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ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
ATP + mitogen-activated protein kinase kinase
ADP + phosphorylated mitogen-activated protein kinase kinase
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
ATP + [branched-chain a-keto acid dehydrogenase (acetyl-transferring)]
ADP + [branched-chain a-keto acid dehydrogenase (acetyl-transferring)] phosphate
-
-
-
?
ATP + [branched-chain keto-acid dehydrogenase (acetyl-transferring)]
ADP + [branched-chain keto-acid dehydrogenase (acetyl-transferring)] phosphate
the enzyme phosphorylates Ser293 of the E1alpha subunit of branched-chain keto-acid dehydrogenase
-
-
?
additional information
?
-
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
-
-
-
-
?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
-
the catalyzed reversible specific phosphorylation of the BCKD subunit regulates the first committed step in the pathway for leucine, isoleucine, and valine catabolism
-
-
?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
-
inactivation of the substrate enzyme
-
-
?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
-
the enzyme catalyzes the regulatory inactivation of the rate limiting enzyme in branched-chain amino acid catabolism
-
-
?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
-
phosphorylation of the branched-chain alpha-keto acid dehydrogenase complex leads to its inactivation, BDK itself is regulated via protein-protein interaction with the BCKD complex
-
-
?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
-
recombinant human wild-type and mutant substrate proteins, overview, phosphorylation at Ser301 and Ser302 in the phosphorylation loop of decarboxylase E1b component of the large branched-chain alpha-keto acid dehydrogenase complex, loop structure, overview
-
-
?
ATP + histone II-S
?
-
-
-
-
?
ATP + histone II-S
?
-
-
-
-
?
ATP + mitogen-activated protein kinase kinase
ADP + phosphorylated mitogen-activated protein kinase kinase
the enzyme promotes cell transformation or colorectal cancer by enhancing the MAPK signaling pathway through direct MEK phosphorylation
-
-
?
ATP + mitogen-activated protein kinase kinase
ADP + phosphorylated mitogen-activated protein kinase kinase
phosphorylation of mitogen-activated protein kinase kinase (MEK) at Ser221
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
-
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
Q14874
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
-
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
-
phosphorylation-mediated inactivation of the E1alpha subunit of branched-chain ketoacid dehydrogenase, BCKDH
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
-
phosphorylation of residue Ser293 of the E1alpha subunit of branched-chain ketoacid dehydrogenase, BCKDH
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
-
inactivation by phosphorylation of BCKDH
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
the enzyme (BCKDK) phosphorylates Ser293 of the E1alpha subunit of the BCKDH protein, which catalyzes the rate-limiting step in the catabolism of the branched-chain amino acids (BCAAs), inhibiting 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) (BCKDH) and thereby, limiting breakdown of the BCAAs
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
phosphorylates alpha-subunit of multienzyme complex component E1
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
phosphorylates alpha-subunit of multienzyme complex component E1
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
2 Ser-residues in E1-alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
2 Ser-residues in E1-alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
2 Ser-residues in E1-alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
incorporates 0.8 mol phosphate/mol alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
Ser-residues of MW 46000-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
phosphorylates alpha-subunit of multienzyme complex component E1 and additional sites not associated with inactivation of the enzyme
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
regulatory enzyme of branched-chain 2-oxoacid dehydrogenase complex
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
phosphorylation inactivates EC 1.2.4.4
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
2 Ser-residues in E1-alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
2 Ser-residues in E1-alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
2 Ser-residues in E1-alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
2 Ser-residues in E1-alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
GTP cannot replace ATP
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
phosphorylates exclusively MW 47000 subunit of substrate
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
incorporates 0.75 mol phosphate per mol phosphorylation site and 1.5 mol/mol alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
branched-chain amino acid metabolism
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
phosphorylation inactivates EC 1.2.4.4
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
2 Ser-residues in E1-alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
2 Ser-residues in E1-alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
2 Ser-residues in E1-alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
2 Ser-residues in E1-alpha-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
tight binding to multienzyme complex is required for phosphorylation, free enzyme is inactive
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
Ser-residues of MW 46000-subunit
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
branched-chain amino acid metabolism
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
regulatory enzyme of branched-chain 2-oxoacid dehydrogenase complex
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
phosphorylation inactivates EC 1.2.4.4
94884, 349052, 349056, 587061, 640578, 640581, 640583, 640585, 640589, 640595, 640597 -
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
phosphorylation inactivates EC 1.2.4.4
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
-
-
-
?
additional information
?
-
-
the branched-chain oxoacid dehydrogenase complex, BCOAD, is rate determining for the oxidation of branched-chain amino acids in skeletal muscle
-
-
?
additional information
?
-
-
R288A mutant of E1 is not phosphorylated by the enzyme
-
-
?
additional information
?
-
enzyme has also ATPase activity in absence of E1
-
-
?
additional information
?
-
-
The branched-chain alpha-keto acid dehydrogenase complex is the most important regulatory enzyme in branched-chain amino acid catabolism, regulation of hepatic BCKDH complex activity in spontaneous type 2 diabetes Otsuka Long-Evans Tokushima Fatty rats and Zucker diabetic fatty rats, both showing reduced enzyme activity, overview
-
-
?
additional information
?
-
-
BCKD kinase transcription regulation, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
ATP + mitogen-activated protein kinase kinase
ADP + phosphorylated mitogen-activated protein kinase kinase
the enzyme promotes cell transformation or colorectal cancer by enhancing the MAPK signaling pathway through direct MEK phosphorylation
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
ATP + [branched-chain a-keto acid dehydrogenase (acetyl-transferring)]
ADP + [branched-chain a-keto acid dehydrogenase (acetyl-transferring)] phosphate
-
-
-
?
ATP + [branched-chain keto-acid dehydrogenase (acetyl-transferring)]
ADP + [branched-chain keto-acid dehydrogenase (acetyl-transferring)] phosphate
the enzyme phosphorylates Ser293 of the E1alpha subunit of branched-chain keto-acid dehydrogenase
-
-
?
additional information
?
-
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
-
the catalyzed reversible specific phosphorylation of the BCKD subunit regulates the first committed step in the pathway for leucine, isoleucine, and valine catabolism
-
-
?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
-
inactivation of the substrate enzyme
-
-
?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
-
the enzyme catalyzes the regulatory inactivation of the rate limiting enzyme in branched-chain amino acid catabolism
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
Q14874
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
-
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
-
phosphorylation-mediated inactivation of the E1alpha subunit of branched-chain ketoacid dehydrogenase, BCKDH
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
-
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
-
inactivation by phosphorylation of BCKDH
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate
the enzyme (BCKDK) phosphorylates Ser293 of the E1alpha subunit of the BCKDH protein, which catalyzes the rate-limiting step in the catabolism of the branched-chain amino acids (BCAAs), inhibiting 3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) (BCKDH) and thereby, limiting breakdown of the BCAAs
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
regulatory enzyme of branched-chain 2-oxoacid dehydrogenase complex
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
phosphorylation inactivates EC 1.2.4.4
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
branched-chain amino acid metabolism
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
phosphorylation inactivates EC 1.2.4.4
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
branched-chain amino acid metabolism
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
regulatory enzyme of branched-chain 2-oxoacid dehydrogenase complex
-
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
phosphorylation inactivates EC 1.2.4.4
94884, 349052, 349056, 587061, 640578, 640581, 640583, 640585, 640589, 640595, 640597 -
-
?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
-
phosphorylation inactivates EC 1.2.4.4
-
-
?
additional information
?
-
-
the branched-chain oxoacid dehydrogenase complex, BCOAD, is rate determining for the oxidation of branched-chain amino acids in skeletal muscle
-
-
?
additional information
?
-
-
The branched-chain alpha-keto acid dehydrogenase complex is the most important regulatory enzyme in branched-chain amino acid catabolism, regulation of hepatic BCKDH complex activity in spontaneous type 2 diabetes Otsuka Long-Evans Tokushima Fatty rats and Zucker diabetic fatty rats, both showing reduced enzyme activity, overview
-
-
?
additional information
?
-
-
BCKD kinase transcription regulation, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2R)-2-chloro-3-phenylpropanoic acid
-
(2S)-2-chloro-3-phenylpropanoic acid
-
(R)-alpha-chloroisocaproate
-
(S)-alpha-chloroisocaproate
-
2-(N-Morpholino)propane sulfonate buffer
3,6-dichlorobenzo[b]thiophene-2-carboxylic acid
3-chloro-6-fluorobenzo[b]thiophene-2-carboxylic acid
3-methyl-2-oxobutanoate
-
-
4-(2-Thienyl)-2-oxo-3-butenoate
-
2 mM
4-(3-Thienyl)-2-oxo-3-butenoate
-
2 mM
4-hydroxyphenylacetate
-
-
4-hydroxyphenyllactate
-
weak
4-methyl-2-oxopentanoate
-
-
acetate
-
weak, in vivo and in vitro
alpha-Ketoisocaproate
-
inhibits the enzyme by releasing it from the BCKD complex via dissociation
alpha-ketoisovalerate
-
inhibits the enzyme by releasing it from the BCKD complex via dissociation
branched-chain 2-oxo acids
CDP
-
50% inhibition at 0.4 mM, inhibition can be reversed by 2 mM Mg2+
CTP
-
50% inhibition at 0.25 mM, inhibition can be reversed by 2 mM Mg2+
dexamethasone
-
decreases enzyme expression level in renal tubule cells
Furfurylidenepyruvate
-
1.85 mM
GDP
-
50% inhibition at 0.2 mM, inhibition can be reversed by 2 mM Mg2+
GTP
-
50% inhibition at 0.06 mM, inhibition can be reversed by 2 mM Mg2+
methylhydrocinnamic acid
-
Mg2+
-
at concentrations above 1.5 mM, activation below
N,N'-(1,2,5-oxadiazole-3,4-diyl)bis(3,6-dichlorobenzo[b]thiophene-2-carboxamide
N-(4-acetamido-1,2,5-oxadiazol-3-yl)-3,6-dichlorobenzo[b]thiophene-2-carboxamide
phenylpyruvate
-
in vivo and in vitro
UDP
-
50% inhibition at 0.25 mM, inhibition can be reversed by 2 mM Mg2+
UTP
-
50% inhibition at 0.1 mM, inhibition can be reversed by 2 mM Mg2+
2-(N-Morpholino)propane sulfonate buffer
-
-
2-(N-Morpholino)propane sulfonate buffer
-
-
2-(N-Morpholino)propane sulfonate buffer
-
-
2-Chloroisohexanoate
-
-
2-Chloroisohexanoate
-
no inhibition by (R)(-)-2-chloroisopentanoate; potassium phosphate increases sensitivity to this inhibitor
2-Chloroisohexanoate
-
ATP does not protect; i.e. 2-chloro-4-methylpentanoate, strong
2-Chloroisohexanoate
-
no inhibition by (R)(-)-2-chloroisopentanoate; potassium phosphate increases sensitivity to this inhibitor; (R)(+)-isomer is twice as effective as (S)(-)-isomer; site-specific inhibitor
2-Chloroisohexanoate
-
enhanced by monovalent cations and further enhanced by phosphate
2-Chloroisohexanoate
-
50% inhibition at 0.014 mM, no inhibition with histone II-S as substrate
2-Chloroisohexanoate
-
50% inhibition at 0.014 mM
2-oxo-3-methylpentanoate
-
more effective than 2-oxoisopentanoate
2-oxo-3-methylpentanoate
-
-
2-oxo-3-methylpentanoate
-
more effective than 2-oxoisopentanoate
2-oxo-3-methylpentanoate
-
-
2-oxohexanedioate
-
-
2-oxoisocaproate
-
-
2-oxoisocaproate
-
more effective than 2-oxo-3-methylpentanoate and 2-oxoisopentanoate
2-oxoisocaproate
-
kinetics, 40% inhibition at 0.065 mM
2-oxoisocaproate
-
more effective than 2-oxo-3-methylpentanoate and 2-oxoisopentanoate
2-oxoisopentanoate
-
less effective than 2-oxoisohexanoate and 2-oxo-3-methylpentanoate
2-oxoisopentanoate
-
less effective than 2-oxoisohexanoate and 2-oxo-3-methylpentanoate
2-oxopentanoate
-
-
2-oxopentanoate
-
kinetics
3,6-dichlorobenzo[b]thiophene-2-carboxylic acid
Q14874
-
3,6-dichlorobenzo[b]thiophene-2-carboxylic acid
-
3-chloro-6-fluorobenzo[b]thiophene-2-carboxylic acid
Q14874
-
3-chloro-6-fluorobenzo[b]thiophene-2-carboxylic acid
-
4-hydroxyphenylpyruvate
-
-
4-hydroxyphenylpyruvate
-
very weak: 3-hydroxyphenylpyruvate
acetoacetyl-CoA
-
-
acetoacetyl-CoA
-
40% inhibition at 0.01 mM
ADP
-
-
ADP
-
50% inhibition at 0.4 mM, inhibition can be reversed by 2 mM Mg2+
ADP
-
50% inhibition at 0.4 mM, inhibition can be reversed by 2 mM Mg2+
ADP
-
50% inhibition at 0.4 mM, inhibition can be reversed by 2 mM Mg2+
alpha-Chloroisocaproate
-
inhibits the enzyme by releasing it from the BCKD complex via dissociation
alpha-Chloroisocaproate
-
-
ATP
-
50% inhibition at 0.2 mM, inhibition can be reversed by 2 mM Mg2+
branched-chain 2-oxo acids
-
-
branched-chain 2-oxo acids
-
-
branched-chain 2-oxo acids
-
-
Ca2+
-
weak
Clofibric acid
-
Clofibric acid
-
in vivo and in vitro
Dichloroacetate
-
weak
Dichloroacetate
-
ATP slightly protects
Dichloroacetate
-
50% inhibition at 1.8 mM
heparin
-
-
heparin
-
40% inhibition at 0.012 mg/ml
heparin
-
50% inhibition at 0.002 mM
methylmalonyl-CoA
-
-
methylmalonyl-CoA
-
40% inhibition at 0.2 mM
N,N'-(1,2,5-oxadiazole-3,4-diyl)bis(3,6-dichlorobenzo[b]thiophene-2-carboxamide
Q14874
-
N,N'-(1,2,5-oxadiazole-3,4-diyl)bis(3,6-dichlorobenzo[b]thiophene-2-carboxamide
-
N-(4-acetamido-1,2,5-oxadiazol-3-yl)-3,6-dichlorobenzo[b]thiophene-2-carboxamide
Q14874
-
N-(4-acetamido-1,2,5-oxadiazol-3-yl)-3,6-dichlorobenzo[b]thiophene-2-carboxamide
-
n-Octanoate
-
-
n-Octanoate
-
40% inhibition at 0.5 mM
NADP+
-
-
NADP+
-
40% inhibition at 1.5 mM
phenylacetate
-
Phenyllactate
-
-
pyruvate
-
-
thiamine diphosphate
-
-
thiamine diphosphate
-
inhibits phosphorylation of wild-type E1, mutant E1-S303A and mutant E1-D296A/S303A, but not phosphorylation of mutant E1-H292A
thiamine diphosphate
Ca2+-dependent inhibition
additional information
-
no inhibition by acetyl-CoA; no inhibition by coenzyme A
-
additional information
-
no inhibition by coenzyme A; no inhibition by isovaleryl-CoA
-
additional information
-
no inhibition by 2-chloropropionate
-
additional information
-
no inhibition by GTP
-
additional information
-
no inhibition by lactate
-
additional information
-
no inhibition by acetate; no inhibition by acetyl-CoA; no inhibition by lactate; no inhibition by methylcrotonyl-CoA, beta-hydroxy-beta-methylglutaryl-CoA, crotonyl-CoA, octanoyl-CoA, succinyl-CoA, propionyl-CoA, 0.1 mM each, propionate, beta-hydroxybutyrate, acetoacetate, malonate, alpha-ketomalonate, succinate, citrate, oxaloacetate, FAD+, NADPH, 2 mM; no inhibition by NADH, NAD+ 1 mM each
-
additional information
-
no inhibition by DL-leucine
-
additional information
-
no inhibition by isovaleryl-CoA
-
additional information
-
no inhibition by 2-chloropropionate
-
additional information
-
-
-
additional information
-
binding of thiamin diphosphate cofactor to branched-chain alpha-keto acid decarboxylase/dehydrogenase, which induces a phosphorylation loop conformation change, inhibits the phosphorylation of the protein by the BCKD kinase, no inhibition of phosphorylation of mutant R287A, D295A, Y300F, and R301A E1B components
-
additional information
-
clofibric acid and thiamine diphosphate do not affect the protein-protein interaction of BDK with the BCKD complex
-
additional information
negligible inhibition by butanoic acid and dodecanoic acid
-
additional information
-
no inhibition by isovaleryl-CoA
-
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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.
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1985
Bos taurus, Oryctolagus cuniculus, Rattus norvegicus
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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
1038
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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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1988
Oryctolagus cuniculus, Rattus norvegicus
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Paxton, R.
Branched-chain alpha-keto acid dehydrogenase and its kinase from rabbit liver and heart
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1988
Bos taurus, Oryctolagus cuniculus, Rattus norvegicus
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Paxton, R.; Harris, R.A.
Isolation of rabbit liver branched chain alpha-ketoacid dehydrogenase and regulation by phosphorylation
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1982
Oryctolagus cuniculus
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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
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1995
Rattus norvegicus
brenda
Odessey, R.
Purification of rat kidney branched-chain oxo acid dehydrogenase complex with endogenous kinase activity
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1982
Rattus norvegicus
brenda
Lau, K.S.; Fatania, H.R.; Randle, P.J.
Regulation of the branched chain 2-oxoacid dehydrogenase kinase reaction
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1982
Bos taurus
brenda
Lawson, R.; Cook, K.G.; Yeaman, S.J.
Rapid purification of bovine kidney branched-chain 2-oxoacid dehydrogenase complex containing endogenous kinase activity
FEBS Lett.
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1982
Bos taurus
brenda
Cook, K.G.; Lawson, R.; Yeaman, S.J.
Multi-site phosphorylation of bovine kidney branched-chain 2-oxoacid dehydrogenase complex
FEBS Lett.
157
59-62
1982
Bos taurus
brenda
Paxton, R.; Harris, R.A.
Clofibric acid, phenylpyruvate, and dichloroacetate inhibition of branched-chain alpha-ketoacid dehydrogenase kinase in vitro and in perfused rat heart
Arch. Biochem. Biophys.
231
58-66
1984
Oryctolagus cuniculus, Rattus norvegicus
brenda
Paxton, R.; Harris, R.A.
Regulation of branched-chain alpha-ketoacid dehydrogenase kinase
Arch. Biochem. Biophys.
231
48-57
1984
Oryctolagus cuniculus
brenda
Harris, R.A.; Paxton, R.; DePaoli-Roach, A.
Inhibition of branched chain alpha-ketoacid dehydrogenase kinase activity by alpha-chloroisocaproate
J. Biol. Chem.
257
13915-13918
1982
Oryctolagus cuniculus
brenda
Shimomura, Y.; Kuntz, M.J.; Suzuki, M.; Ozawa, T.; Harris, R.A.
Monovalent cations and inorganic phosphate alter branched-chain alpha-ketoacid dehydrogenase-kinase activity and inhibitor sensitivity
Arch. Biochem. Biophys.
266
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1988
Rattus norvegicus
brenda
Espinal, J.; Beggs, M.; Randle, P.J.
Assay of branched-chain alpha-keto acid dehydrogenase kinase in mitochondrial extracts and purified branched-chain alpha-keto acid dehydrogenase complexes
Methods Enzymol.
166
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1988
Bos taurus, Oryctolagus cuniculus, Rattus norvegicus
brenda
Shimomura, Y.; Nanaumi, N.; Suzuki, M.; Popov, K.M.; Harris, R.A.
Purification and partial characterization of branched-chain alpha-ketoacid dehydrogenase kinase from rat liver and rat heart
Arch. Biochem. Biophys.
283
293-299
1990
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Popov, K.M.; Zhao, Y.; Shimomura, Y.; Kuntz, M.J.; Harris, R.A.
Branched-chain alpha-ketoacid dehydrogenase kinase. Molecular cloning, expression, and sequence similarity with histidine protein kinases
J. Biol. Chem.
267
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1992
Rattus norvegicus
brenda
Lee, H.Y.; Hall, T.B.; Kee, S.M.; Tung, H.Y.L.; Reed, L.J.
Purification and properties of branched-chain alpha-keto acid dehydrogenase kinase from bovine kidney
BioFactors
3
109-112
1991
Bos taurus
brenda
Davie, J.R.; Wynn, R.M.; Meng, M.; Huang, Y.S.; Aalund, G.; Chuang, D.T.; Lau, K.S.
Expression and characterization of branched-chain alpha-ketoacid dehydrogenase kinase from the rat. Is it a histidine-protein kinase?
J. Biol. Chem.
270
19861-19867
1995
Rattus norvegicus
brenda
Doering, C.B.; Coursey, C.; Spangler, W.; Danner, D.J.
Murine branched chain alpha-ketoacid dehydrogenase kinase; cDNA cloning, tissue distribution, and temporal expression during embryonic development
Gene
212
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1998
Mus musculus, Mus musculus C57/BL6J
brenda
Doering, C.B.; Danner, D.J.
Expression of murine branched-chain alpha-keto acid dehydrogenase kinase
Methods Enzymol.
324
491-497
2000
Mus musculus, Mus musculus C57/BL6J
brenda
Fujii, H.; Shimomura, Y.; Murakami, T.; Nakai, N.; Sato, T.; Suzuki, M.; Harris, R.A.
Branched-chain alpha-keto acid dehydrogenase kinase content in rat skeletal muscle is decreased by endurance training
Biochem. Mol. Biol. Int.
44
1211-1216
1998
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Machius, M.; Chuang, J.L.; Wynn, R.M.; Tomchick, D.R.; Chuang, D.T.
Structure of rat BCKD kinase: nucleotide-induced domain communication in a mitochondrial protein kinase
Proc. Natl. Acad. Sci. USA
98
11218-11223
2001
Rattus norvegicus (Q00972)
brenda
Nakai, N.; Kobayashi, R.; Popov, K.M.; Harris, R.A.; Shimomura, Y.
Determination of branched-chain alpha-keto acid dehydrogenase activity state and branched-chain alpha-keto acid dehydrogenase kinase activity and protein in mammalian tissues
Methods Enzymol.
324
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2000
Rattus norvegicus
brenda
Nellis, M.M.; Doering, C.B.; Kasinski, A.; Danner, D.J.
Insulin increases branched-chain alpha-ketoacid dehydrogenase kinase expression in Clone 9 rat cells
Am. J. Physiol.
283
E853-E860
2002
Rattus norvegicus
brenda
Obayashi, M.; Sato, Y.; Harris, R.A.; Shimomura, Y.
Regulation of the activity of branched-chain 2-oxo acid dehydrogenase (BCODH) complex by binding BCODH kinase
FEBS Lett.
491
50-54
2001
Rattus norvegicus
brenda
Popov, K.M.; Shimomura, Y.; Hawes, J.W.; Harris, R.A.
Branched-chain alpha-keto acid dehydrogenase kinase
Methods Enzymol.
324
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2000
Rattus norvegicus
brenda
Popov, K.M.; Zhao, Y.; Shimomura, Y.; Jaskiewicz, J.; Kedishvili, N.Y.; Irwin, J.; Goodwin, G.W.; Harris, R.A.
Dietary control and tissue specific expression of branched-chain alpha-ketoacid dehydrogenase kinase
Arch. Biochem. Biophys.
316
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1995
Rattus norvegicus
brenda
Li, J.; Wynn, R.M.; Machius, M.; Chuang, J.L.; Karthikeyan, S.; Tomchick, D.R.; Chuang, D.T.
Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain alpha-keto acid decarboxylase/dehydrogenase
J. Biol. Chem.
279
32968-32978
2004
Rattus norvegicus
brenda
Wang, X.; Price, S.R.
Differential regulation of branched-chain alpha-ketoacid dehydrogenase kinase expression by glucocorticoids and acidification in LLC-PK1-GR101 cells
Am. J. Physiol. Renal. Physiol.
286
F504-508
2004
Sus scrofa
brenda
Muller, E.A.; Danner, D.J.
Tissue-specific translation of murine branched-chain alpha-ketoacid dehydrogenase kinase mRNA is dependent upon an upstream open reading frame in the 5'-untranslated region
J. Biol. Chem.
279
44645-44655
2004
Mus musculus
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
Howarth, K.R.; Burgomaster, K.A.; Phillips, S.M.; Gibala, M.J.
Exercise training increases branched-chain oxoacid dehydrogenase kinase content in human skeletal muscle
Am. J. Physiol.
293
R1335-R1341
2007
Homo sapiens
brenda
Kuzuya, T.; Katano, Y.; Nakano, I.; Hirooka, Y.; Itoh, A.; Ishigami, M.; Hayashi, K.; Honda, T.; Goto, H.; Fujita, Y.; Shikano, R.; Muramatsu, Y.; Bajotto, G.; Tamura, T.; Tamura, N.; Shimomura, Y.
Regulation of branched-chain amino acid catabolism in rat models for spontaneous type 2 diabetes mellitus
Biochem. Biophys. Res. Commun.
373
94-98
2008
Rattus norvegicus
brenda
Akita, K.; Fujimura, Y.; Bajotto, G.; Shimomura, Y.
Inhibition of branched-chain alpha-ketoacid dehydrogenase kinase by thiamine pyrophosphate at different potassium ionic levels
Biosci. Biotechnol. Biochem.
73
1189-1191
2009
Rattus norvegicus
brenda
Doisaki, M.; Katano, Y.; Nakano, I.; Hirooka, Y.; Itoh, A.; Ishigami, M.; Hayashi, K.; Goto, H.; Fujita, Y.; Kadota, Y.; Kitaura, Y.; Bajotto, G.; Kazama, S.; Tamura, T.; Tamura, N.; Feng, G.G.; Ishikawa, N.; Shimomura, Y.
Regulation of hepatic branched-chain alpha-keto acid dehydrogenase kinase in a rat model for type 2 diabetes mellitus at different stages of the disease
Biochem. Biophys. Res. Commun.
393
303-307
2010
Rattus norvegicus
brenda
Novarino, G.; El-Fishawy, P.; Kayserili, H.; Meguid, N.; Scott, E.; Schroth, J.; Silhavy, J.; Kara, M.; Khalil, R.; Ben-Omran, T.; Ercan-Sencicek, A.; Hashish, A.; Sanders, S.; Gupta, A.; Hashem, H.; Matern, D.; Gabriel, S.; Sweetman, L.; Rahimi, Y.; Harr
Mutations in BCKD-kinase lead to a potentially treatable form of autism with epilepsy
Science
338
394-397
2012
Homo sapiens
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
Garcia-Cazorla, A.; Oyarzabal, A.; Fort, J.; Robles, C.; Castejon, E.; Ruiz-Sala, P.; Bodoy, S.; Merinero, B.; Lopez-Sala, A.; Dopazo, J.; Nunes, V.; Ugarte, M.; Artuch, R.; Palacin, M.; Rodriguez-Pombo, P.; Alcaide, P.; Navarrete, R.; Sanz, P.; Font-Llitjos, M.; Vilaseca, M.A.; Ormaizabal, A.; P, P.r.
Two novel mutations in the BCKDK (branched-chain keto-acid dehydrogenase kinase) gene are responsible for a neurobehavioral deficit in two pediatric unrelated patients
Hum. Mutat.
35
470-477
2014
Homo sapiens (Q14874), Homo sapiens
brenda
Tso, S.C.; Gui, W.J.; Wu, C.Y.; Chuang, J.L.; Qi, X.; Skvora, K.J.; Dork, K.; Wallace, A.L.; Morlock, L.K.; Lee, B.H.; Hutson, S.M.; Strom, S.C.; Williams, N.S.; Tambar, U.K.; Wynn, R.M.; Chuang, D.T.
Benzothiophene carboxylate derivatives as novel allosteric inhibitors of branched-chain alpha-ketoacid dehydrogenase kinase
J. Biol. Chem.
289
20583-20593
2014
Mus musculus (O55028), Mus musculus, Homo sapiens (Q14874), Homo sapiens
brenda
Kadota, Y.; Toyoda, T.; Hayashi-Kato, M.; Kitaura, Y.; Shimomura, Y.
Octanoic acid promotes branched-chain amino acid catabolisms via the inhibition of hepatic branched-chain alpha-keto acid dehydrogenase kinase in rats
Metab. Clin. Exp.
64
1157-1164
2015
Rattus norvegicus (Q00972)
brenda
Zigler, J.S.; Hodgkinson, C.A.; Wright, M.; Klise, A.; Sundin, O.; Broman, K.W.; Hejtmancik, F.; Huang, H.; Patek, B.; Sergeev, Y.; Hose, S.; Brayton, C.; Xaiodong, J.; Vasquez, D.; Maragakis, N.; Mori, S.; Goldman, D.; Hoke, A.; Sinha, D.
A spontaneous missense mutation in branched chain keto acid dehydrogenase kinase in the rat affects both the central and peripheral nervous systems
PLoS ONE
11
e0160447
2016
Rattus norvegicus (Q00972)
brenda
Hatazawa, Y.; Tadaishi, M.; Nagaike, Y.; Morita, A.; Ogawa, Y.; Ezaki, O.; Takai-Igarashi, T.; Kitaura, Y.; Shimomura, Y.; Kamei, Y.; Miura, S.
PGC-1alpha-mediated branched-chain amino acid metabolism in the skeletal muscle
PLoS ONE
9
e91006
2014
Mus musculus (O55028), Mus musculus
brenda
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
110
9728-9733
2013
Mus musculus (O55028)
brenda
Noguchi, S.; Kondo, Y.; Ito, R.; Katayama, T.; Kazama, S.; Kadota, Y.; Kitaura, Y.; Harris, R.A.; Shimomura, Y.
Ca2+-dependent inhibition of branched-chain alpha-ketoacid dehydrogenase kinase by thiamine pyrophosphate
Biochem. Biophys. Res. Commun.
504
916-920
2018
Rattus norvegicus (Q00972)
brenda
Xue, P.; Zeng, F.; Duan, Q.; Xiao, J.; Liu, L.; Yuan, P.; Fan, L.; Sun, H.; Malyarenko, O.S.; Lu, H.; Xiu, R.; Liu, S.; Shao, C.; Zhang, J.; Yan, W.; Wang, Z.; Zheng, J.; Zhu, F.
BCKDK of BCAA catabolism cross-talking with the MAPK pathway promotes tumorigenesis of colorectal cancer
EBioMedicine
20
50-60
2017
Homo sapiens (O13874), Homo sapiens
brenda
Krishnan, B.; Massilamany, C.; Basavalingappa, R.H.; Gangaplara, A.; Kang, G.; Li, Q.; Uzal, F.A.; Strande, J.L.; Delhon, G.A.; Riethoven, J.J.; Steffen, D.; Reddy, J.
Branched chain alpha-ketoacid dehydrogenase kinase 111-130, a T cell epitope that induces both autoimmune myocarditis and hepatitis in A/J mice
Immun. Inflamm. Dis.
5
421-434
2017
Mus musculus (O55028)
brenda
Samuel Zigler, J.; Hodgkinson, C.; Wright, M.; Klise, A.; Sundin, O.; Broman, K.; Hejtmancik, F.; Huang, H.; Patek, B.; Sergeev, Y.; Hose, S.; Brayton, C.; Xaiodong, J.; Vasquez, D.; Maragakis, N.; Mori, S.; Goldman, D.; Hoke, A.; Sinha, D.
A spontaneous missense mutation in branched chain keto acid dehydrogenase kinase in the rat affects both the central and peripheral nervous systems
PLoS ONE
11
e0160447
2016
Rattus norvegicus (Q00972)
brenda
Xu, M.; Kitaura, Y.; Ishikawa, T.; Kadota, Y.; Terai, C.; Shindo, D.; Morioka, T.; Ota, M.; Morishita, Y.; Ishihara, K.; Shimomura, Y.
Endurance performance and energy metabolism during exercise in mice with a muscle-specific defect in the control of branched-chain amino acid catabolism
PLoS ONE
12
e0180989
2017
Mus musculus (O55028)
brenda