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Information on EC 1.2.1.25 - branched-chain alpha-keto acid dehydrogenase system
for references in articles please use BRENDA:EC1.2.1.25
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EC Tree 1 Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.1 With NAD+ or NADP+ as acceptor
1.2.1.25 branched-chain alpha-keto acid dehydrogenase system
IUBMB Comments
This enzyme system catalyses the oxidative decarboxylation of branched-chain α-keto acids derived from L-leucine, L-isoleucine, and L-valine to branched-chain acyl-CoAs. It belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.104, pyruvate dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.4.1.27, glycine cleavage system, and EC 2.3.1.190, acetoin dehydrogenase system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). The reaction catalysed by this system is the sum of three activities: EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), EC 2.3.1.168, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The system also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2-oxopentanoate.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.2.1.25
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maple
- syrup
- pdha1
- dihydrolipoamide
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alpha2beta2
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transacylase
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keto-acids
- bckdhb
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dihydrolipoyl
showSynonyms
e1alpha subunit, bckd complex, e1beta subunit, branched chain alpha-keto acid dehydrogenase complex, branched chain keto-acid dehydrogenase, mitochondrial branched-chain keto-acid dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-oxoisovalerate dehydrogenase
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alpha-ketoisovalerate dehydrogenase
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BCKD
BCKDalpha
BCKDC
BCKDH
branched chain keto-acid dehydrogenase
branched-chain alpha-keto acid dehydrogenase complex
branched-chain alpha-ketoacid dehydrogenase
branched-chain alpha-ketoacid dehydrogenase complex
branched-chain alpha-ketoacid dehydrogenase complex E1alpha subunit
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branched-chain-keto-acid dehydrogenase alpha
dehydrogenase, 2-oxoisovalerate (acylating)
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mitochondrial branched-chain keto-acid dehydrogenase
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-methyl-2-oxobutanoate + CoA + NAD+ = 2-methylpropanoyl-CoA + CO2 + NADH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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oxidative decarboxylation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
MetaCyc
2-oxobutanoate degradation I, anteiso-branched-chain fatty acid biosynthesis, even iso-branched-chain fatty acid biosynthesis, L-isoleucine degradation I, L-leucine degradation I, L-threonine degradation V, L-valine degradation I, odd iso-branched-chain fatty acid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
3-methyl-2-oxobutanoate:NAD+ 2-oxidoreductase (CoA-methylpropanoylating)
This enzyme system catalyses the oxidative decarboxylation of branched-chain alpha-keto acids derived from L-leucine, L-isoleucine, and L-valine to branched-chain acyl-CoAs. It belongs to the 2-oxoacid dehydrogenase system family, which also includes EC 1.2.1.104, pyruvate dehydrogenase system, EC 1.2.1.105, 2-oxoglutarate dehydrogenase system, EC 1.4.1.27, glycine cleavage system, and EC 2.3.1.190, acetoin dehydrogenase system. With the exception of the glycine cleavage system, which contains 4 components, the 2-oxoacid dehydrogenase systems share a common structure, consisting of three main components, namely a 2-oxoacid dehydrogenase (E1), a dihydrolipoamide acyltransferase (E2), and dihydrolipoamide dehydrogenase (E3). The reaction catalysed by this system is the sum of three activities: EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring), EC 2.3.1.168, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, and EC 1.8.1.4, dihydrolipoyl dehydrogenase. The system also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2-oxopentanoate.
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CAS REGISTRY NUMBER
COMMENTARY
37211-61-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methyl-butanoyl-CoA + CO2 + NADH
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH
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L-alpha-keto-beta-methylvalerate + CoA + NAD+
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additional information
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Substrates: the human BCKD complex catalyzes the irreversible oxidative decarboxylation of the branched-chain ketoacids (2-keto-isocaproate derived from leucine, 2-keto-3-methylglutarate obtained from isoleucine, and 2-keto-isovalerate from valine). This reaction produces CO2, NADH, and the respective branched-chain acyl-coA intermediates with a 1:1:1 stoichiometry. The action of BCKD complex generates isovaleryl-CoA from 2-ketoisocaproate (leucine), 2-methylbutyryl-CoA from 2-keto-3-methylglutarate (isoleucine), and isobutyryl-CoA from 2-keto-isovalerate (valine)
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH
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Substrates: specific for the L-isomer
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH
Substrates: -
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additional information
?
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Substrates: the human BCKD complex catalyzes the irreversible oxidative decarboxylation of the branched-chain ketoacids (2-keto-isocaproate derived from leucine, 2-keto-3-methylglutarate obtained from isoleucine, and 2-keto-isovalerate from valine). This reaction produces CO2, NADH, and the respective branched-chain acyl-coA intermediates with a 1:1:1 stoichiometry. The action of BCKD complex generates isovaleryl-CoA from 2-ketoisocaproate (leucine), 2-methylbutyryl-CoA from 2-keto-3-methylglutarate (isoleucine), and isobutyryl-CoA from 2-keto-isovalerate (valine)
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxobutanoate + CoA + NAD+
2-methylpropanoyl-CoA + CO2 + NADH + H+
Substrates: -
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?
3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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3-methyl-2-oxopentanoate + CoA + NAD+
2-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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4-methyl-2-oxopentanoate + CoA + NAD+
3-methylbutanoyl-CoA + CO2 + NADH + H+
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Substrates: -
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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CoA and NAD+ can be replaced by potassium ferricyanide but the activity is much lower
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
product inhibition of BCKDH by acyl-CoA can occur
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
E1 binds thiamine diphosphate, possessing two thiamine-binding pockets located between alpha and beta subunits
additional information
BCAT2 binding to BCKDH also increases BCKDH activity. Activation of BCKDH with 3,6-dichlorobrenzo(b)thiophene-2-carboxylic acid (BT2), a small-molecule BCKDK inhibitor, improves insulin sensitivity
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis
Tissue-specific responses of branched-chain alpha-ketoacid dehydrogenase activity in metabolic acidosis.
Acidosis, Lactic
A pathogenic glutamate-to-aspartate substitution (D296E) in the pyruvate dehydrogenase E1 subunit gene PDHA1.
Acidosis, Lactic
Biochemical characterization of two mutants of human pyruvate dehydrogenase, F205L and T231A of the E1alpha subunit.
Acidosis, Lactic
Cerebral palsy and pyruvate dehydrogenase deficiency: identification of two new mutations in the E1alpha gene.
Acidosis, Lactic
Down-regulation of expression of rat pyruvate dehydrogenase E1alpha gene by self-complementary adeno-associated virus-mediated small interfering RNA delivery.
Acidosis, Lactic
Pyruvate dehydrogenase E1alpha subunit deficiency in a female patient: evidence of antenatal origin of brain damage and possible etiology of infantile spasms.
Arthritis, Rheumatoid
Epitope mapping of the branched chain alpha-ketoacid dehydrogenase dihydrolipoyl transacylase (BCKD-E2) protein that reacts with sera from patients with idiopathic dilated cardiomyopathy.
Brain Injuries, Traumatic
Divergent Induction of Branched-Chain Aminotransferases and Phosphorylation of Branched Chain Keto-Acid Dehydrogenase Is a Potential Mechanism Coupling Branched-Chain Keto-Acid-Mediated-Astrocyte Activation to Branched-Chain Amino Acid Depletion-Mediated Cognitive Deficit after Traumatic Brain Injury.
branched-chain alpha-keto acid dehydrogenase system deficiency
Pyruvate dehydrogenase E1alpha subunit deficiency in a female patient: evidence of antenatal origin of brain damage and possible etiology of infantile spasms.
Cholangitis, Sclerosing
Antimitochondrial antibodies of primary biliary cirrhosis recognize dihydrolipoamide acyltransferase and inhibit enzyme function of the branched chain alpha-ketoacid dehydrogenase complex.
Hepatitis
Antimitochondrial antibodies of primary biliary cirrhosis recognize dihydrolipoamide acyltransferase and inhibit enzyme function of the branched chain alpha-ketoacid dehydrogenase complex.
Hepatitis, Chronic
Antimitochondrial antibodies of primary biliary cirrhosis recognize dihydrolipoamide acyltransferase and inhibit enzyme function of the branched chain alpha-ketoacid dehydrogenase complex.
Infertility, Male
Antisense inhibition of mitochondrial pyruvate dehydrogenase E1alpha subunit in anther tapetum causes male sterility.
Liver Cirrhosis, Biliary
Epitope mapping on E1alpha subunit of pyruvate dehydrogenase complex with autoantibodies of patients with primary biliary cirrhosis.
Maple Syrup Urine Disease
A nonsense mutation (R242X) in the branched-chain alpha-keto acid dehydrogenase E1alpha subunit gene (BCKDHA) as a cause of maple syrup urine disease. Mutations in brief no. 160. Online.
Maple Syrup Urine Disease
Definition of the mutation responsible for maple syrup urine disease in Poll Shorthorns and genotyping Poll Shorthorns and Poll Herefords for maple syrup urine disease alleles.
Maple Syrup Urine Disease
DNA carrier testing and newborn screening for maple syrup urine disease in old order mennonite communities.
Maple Syrup Urine Disease
Impaired assembly of E1 decarboxylase of the branched-chain alpha-ketoacid dehydrogenase complex in type IA maple syrup urine disease.
Maple Syrup Urine Disease
Loss of the Drosophila branched-chain ?-keto acid dehydrogenase complex (BCKDH) results in neuronal dysfunction.
Maple Syrup Urine Disease
Maple syrup urine disease caused by a partial deletion in the inner E2 core domain of the branched chain alpha-keto acid dehydrogenase complex due to aberrant splicing. A single base deletion at a 5'-splice donor site of an intron of the E2 gene disrupts the consensus sequence in this region.
Maple Syrup Urine Disease
Maple syrup urine disease in Cypriot families: identification of three novel mutations and biochemical characterization of the p.Thr211Met mutation in the E1alpha subunit.
Maple Syrup Urine Disease
Metformin inhibits Branched Chain Amino Acid (BCAA) derived ketoacidosis and promotes metabolic homeostasis in MSUD.
Maple Syrup Urine Disease
Molecular phenotypes in cultured maple syrup urine disease cells. Complete E1 alpha cDNA sequence and mRNA and subunit contents of the human branched chain alpha-keto acid dehydrogenase complex.
Maple Syrup Urine Disease
[Maple syrup urine disease: molecular pathology of the branched chain alpha-keto acid dehydrogenase complex]
Myocardial Ischemia
Epitope mapping of the branched chain alpha-ketoacid dehydrogenase dihydrolipoyl transacylase (BCKD-E2) protein that reacts with sera from patients with idiopathic dilated cardiomyopathy.
Neoplasms
AAV3-mediated transfer and expression of the pyruvate dehydrogenase E1 alpha subunit gene causes metabolic remodeling and apoptosis of human liver cancer cells.
Neoplasms
Dichloroacetate induces apoptosis and cell-cycle arrest in colorectal cancer cells.
Neoplasms
Tentative identification of the toxohormones of cancer cachexia: roles of vasopressin, prostaglandin E2 and cachectin-TNF.
Nervous System Diseases
Loss of the Drosophila branched-chain ?-keto acid dehydrogenase complex (BCKDH) results in neuronal dysfunction.
pyruvate dehydrogenase (acetyl-transferring) deficiency
Mechanisms of expression of pyruvate dehydrogenase deficiency caused by an E1alpha subunit mutation.
pyruvate dehydrogenase (acetyl-transferring) deficiency
Mutations in the gene for the E1beta subunit: a novel cause of pyruvate dehydrogenase deficiency.
pyruvate dehydrogenase (acetyl-transferring) deficiency
Pyruvate dehydrogenase complex deficiency caused by ubiquitination and proteasome-mediated degradation of the E1 subunit.
pyruvate dehydrogenase (nadp+) deficiency
A pathogenic glutamate-to-aspartate substitution (D296E) in the pyruvate dehydrogenase E1 subunit gene PDHA1.
pyruvate dehydrogenase (nadp+) deficiency
Dichloroacetate stabilizes the mutant E1alpha subunit in pyruvate dehydrogenase deficiency.
pyruvate dehydrogenase (nadp+) deficiency
Mechanisms of expression of pyruvate dehydrogenase deficiency caused by an E1alpha subunit mutation.
pyruvate dehydrogenase (nadp+) deficiency
Mutations in the gene for the E1beta subunit: a novel cause of pyruvate dehydrogenase deficiency.
pyruvate dehydrogenase (nadp+) deficiency
Mutations of the E1beta subunit gene (PDHB) in four families with pyruvate dehydrogenase deficiency.
Pyruvate Dehydrogenase Complex Deficiency Disease
A pathogenic glutamate-to-aspartate substitution (D296E) in the pyruvate dehydrogenase E1 subunit gene PDHA1.
Pyruvate Dehydrogenase Complex Deficiency Disease
Diagnosis and molecular analysis of three male patients with thiamine-responsive pyruvate dehydrogenase complex deficiency.
Pyruvate Dehydrogenase Complex Deficiency Disease
Dichloroacetate stabilizes the mutant E1alpha subunit in pyruvate dehydrogenase deficiency.
Pyruvate Dehydrogenase Complex Deficiency Disease
Mechanisms of expression of pyruvate dehydrogenase deficiency caused by an E1alpha subunit mutation.
Pyruvate Dehydrogenase Complex Deficiency Disease
Mutations in the gene for the E1beta subunit: a novel cause of pyruvate dehydrogenase deficiency.
Pyruvate Dehydrogenase Complex Deficiency Disease
Mutations of the E1beta subunit gene (PDHB) in four families with pyruvate dehydrogenase deficiency.
Pyruvate Dehydrogenase Complex Deficiency Disease
Pyruvate dehydrogenase complex deficiency caused by ubiquitination and proteasome-mediated degradation of the E1 subunit.
Spasms, Infantile
Pyruvate dehydrogenase E1alpha subunit deficiency in a female patient: evidence of antenatal origin of brain damage and possible etiology of infantile spasms.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.5
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pH 6.0: about 25% of maximal activity, pH 7.5: about 45% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
alpha and beta subunits of complex component E1 (BCKD), a tetramer (alpha2beta2), cf. EC 1.2.4.4
UniProt
brenda
subunits BCKDHA and BCKDHB of the E1 component, cf. EC 1.2.4.4
UniProt
brenda
alpha and beta subunits of complex component E1 (BCKD), a tetramer (alpha2beta2), cf. EC 1.2.4.4
UniProt
brenda
alpha and beta subunits of complex component E1 (BCKD), a tetramer (alpha2beta2), cf. EC 1.2.4.4
UniProt
brenda
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within the cerebellum, there is punctate labelling in the processes of cells within the Purkinje cell layer, most likely to be Bergmann astrocytes. The Purkinje cells themselves are unlabelled (12/18 brains examined) or weakly immunopositive. Within the granule cell layer, rosette like structures (glomeruli) are immunopositive. Within the deep cerebellar nuclei, there is strong granular immunopositivity in small glial cells in contrast to the largely immunonegative neurons
brenda
additional information
distribution of BCKD-E1alpha in the human brain, immunohistochemic analysis, overview. Within the hippocampus, neuronal labelling is strongest within the cornu ammonis area 4 (CA4), and weaker in successive CA regions through to CA1. In the cerebral cortex, larger pyramidal cells are strongly immunopositive. Vasculature labelling is observed throughout the cerebral cortex with only weak astrocytic labelling (9/18 brains examined), in the vicinity of the hippocampus and within the white matter. The subependymal and the ependymal tissue are immunopositive
brenda
additional information
BCKDC activity is highest in liver but present in all tissues tested. In the liver, BCKDC activity is high, with moderate activity in the kidney and heart, and limited active enzyme in skeletal muscle
brenda
additional information
human tissue distribution of the BCKD complex: BCKD is highly found in kidney, liver, brain, and heart, more moderately in skeletal muscle, stomach, and colon. Subcutaneous adipose tissue and small intestine show the lowest BCKD complex activity
brenda
additional information
tissue-specific preference for BCAA oxidation relative to other fuels
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additional information
within the hippocampus, GDH labelling is entirely astrocytic. There is also labelling of astrocytes in the neocortex and white matter, but labelling in the white matter is less dense than that in the cortex. The subpial feltwork of astrocytic processes is strongly immunopositive for GDH in all brain regions, not just in the cerebrum. Neurons are largely unlabelled (16/18 brains examined), apart from occasional pyramidal neurons in the vicinity of blood vessels. The labelling of perivascular astrocytic processes is evident throughout the cerebral cortex and cerebellum, in places, the labelling also involves the adjacent endothelium
brenda