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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
?
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starvation causes a significant decrease in activity in maternal tissues
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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
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enzyme probably is identical with EC 1.2.1.25
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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
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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
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the enzyme can be regulated by an endogenous protein kinase
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high-protein diet increases the enzyme concentration in rat liver, protein-free diet decreases enzyme concentration in rat liver
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enzyme regulates the catabolism of branched-chain amino acids, and is regulated by phosphorylation-dephosphorylation
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does not interact with human mitochondrial branched-chain aminotransferase isozymes
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the enzyme catalyzes a reaction of branched-chain amino acid catabolism which constitutes a crucial step to provide fatty acid precursors for antibiotic biosynthesis
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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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the 2-oxoisovalerate dehydrogenase alpha subunit interacts directly with the superoxid dismutase of Thermus thermophilus
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the 2-oxoisovalerate dehydrogenase alpha subunit interacts directly with the superoxid dismutase of Thermus thermophilus
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the 2-oxoisovalerate dehydrogenase alpha subunit interacts directly with the superoxid dismutase of Thermus thermophilus
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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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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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