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Information on EC 1.2.4.4 - 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) and Organism(s) Rattus norvegicus and UniProt Accession P35738

for references in articles please use BRENDA:EC1.2.4.4
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IUBMB Comments
Contains thiamine diphosphate. It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168.
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Rattus norvegicus
UNIPROT: P35738
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
bckdh, bckdhb, bckdha, branched-chain 2-oxo acid dehydrogenase, branched-chain alpha-keto acid dehydrogenase, alpha-ketoacid dehydrogenase, branched-chain alpha-ketoacid dehydrogenase, bckdc, branched-chain alpha-ketoacid dehydrogenase complex, bcka dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dihydrolipoyl transacylase
E2
2-oxoisocaproate dehydrogenase
-
-
-
-
2-oxoisovalerate dehydrogenase (lipoate)
-
-
-
-
alpha-keto-beta-methylvalerate dehydrogenase
-
-
-
-
alpha-ketoisocaproate dehydrogenase
-
-
-
-
alpha-ketoisocaproic dehydrogenase
-
-
-
-
alpha-ketoisocaproic-alpha-keto-beta-methylvaleric dehydrogenase
-
-
-
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alpha-ketoisovalerate dehydrogenase
-
-
-
-
alpha-oxoisocaproate dehydrogenase
-
-
-
-
BCDH
-
-
-
-
BCKA dehydrogenase
-
-
BCKADC
-
-
-
-
BCKDH
BCKDH E1-alpha
-
-
-
-
BCKDH E1-beta
-
-
-
-
BCOAD
-
-
-
-
branched chain keto acid dehydrogenase
-
-
-
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branched-chain (-2-oxoacid BCD) dehydrogenase
-
-
-
-
branched-chain 2-keto acid dehydrogenase
-
-
-
-
branched-chain 2-oxo acid dehydrogenase
-
-
-
-
branched-chain alpha-keto acid dehydrogenase
branched-chain alpha-keto acid dehydrogenase complex
-
-
branched-chain alpha-ketoacid dehydrogenase
-
-
branched-chain alpha-ketoacid dehydrogenase complex
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-
branched-chain alpha-ketoacid dehydrogenase enzyme complex
-
-
branched-chain alpha-oxo acid dehydrogenase
-
-
-
-
branched-chain keto acid dehydrogenase
-
-
-
-
branched-chain ketoacid dehydrogenase
-
-
-
-
dehydrogenase, 2-oxoisocaproate
-
-
-
-
dehydrogenase, 2-oxoisovalerate (lipoate)
-
-
-
-
dehydrogenase, branched chain alpha-keto acid
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
show the reaction diagram
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, the multienzyme complex also contains small amounts of a specific kinase and a specific phosphatase which modulate the activity of E1 by phosphorylation and dephosphorylation
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
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-
-
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oxidative decarboxylation
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-
-
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SYSTEMATIC NAME
IUBMB Comments
3-methyl-2-oxobutanoate:[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-2-methylpropanoylating)
Contains thiamine diphosphate. It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-05-4
-
9082-72-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxo-isocaproate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
show the reaction diagram
-
-
-
-
?
2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(propanoyl)dihydrolipoyllysine + CO2
show the reaction diagram
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-
-
-
?
2-oxoglutarate + NAD+ + CoA
3-carboxypropionyl-CoA + NADH + CO2
show the reaction diagram
-
-
-
-
?
2-oxoisovalerate + NAD+
?
show the reaction diagram
-
-
-
-
?
2-oxoisovalerate + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
show the reaction diagram
-
-
-
-
?
3-methyl-2-oxopentanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
show the reaction diagram
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-
-
-
?
4-methyl-2-oxopentanoate + NAD+ + CoA
3-methylbutanoyl-CoA + CO2 + NADH
show the reaction diagram
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-
-
-
?
pyruvate + NAD+ + CoA
acetyl-CoA + CO2 + NADH
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxo-isocaproate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine + CO2
show the reaction diagram
-
-
-
-
?
3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine
[dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2
show the reaction diagram
-
-
-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-chloroisocaproate
-
-
isopentanoyl-CoA
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-
Skeletal muscle factor
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activity from liver, kidney and brains
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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-Chloroisocaproate
alpha-Ketoisocaproate
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
-
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
simvastatin
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Skeletal muscle factor
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stimulates enzyme from liver
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thiamine diphosphate
tumor necrosis factor-alpha
-
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0258
2-oxobutanoate
-
-
2.5
2-oxoglutarate
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-
0.011 - 0.568
3-methyl-2-oxobutanoate
0.01 - 0.0219
3-methyl-2-oxopentanoate
0.011 - 0.0215
4-methyl-2-oxopentanoate
0.0105
DL-3-methyl-2-oxopentanoate
-
-
0.0387 - 0.0423
NAD+
0.82 - 2.2
pyruvate
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0082 - 0.0136
isovaleryl-CoA
0.0177 - 0.023
NADH
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
not detected in astrocytes and Bergmann glia cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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maple syrup urine disease results from genetic enzyme defects, which lead to accumulation of toxic levels of branched chain amino acids and branched-chain alpha-keto acids that result in brain swelling
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ODBB_RAT
390
0
42823
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160000
-
wild-type enzyme and mutant enzymes S293E, S293A, S303A and S293E/S303E, gel filtration
190000
-
E1 component, gel filtration
37000
-
alpha2,beta2, 2 * 46000 + 2 * 37000, SDS-PAGE
38500
-
alphax,betax, x * 46500 + x * 38500, SDS-PAGE
46000
-
alpha2,beta2, 2 * 46000 + 2 * 37000, SDS-PAGE
46500
-
alphax,betax, x * 46500 + x * 38500, SDS-PAGE
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
alphax,betax, x * 46500 + x * 38500, SDS-PAGE
tetramer
-
alpha2,beta2, 2 * 46000 + 2 * 37000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
S293A
S293E
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hydrophobic interaction chromatography on phenyl-Sepharose
-
multienzyme complex
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
in skeletal muscle, subunits E1alpha protein is significantly reduced in OLETF rats
-
mRNA expression is not upregulated by bezafibrate treatment
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the total amount of hepatic enzyme is significantly decreased in diet-induced obesity rats
-
total BCKDC activity and protein abundance of E1alpha, E1beta, and E2 subunits are markedly lower in Otsuka Long-Evans Tokushima Fatty (OLETF) than in Long-Evans Tokushima Otsuka (LETO) rats at 8 and 25 weeks of age. In addition, hepatic BCKDC activity and protein amounts are significantly decreased in LETO rats aged 25 weeks than in LETO rats aged 8 weeks. In skeletal muscle, subunits E1beta and E2 proteins are significantly reduced in OLETF rats
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Parker, P.J.; Randle, P.J.
Branched chain 2-oxo-acid dehydrogenase complex of rat liver
FEBS Lett.
90
183-186
1978
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Odessey, R.
Purification of rat kidney branched-chain oxo acid dehydrogenase complex with endogenous kinase activity
Biochem. J.
204
353-356
1982
Rattus norvegicus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team