain alpha-keto acid dehydrogenase complex from Streptomyces avermitilis in Escherichia coli by selectively regulating individual subunit gene expression
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Streptomyces avermitilis
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Knapik-Czajka, M.; Jurczyk, M.; Bielen, J.; Aleksandrovych, V.; Gawedzka, A.; Stach, P.; Drag, J.; Gil, K.
Effect of 5-fluorouracil on branched-chain alpha-keto acid dehydrogenase (BCKDH) complex in rats heart
Folia Med. Crac.
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2021
Rattus norvegicus (P11960 and P35738)
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Singh, V.K.; Sirobhushanam, S.; Ring, R.P.; Singh, S.; Gatto, C.; Wilkinson, B.J.
Roles of pyruvate dehydrogenase and branched-chain alpha-keto acid dehydrogenase in branched-chain membrane fatty acid levels and associated functions in Staphylococcus aureus
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Staphylococcus aureus, Staphylococcus aureus JE2
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Hull, J.; Usmari Moraes, M.; Brookes, E.; Love, S.; Conway, M.
Distribution of the branched-chain alpha-ketoacid dehydrogenase complex E1alpha subunit and glutamate dehydrogenase in the human brain and their role in neuro-metabolism
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Homo sapiens (A0A024R0K3)
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