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Information on EC 2.7.11.4 - [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase and Organism(s) Rattus norvegicus and UniProt Accession Q00972
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2.7.11.4 [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinaseIUBMB Comments
The enzyme has no activating compound but is specific for its substrate. It is a mitochondrial enzyme associated with the branched-chain 2-oxoacid dehydrogenase complex. Phosphorylation inactivates EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring).
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Word Map
- 2.7.11.4
- alpha-ketoacids
-
bckas
- alpha-chloroisocaproate
-
maple
- e1alpha
- syrup
- alpha-ketoisocaproate
-
transacylase
- alpha-ketoisovalerate
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
bckdk, bckdh kinase, branched-chain alpha-ketoacid dehydrogenase kinase, bckd kinase, branched-chain alpha-keto acid dehydrogenase kinase, bckd-kinase, branched-chain 2-oxo acid dehydrogenase kinase, bcka dehydrogenase kinase, branched chain alpha-ketoacid dehydrogenase kinase, bckdc kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BCK
-
-
-
-
BCKDH kinase
branched-chain 2-oxo acid dehydrogenase kinase
-
-
-
-
branched-chain alpha-keto acid dehydrogenase kinase
branched-chain alpha-ketoacid dehydrogenase kinase
branched-chain keto acid dehydrogenase kinase
-
-
-
-
kinase, branched-chain oxo acid dehydrogenase (phosphorylating)
-
-
-
-
additional information
-
kinase activity is an intrinsic activity of branched-chain oxo acid dehydrogenase complex
BCKDH kinase
-
-
-
-
branched-chain alpha-keto acid dehydrogenase kinase
-
-
-
-
branched-chain alpha-ketoacid dehydrogenase kinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphotransferase
The enzyme has no activating compound but is specific for its substrate. It is a mitochondrial enzyme associated with the branched-chain 2-oxoacid dehydrogenase complex. Phosphorylation inactivates EC 1.2.4.4, 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring).
CAS REGISTRY NUMBER
COMMENTARY
82391-38-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate 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
-
-
?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
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 (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] 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
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 + 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 + [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
-
-
?
additional information
?
-
enzyme has also ATPase activity in absence of E1
-
-
?
additional information
?
-
-
R288A mutant of E1 is not phosphorylated by the enzyme
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)]
ADP + [3-methyl-2-oxobutanoate 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
-
-
?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase
ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase
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 (lipoamide)]
ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate
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
-
-
?
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
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 + 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 (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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
2-Chloroisohexanoate
-
(R)(+)-isomer is twice as effective as (S)(-)-isomer
2-Chloroisohexanoate
-
50% inhibition at 0.014 mM, no inhibition with histone II-S as substrate
2-Chloroisohexanoate
-
potassium phosphate increases sensitivity to this inhibitor
2-Chloroisohexanoate
-
enhanced by monovalent cations and further enhanced by phosphate
2-oxoisocaproate
-
more effective than 2-oxo-3-methylpentanoate and 2-oxoisopentanoate
2-oxoisopentanoate
-
less effective than 2-oxoisohexanoate and 2-oxo-3-methylpentanoate
alpha-Chloroisocaproate
-
inhibits the enzyme by releasing it from the BCKD complex via dissociation
thiamine diphosphate
-
inhibits phosphorylation of wild-type E1, mutant E1-S303A and mutant E1-D296A/S303A, but not phosphorylation of mutant E1-H292A
additional information
negligible inhibition by butanoic acid and dodecanoic acid
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
dietary supplementation of branched-chain amino acid over several weeks increases the enzyme activity in spontaneous type II diabetic rats, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0025
thiamine diphosphate
Rattus norvegicus
pH 7.4, 30°C, in the presence of 0.001 mM Ca2+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
-
type 2 diabetes Otsuka Long-Evans Tokushima Fatty rats and Zucker diabetic fatty rats
-
activity of BDK is higher in fatty diabetic rats than in lean non-diabetic rats
-
enzyme content decreases 0.7fold after running exercise for 5 weeks
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
2 forms: first form is bound to E2, second form is free and seems to be inactive
-
part of intramitochondrial branched-chain 2-oxoacid dehydrogenase complex
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme (Bckdk) is an integral part of an enzyme complex located in the mitochondrial matrix of many tissues which regulates the levels of the branched-chain amino acids (BCAAs), leucine, isoleucine and valine
malfunction
-
the BDK activity is decreased in the livers of streptozotocin-induced diabetic rats
metabolism
-
the enzyme is involved in the regulation of the branched-chain alpha-keto acid dehydrogenase complex by inactivating it through phopshorylation, complex regulation and effects of the drug benzofibrate, overview
physiological function
-
branched-chain alpha-keto acid dehydrogenase kinase is responsible for the regulation of branched-chain alpha-keto acid dehydrogenase complex, which is the rate-limiting enzyme in the catabolism of branched-chain amino acids
additional information
-
activity of BDK practically corresponds with plasma insulin concentrations
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BCKD_RAT
412
0
46474
Swiss-Prot
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimerizes through direct interaction of two opposing nucleotide-binding domains, crystallographic data
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
circulating levels of the branched-chain amino acids (BCAAs) are reduced by 70-80% in animals homozygous for the mutation causing a phenotype named frogleg. The mutationis located within the kinase domain of Bckdk. The frogleg phenotype shares important characteristics with a previously described Bckdk knockout mouse and with human subjects with Bckdk mutations. The mutation affects both the central and peripheral nervous systems
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
precipitation of branched-chain oxo acid dehydrogenase enzyme complex at acid pH-values, especially below 6.5, results in specific loss of kinase activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
liver enzyme, heart enzyme and recombinant enzyme expressed in Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
insulin is known to increase the enzyme expression in cultured rat hepatocytes
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
27
41-49
1985
Bos taurus, Oryctolagus cuniculus, Rattus norvegicus
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
Oryctolagus cuniculus, Rattus norvegicus
Paxton, R.
Branched-chain alpha-keto acid dehydrogenase and its kinase from rabbit liver and heart
Methods Enzymol.
166
313-320
1988
Bos taurus, Oryctolagus cuniculus, Rattus norvegicus
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
Odessey, R.
Purification of rat kidney branched-chain oxo acid dehydrogenase complex with endogenous kinase activity
Biochem. J.
204
353-356
1982
Rattus norvegicus
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
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
210-218
1988
Rattus norvegicus
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
166-175
1988
Bos taurus, Oryctolagus cuniculus, Rattus norvegicus
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
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
13127-13130
1992
Rattus norvegicus
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
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
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)
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
48-62
2000
Rattus norvegicus
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
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
Popov, K.M.; Shimomura, Y.; Hawes, J.W.; Harris, R.A.
Branched-chain alpha-keto acid dehydrogenase kinase
Methods Enzymol.
324
162-178
2000
Rattus norvegicus
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
148-154
1995
Rattus norvegicus
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
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
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
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
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
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
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)
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)
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)
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)
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