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dihydrolipoyl transacylase
E2
2-oxoisocaproate dehydrogenase
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2-oxoisovalerate dehydrogenase (lipoate)
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alpha-keto-beta-methylvalerate dehydrogenase
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alpha-ketoisocaproate dehydrogenase
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alpha-ketoisocaproic dehydrogenase
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alpha-ketoisocaproic-alpha-keto-beta-methylvaleric dehydrogenase
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alpha-ketoisovalerate dehydrogenase
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alpha-oxoisocaproate dehydrogenase
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branched chain keto acid dehydrogenase
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branched-chain (-2-oxoacid BCD) dehydrogenase
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branched-chain 2-keto acid dehydrogenase
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branched-chain 2-oxo acid dehydrogenase
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branched-chain alpha-keto acid dehydrogenase
branched-chain alpha-keto acid dehydrogenase complex
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branched-chain alpha-ketoacid dehydrogenase
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branched-chain alpha-ketoacid dehydrogenase complex
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branched-chain alpha-ketoacid dehydrogenase enzyme complex
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branched-chain alpha-oxo acid dehydrogenase
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branched-chain keto acid dehydrogenase
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branched-chain ketoacid dehydrogenase
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dehydrogenase, 2-oxoisocaproate
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dehydrogenase, 2-oxoisovalerate (lipoate)
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dehydrogenase, branched chain alpha-keto acid
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BCKDH
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branched-chain alpha-keto acid dehydrogenase
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branched-chain alpha-keto acid dehydrogenase
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2-oxo-isocaproate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
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2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(propanoyl)dihydrolipoyllysine + CO2
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2-oxoglutarate + NAD+ + CoA
3-carboxypropionyl-CoA + NADH + CO2
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2-oxoisovalerate + NAD+
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2-oxoisovalerate + NAD+
? + NADH
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3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
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3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
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4-methyl-2-oxopentanoate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH
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pyruvate + NAD+ + CoA
acetyl-CoA + CO2 + NADH
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additional information
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additional information
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does not interact with human mitochondrial branched-chain aminotransferase isozymes
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additional information
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additional information
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enzyme probably is identical with EC 1.2.1.25
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additional information
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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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additional information
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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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additional information
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the enzyme can be regulated by an endogenous protein kinase
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additional information
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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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additional information
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enzyme regulates the catabolism of branched-chain amino acids, and is regulated by phosphorylation-dephosphorylation
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5-fluorouracil
in male rats administered with 4 doses of 5-FU, 150 mg/kg b.wt. each, 5-FU treatment causes an increase in branched-chain alpha-keto acid dehydrogenase complex BCKDH activity that results mainly from increased dephosphorylation of the complex and is associated with an increase of phosphatase PPM1K mRNA level and reduction of BDK and dehydrogenase E1 mRNA levels
Activator protein
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a protein in rat liver and kidney mitochondria that reactivates phosphorylated branched-chain complex without dephosphorylation
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alpha-ketoisovalerate
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activates through release of branched-chain alpha-keto acid dehydrogenase kinase from the BCKD complex
bezafibrate
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i.e. 2-[4-[2-(4-chlorobenzamido)ethyl]phenoxy]-2-methylpropanoic acid. In rats treated with 5, 10, 20 mg/kg bezafibrate mean enzyme actual activity is 1.9, 2.9, and 4.3fold higher than in the control group, respectively. Enzymatic total activity increases by 1.3 and 1.6fold in rats treated with 10 and 20 mg/kg bezafibrate
Lipoamide
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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)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
Skeletal muscle factor
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stimulates enzyme from liver
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tumor necrosis factor-alpha
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alpha-Chloroisocaproate
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activation of the enzyme complex in intact cell and tissue preparations
alpha-Chloroisocaproate
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activates through release of branched-chain alpha-keto acid dehydrogenase kinase from the BCKD complex
alpha-Ketoisocaproate
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activates through release of branched-chain alpha-keto acid dehydrogenase kinase from the BCKD complex
alpha-Ketoisocaproate
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promotes dissociation of the BCKDH kinase from the BCKDH complex, consistent with activation of BCKDH complex
thiamine diphosphate
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349052, 349053, 349060, 349067, 349068, 349070, 349074, 349077, 349085, 349088, 349090, 587061
thiamine diphosphate
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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)-COHCHR1R2 + lipoyl-E2 = R1R2CHCO-SCoA + dihydrolipoyl-E2, 4. dihydrolipoyl-E2 + NAD+ = lipoyl-E2 + NADH
thiamine diphosphate
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Km: 0.0012 mM in the reaction with 3-methyl-2-oxobutanoate
tumor necrosis factor-alpha
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activates the multienzyme complex about 4fold at 0.05 mg/kg body weight 4 h prior to slaughtering, reduces the amount of phosphorylated E1b component
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tumor necrosis factor-alpha
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0.025 or 0.5 mg per kg body weight elevate the activity state of BCKDH complex from 22% to 69% and 86%, respectively, decrease in the bound form of BCKDH kinase is involved in the mechanism responsible for tumor necrosis factor-alpha induced activation of the BCKDH complex
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tumor necrosis factor-alpha
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promotes dissociation of the BCKDH kinase from the BCKDH complex in rat liver, resulting in activation of the BCKDH complex
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additional information
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clofibric acid and thiamine diphosphate have no effect on the protein-protein interaction between branched-chain alpha-keto acid dehydrogenase kinase and BCKD complex
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additional information
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endurance exercise activates the BCKDH complex
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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
97-121
1987
Bos taurus, Oryctolagus cuniculus, Rattus norvegicus
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brenda
Harris, R.A.; Kuntz, M.J.; Simpson, R.
Inhibition of branched-chain alpha-keto acid dehydrogenase kinase by alpha-chloroisocaproate
Methods Enzymol.
166
114-123
1988
Rattus norvegicus
brenda
Argiles, J.M.; Lopez-Soriano, F.J.
Oxidation of branched-chain amino acids in tumor-bearing rats
Biochem. Soc. Trans.
17
1044-1045
1989
Rattus norvegicus
brenda
Beggs, M.; Randle, P.J.
Activity of branched-chain 2-oxo acid dehydrogenase complex in rat liver mitochondria and in rat liver
Biochem. J.
256
929-934
1988
Rattus norvegicus
brenda
Ono, K.; Hakozaki, M.; Kimura, A.; Kochi, H.
Purification, resolution, and reconstitution of rat liver branched-chain alpha-keto acid dehydrogenase complex
J. Biochem.
101
19-27
1987
Rattus norvegicus
brenda
Shimomura, Y.; Paxton, R.; Ozawa, T.; Harris, R.A.
Purification of branched chain alpha-ketoacid dehydrogenase complex from rat liver
Anal. Biochem.
163
74-78
1987
Rattus norvegicus
brenda
Paxton, R.; Scislowski, P.W.D.; Davis, E.J.; Harris, R.A.
Role of branched-chain 2-oxo acid dehydrogenase and pyruvate dehydrogenase in 2-oxobutyrate metabolism
Biochem. J.
234
295-303
1986
Rattus norvegicus
brenda
Paul, H.S.; Adibi, S.A.
Activation of hepatic branched chain alpha-keto acid dehydrogenase by a skeletal muscle factor
J. Biol. Chem.
257
12581-12588
1982
Rattus norvegicus
brenda
Parker, P.J.; Randle, P.J.
Inactivation of rat heart branched-chain 2-oxoacid dehydrogenase complex by adenosine triphosphate
FEBS Lett.
95
153-156
1978
Rattus norvegicus
brenda
Parker, P.J.; Randle, P.J.
Branched chain 2-oxo-acid dehydrogenase complex of rat liver
FEBS Lett.
90
183-186
1978
Rattus norvegicus
brenda
Zhao, Y.; Hawes, J.; Popov, K.M.; Jaskiewicz, J.; Shimomura, Y.; Crabb, D.W.; Harris, R.A.
Site-directed mutagenesis of phosphorylation sites of the branched chain alpha-ketoacid dehydrogenase complex
J. Biol. Chem.
269
18583-18587
1994
Rattus norvegicus
brenda
Aevarsson, A.; Seger, K.; Turley, S.; Sokatch, J.R.; Hol, W.G.J.
Crystal structure of 2-oxoisovalerate dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes
Nat. Struct. Biol.
6
785-792
1999
Pseudomonas putida, Rattus norvegicus
brenda
Hawes, J.W.; Schnepf, R.J.; Jenkins, A.E.; Shimomura, Y.; Popov, K.M.; Harris, R.A.
Roles of amino acid residues surrounding phosphorylation site 1 and branched-chain alpha-ketoacid dehydrogenase (BCKDH) in catalysis and phosphorylation site recognition by BCKDH kinase
J. Biol. Chem.
270
31071-31076
1995
Rattus norvegicus
brenda
Odessey, R.
Purification of rat kidney branched-chain oxo acid dehydrogenase complex with endogenous kinase activity
Biochem. J.
204
353-356
1982
Rattus norvegicus
brenda
Shiraki, M.; Shimomura, Y.; Miwa, Y.; Fukushima, H.; Murakami, T.; Tamura, T.; Tamura, N.; Moriwaki, H.
Activation of hepatic branched-chain alpha-keto acid dehydrogenase complex by tumor necrosis factor-alpha in rats
Biochem. Biophys. Res. Commun.
328
973-978
2005
Rattus norvegicus
brenda
Murakami, T.; Matsuo, M.; Shimizu, A.; Shimomura, Y.
Dissociation of branched-chain alpha-keto acid dehydrogenase kinase (BDK) from branched-chain alpha-keto acid dehydrogenase complex (BCKDC) by BDK inhibitors
J. Nutr. Sci. Vitaminol.
51
48-50
2005
Rattus norvegicus
brenda
Shimomura, Y.; Honda, T.; Shiraki, M.; Murakami, T.; Sato, J.; Kobayashi, H.; Mawatari, K.; Obayashi, M.; Harris, R.A.
Branched-chain amino acid catabolism in exercise and liver disease
J. Nutr.
136
250S-253S
2006
Homo sapiens, Rattus norvegicus
brenda
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
J. Biol. Chem.
282
11893-11903
2007
Rattus norvegicus (P35738)
brenda
Matsumoto, H.; Akita, K.; Sakai, R.; Shimomura, Y.
Analysis of branched-chain alpha-keto acid dehydrogenase complex activity in rat tissues using alpha-keto[1-13C]isocaproate as substrate
Anal. Biochem.
399
1-6
2010
Bos taurus, Rattus norvegicus
brenda
Bajotto, G.; Murakami, T.; Nagasaki, M.; Sato, Y.; Shimomura, Y.
Decreased enzyme activity and contents of hepatic branched-chain alpha-keto acid dehydrogenase complex subunits in a rat model for type 2 diabetes mellitus
Metab. Clin. Exp.
58
1489-1495
2009
Rattus norvegicus
brenda
Knapik-Czajka, M.
Stimulation of rat liver branched-chain alpha-keto acid dehydrogenase activity by low doses of bezafibrate
Toxicology
306
101-107
2013
Rattus norvegicus
brenda
Cole, J.T.; Sweatt, A.J.; Hutson, S.M.
Expression of mitochondrial branched-chain aminotransferase and alpha-keto-acid dehydrogenase in rat brain: implications for neurotransmitter metabolism
Front. Neuroanat.
6
18
2012
Rattus norvegicus
brenda
Knapik-Czajka, M.
Simvastatin increases liver branched-chain alpha-ketoacid dehydrogenase activity in rats fed with low protein diet
Toxicology
325
107-114
2014
Rattus norvegicus
brenda
Kadota, Y.; Toyoda, T.; Kitaura, Y.; Adams, S.H.; Shimomura, Y.
Regulation of hepatic branched-chain alpha-ketoacid dehydrogenase complex in rats fed a high-fat diet
Obes. Res. Clin. Pract.
7
e439-e444
2013
Rattus norvegicus
brenda
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.
61
121-129
2021
Rattus norvegicus (P11960 and P35738)
brenda