Information on EC 2.7.11.4 -

Information on EC 2.7.11.4 - [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase:

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EC NUMBER	COMMENTARY
2.7.11.4	-

RECOMMENDED NAME	GeneOntology No.
[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase	GO:0047323

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
ATP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] = ADP + [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] phosphate		-	-	-	-

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
phospho group transfer	-	-	-	-

PATHWAY	KEGG Link	MetaCyc Link
No entries in this field

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).

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
BCK	-	-	-	-
BCKD kinase	Rattus norvegicus	-	-	656230
BCKD kinase	Sus scrofa	-	-	660683
BCKD kinase	Mus musculus	-	-	662283
BCKDH	Rattus norvegicus	-	-	690740
BCKDH kinase	-	-	-	-
BCOAD	Homo sapiens	-	-	690337
BDK	Rattus norvegicus	-	-	662695
branched-chain 2-oxo acid dehydrogenase kinase	-	-	-	-
branched-chain alpha-keto acid decarboxylase/dehydrogenase kinase	Rattus norvegicus	-	-	656230
branched-chain alpha-keto acid dehydrogenase	Rattus norvegicus	-	-	690740
branched-chain alpha-keto acid dehydrogenase kinase	-	-	-	-
branched-chain alpha-keto acid dehydrogenase kinase	Rattus norvegicus	-	-	662695
branched-chain alpha-ketoacid dehydrogenase kinase	-	-	-	-
branched-chain alpha-ketoacid dehydrogenase kinase	Sus scrofa	-	-	660683
branched-chain alpha-ketoacid dehydrogenase kinase	Mus musculus	-	-	662283
branched-chain alpha-ketoacid dehydrogenase kinase	Rattus norvegicus	-	-	702742
branched-chain keto acid dehydrogenase kinase	-	-	-	-
branched-chain oxoacid dehydrogenase complex	Homo sapiens	-	-	690337
branched-chain oxoacid dehydrogenase kinase	Homo sapiens	-	-	690337
kinase, branched-chain oxo acid dehydrogenase (phosphorylating)	-	-	-	-
additional information	Rattus norvegicus	-	kinase activity is an intrinsic activity of branched-chain oxo acid dehydrogenase complex	587061

CAS REGISTRY NUMBER	COMMENTARY
82391-38-6	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Bos taurus	-	349051, 349056, 640575, 640576, 640577, 640583, 640588, 94884	-	-
Homo sapiens	-	690337	-	-
Mus musculus	-	662283	-	-
Mus musculus	mouse, C57BL/6J	640590, 640591	-	-
Oryctolagus cuniculus	-	349052, 349056, 349073, 640578, 640579, 640580, 640583, 94884	-	-
Rattus norvegicus	-	349052, 349056, 349090, 587061, 640578, 640581, 640583, 640587, 640589, 640595, 640598, 656230, 662695, 690740, 702742, 94884	-	-
Rattus norvegicus	-	640594	Q00972	Uniprot
Rattus norvegicus	clone 9 cells express higher amounts of the enzyme after insulin treatment	640596	-	-
Rattus norvegicus	female Sprague-Dawley	640597	-	-
Rattus norvegicus	male Wistar	640599	-	-
Rattus norvegicus	Sprague-Dawley	640585, 640592	-	-
Sus scrofa	-	660683	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase	ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase		Mus musculus	-	-	662283	-	-	?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase	ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase		Rattus norvegicus	-	inactivation of the substrate enzyme	656230	-	-	?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase	ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase		Mus musculus	-	the catalyzed reversible specific phosphorylation of the BCKD subunit regulates the first committed step in the pathway for leucine, isoleucine, and valine catabolism	662283	-	-	?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase	ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase		Rattus norvegicus	-	the enzyme catalyzes the regulatory inactivation of the rate limiting enzyme in branched-chain amino acid catabolism, 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	662695	-	-	?
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase	ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase		Rattus norvegicus	-	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	656230	-	-	?
ATP + histone II-S	?		Rattus norvegicus	-	-	640585, 640598	-	-	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	-	349090, 640578, 640581, 640585, 640587, 640589, 640592, 640595, 640598, 640599	-	-	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Bos taurus	-	-	349051, 640588	-	-	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Oryctolagus cuniculus	-	-	640578, 640579, 640580	-	-	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Bos taurus	-	phosphorylates alpha-subunit of multienzyme complex component E1	640575	-	640575	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Bos taurus	-	phosphorylates alpha-subunit of multienzyme complex component E1	640576	-	640576	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	2 Ser-residues in E1-alpha-subunit	94884	-	94884	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	2 Ser-residues in E1-alpha-subunit	349052	-	349052	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	2 Ser-residues in E1-alpha-subunit	349056	-	349056	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	2 Ser-residues in E1-alpha-subunit	640583	-	640583	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Bos taurus	-	2 Ser-residues in E1-alpha-subunit	94884	-	94884	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Bos taurus	-	2 Ser-residues in E1-alpha-subunit	349056	-	349056	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Bos taurus	-	2 Ser-residues in E1-alpha-subunit	640583	-	640583	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Oryctolagus cuniculus	-	2 Ser-residues in E1-alpha-subunit	94884	-	94884	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Oryctolagus cuniculus	-	2 Ser-residues in E1-alpha-subunit	349052	-	349052	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Oryctolagus cuniculus	-	2 Ser-residues in E1-alpha-subunit	349056	-	349056	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Oryctolagus cuniculus	-	2 Ser-residues in E1-alpha-subunit	640583	-	640583	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Bos taurus	-	incorporates 0.8 mol phosphate/mol alpha-subunit	640576	-	640576	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	tight binding to multienzyme complex is required for phosphorylation, free enzyme is inactive	640597	-	-	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	Ser-residues of MW 46000-subunit	587061	-	587061	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Bos taurus	-	Ser-residues of MW 46000-subunit	640575	-	640575	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Oryctolagus cuniculus	-	GTP cannot replace ATP	349073	-	-	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Bos taurus	-	phosphorylates alpha-subunit of multienzyme complex component E1 and additional sites not associated with inactivation of the enzyme	640577	-	640577	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Oryctolagus cuniculus	-	phosphorylates exclusively MW 47000 subunit of substrate	349073	-	-	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Oryctolagus cuniculus	-	incorporates 0.75 mol phosphate per mol phosphorylation site and 1.5 mol/mol alpha-subunit	349056	-	349056	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	branched-chain amino acid metabolism	349052, 640595	-	-	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Oryctolagus cuniculus	-	branched-chain amino acid metabolism	349052	-	-	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	regulatory enzyme of branched-chain 2-oxoacid dehydrogenase complex	640595	-	-	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Bos taurus	-	regulatory enzyme of branched-chain 2-oxoacid dehydrogenase complex	349051	-	-	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	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		Bos taurus	-	phosphorylation inactivates EC 1.2.4.4	94884, 349051, 349056, 640575, 640576, 640577, 640583, 640588	-	-	?
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Oryctolagus cuniculus	-	phosphorylation inactivates EC 1.2.4.4	94884, 349052, 349056, 349073, 640578, 640579, 640580, 640583	-	-	?
additional information	?	-	Rattus norvegicus	-	R288A mutant of E1 is not phosphorylated by the enzyme	349090	-	-	-
additional information	?	-	Rattus norvegicus	Q00972	enzyme has also ATPase activity in absence of E1	640594	-	-	-
additional information	?	-	Sus scrofa	-	BCKD kinase transcription regulation, overview	660683	-	-	-
additional information	?	-	Rattus norvegicus	-	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	690740	-	-	-
additional information	?	-	Homo sapiens	-	the branched-chain oxoacid dehydrogenase complex, BCOAD, is rate determining for the oxidation of branched-chain amino acids in skeletal muscle	690337	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase	ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase		Rattus norvegicus	-	inactivation of the substrate enzyme	656230	-	-
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase	ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase		Mus musculus	-	the catalyzed reversible specific phosphorylation of the BCKD subunit regulates the first committed step in the pathway for leucine, isoleucine, and valine catabolism	662283	-	-
ATP + branched-chain alpha-keto acid decarboxylase/dehydrogenase	ADP + phosphorylated branched-chain alpha-keto acid decarboxylase/dehydrogenase		Rattus norvegicus	-	the enzyme catalyzes the regulatory inactivation of the rate limiting enzyme in branched-chain amino acid catabolism	662695	-	-
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	branched-chain amino acid metabolism	349052, 640595	-	-
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Oryctolagus cuniculus	-	branched-chain amino acid metabolism	349052	-	-
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	regulatory enzyme of branched-chain 2-oxoacid dehydrogenase complex	640595	-	-
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Bos taurus	-	regulatory enzyme of branched-chain 2-oxoacid dehydrogenase complex	349051	-	-
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Rattus norvegicus	-	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		Bos taurus	-	phosphorylation inactivates EC 1.2.4.4	94884, 349051, 349056, 640575, 640576, 640577, 640583, 640588	-	-
ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]	ADP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate		Oryctolagus cuniculus	-	phosphorylation inactivates EC 1.2.4.4	94884, 349052, 349056, 349073, 640578, 640579, 640580, 640583	-	-
additional information	?	-	Sus scrofa	-	BCKD kinase transcription regulation, overview	660683	-	-
additional information	?	-	Rattus norvegicus	-	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	690740	-	-
additional information	?	-	Homo sapiens	-	the branched-chain oxoacid dehydrogenase complex, BCOAD, is rate determining for the oxidation of branched-chain amino acids in skeletal muscle	690337	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
ATP	Rattus norvegicus	-	-	656230, 662695	2D-image
ATP	Mus musculus	-	-	662283	2D-image
Calmodulin	Oryctolagus cuniculus	-	activation	349073	2D-image

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
EGTA	Oryctolagus cuniculus	-	activation, presumably by chelation of Ca2+	349056
EGTA	Oryctolagus cuniculus	-	0.1 mM	349073
K+	Rattus norvegicus	-	activation, 0.1 M	640581
K+	Rattus norvegicus	-	-	702742
Mg2+	Rattus norvegicus	-	-	349056, 656230
Mg2+	Bos taurus	-	-	349056
Mg2+	Oryctolagus cuniculus	-	maximum activity at 1.5 mM, inhibits above 1.5 mM	349056
Mg2+	Oryctolagus cuniculus	-	Km-value: 0.025 mM; requirement, actual substrate: MgATP2-	349073
Mg2+	Bos taurus	-	requirement, actual substrate: MgATP2-	640575, 640576, 640583
Mg2+	Rattus norvegicus	-	requirement, actual substrate: MgATP2-	640581, 640583
Rb+	Rattus norvegicus	-	activation	640581
Mg2+	Oryctolagus cuniculus	-	requirement, actual substrate: MgATP2-	640583
additional information	Oryctolagus cuniculus	-	no activation by Ca2+	349073
additional information	Rattus norvegicus	-	no activation by Li+, Na+	640581

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
2-(N-Morpholino)propane sulfonate buffer	Bos taurus, Oryctolagus cuniculus, Rattus norvegicus	-	-	640583	2D-image
2-Chloroisohexanoate	Oryctolagus cuniculus	-	no inhibition by (R)(-)-2-chloroisopentanoate; potassium phosphate increases sensitivity to this inhibitor	349052	2D-image
2-Chloroisohexanoate	Rattus norvegicus	-	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	349052	2D-image
2-Chloroisohexanoate	Oryctolagus cuniculus	-	-	349056, 640579	2D-image
2-Chloroisohexanoate	Bos taurus, Rattus norvegicus	-	-	349056	2D-image
2-Chloroisohexanoate	Oryctolagus cuniculus	-	ATP does not protect; i.e. 2-chloro-4-methylpentanoate, strong	640580	2D-image
2-Chloroisohexanoate	Rattus norvegicus	-	enhanced by monovalent cations and further enhanced by phosphate	640581	2D-image
2-Chloroisohexanoate	Rattus norvegicus	-	50% inhibition at 0.014 mM, no inhibition with histone II-S as substrate	640585	2D-image
2-Chloroisohexanoate	Rattus norvegicus	-	50% inhibition at 0.014 mM	640598	2D-image
2-oxo-3-methylpentanoate	Oryctolagus cuniculus, Rattus norvegicus	-	more effective than 2-oxoisopentanoate	349052	2D-image
2-oxo-3-methylpentanoate	Oryctolagus cuniculus	-	-	349056, 640579	2D-image
2-oxo-3-methylpentanoate	Rattus norvegicus	-	-	349056	2D-image
2-oxobutanoate	Oryctolagus cuniculus	-	-	349056	2D-image
2-oxohexanedioate	Bos taurus, Oryctolagus cuniculus, Rattus norvegicus	-	-	349056, 640583	2D-image
2-Oxohexanoate	Oryctolagus cuniculus	-	-	349056, 640579	2D-image
2-oxoisocaproate	Oryctolagus cuniculus, Rattus norvegicus	-	more effective than 2-oxo-3-methylpentanoate and 2-oxoisopentanoate	349052	2D-image
2-oxoisocaproate	Bos taurus	-	-	349056, 640575	2D-image
2-oxoisocaproate	Oryctolagus cuniculus, Rattus norvegicus	-	-	349056	2D-image
2-oxoisocaproate	Oryctolagus cuniculus	-	kinetics, 40% inhibition at 0.065 mM	640579	2D-image
2-oxoisopentanoate	Oryctolagus cuniculus, Rattus norvegicus	-	less effective than 2-oxoisohexanoate and 2-oxo-3-methylpentanoate	349052	2D-image
2-oxoisopentanoate	Oryctolagus cuniculus	-	-	349056, 640579	2D-image
2-oxoisopentanoate	Rattus norvegicus	-	-	349056	2D-image
2-Oxopentanoate	Bos taurus, Oryctolagus cuniculus	-	-	349056, 640583	2D-image
2-Oxopentanoate	Oryctolagus cuniculus	-	kinetics	640579	2D-image
3-methyl-2-oxobutanoate	Bos taurus	-	-	640575	2D-image
4-(2-Thienyl)-2-oxo-3-butenoate	Bos taurus	-	2 mM	349051	2D-image
4-(3-Thienyl)-2-oxo-3-butenoate	Bos taurus	-	2 mM	349051	2D-image
4-hydroxyphenylacetate	Oryctolagus cuniculus	-	-	640578	2D-image
4-hydroxyphenyllactate	Oryctolagus cuniculus	-	weak	640578	2D-image
4-hydroxyphenylpyruvate	Oryctolagus cuniculus	-	-	349056	2D-image
4-hydroxyphenylpyruvate	Oryctolagus cuniculus	-	very weak: 3-hydroxyphenylpyruvate	640578	2D-image
4-Methyl-2-oxopentanoate	Bos taurus	-	-	640575	2D-image
acetate	Oryctolagus cuniculus	-	weak, in vivo and in vitro	640578	2D-image
acetoacetyl-CoA	Bos taurus, Oryctolagus cuniculus, Rattus norvegicus	-	-	349056, 640583	2D-image
acetoacetyl-CoA	Oryctolagus cuniculus	-	40% inhibition at 0.01 mM	640579	2D-image
acyl-CoA	Oryctolagus cuniculus	-	-	94884	2D-image
ADP	Bos taurus	-	-	349056, 640575, 640583	2D-image
ADP	Rattus norvegicus	-	-	349056, 640583	2D-image
ADP	Oryctolagus cuniculus	-	competitive	349056	2D-image
ADP	Oryctolagus cuniculus	-	kinetics	349073	2D-image
ADP	Oryctolagus cuniculus	-	-	640583	2D-image
ADP	Rattus norvegicus	Q00972	product inhibition	640594	2D-image
ADP	Bos taurus, Oryctolagus cuniculus, Rattus norvegicus	-	50% inhibition at 0.4 mM, inhibition can be reversed by 2 mM Mg2+	94884	2D-image
alpha-Chloroisocaproate	Rattus norvegicus	-	inhibits the enzyme by releasing it from the BCKD complex via dissociation	662695	2D-image
alpha-Chloroisocaproate	Rattus norvegicus	-	-	702742	2D-image
alpha-Ketoisocaproate	Rattus norvegicus	-	inhibits the enzyme by releasing it from the BCKD complex via dissociation	662695	2D-image
alpha-ketoisovalerate	Rattus norvegicus	-	inhibits the enzyme by releasing it from the BCKD complex via dissociation	662695	2D-image
ATP	Rattus norvegicus	-	-	587061, 94884	2D-image
ATP	Oryctolagus cuniculus	-	50% inhibition at 0.2 mM, inhibition can be reversed by 2 mM Mg2+	94884	2D-image
branched-chain 2-oxo acids	Bos taurus	-	-	640575, 94884	2D-image
branched-chain 2-oxo acids	Oryctolagus cuniculus, Rattus norvegicus	-	-	94884	2D-image
Ca2+	Oryctolagus cuniculus	-	weak	349056	2D-image
Ca2+	Oryctolagus cuniculus	-	-	349073	2D-image
CDP	Oryctolagus cuniculus	-	50% inhibition at 0.4 mM, inhibition can be reversed by 2 mM Mg2+	94884	2D-image
Clofibric acid	Oryctolagus cuniculus	-	-	349056	2D-image
Clofibric acid	Oryctolagus cuniculus	-	in vivo and in vitro	640578	2D-image
CoA	Oryctolagus cuniculus	-	-	94884	2D-image
CTP	Oryctolagus cuniculus	-	50% inhibition at 0.25 mM, inhibition can be reversed by 2 mM Mg2+	94884	2D-image
dexamethasone	Sus scrofa	-	decreases enzyme expression level in renal tubule cells	660683	2D-image
Dichloroacetate	Oryctolagus cuniculus, Rattus norvegicus	-	weak	349052	2D-image
Dichloroacetate	Oryctolagus cuniculus	-	-	349056, 640578, 640580	2D-image
Dichloroacetate	Rattus norvegicus	-	-	349056, 640578	2D-image
Dichloroacetate	Oryctolagus cuniculus	-	ATP slightly protects	349073	2D-image
Dichloroacetate	Rattus norvegicus	-	50% inhibition at 1.8 mM	640585, 640598	2D-image
diphosphate	Bos taurus	-	-	640575	2D-image
Furfurylidenepyruvate	Bos taurus	-	1.85 mM	349051	2D-image
GDP	Oryctolagus cuniculus	-	50% inhibition at 0.2 mM, inhibition can be reversed by 2 mM Mg2+	94884	2D-image
GTP	Oryctolagus cuniculus	-	50% inhibition at 0.06 mM, inhibition can be reversed by 2 mM Mg2+	94884	2D-image
heparin	Oryctolagus cuniculus	-	-	349056	2D-image
heparin	Oryctolagus cuniculus	-	40% inhibition at 0.012 mg/ml	640579	2D-image
heparin	Oryctolagus cuniculus	-	50% inhibition at 0.002 mM	94884	2D-image
isobutyryl-CoA	Oryctolagus cuniculus	-	-	349056, 640579	2D-image
isovaleryl-CoA	Oryctolagus cuniculus	-	-	349056, 640579	2D-image
malonyl-CoA	Oryctolagus cuniculus	-	-	349056, 640579	2D-image
methylmalonyl-CoA	Bos taurus, Oryctolagus cuniculus, Rattus norvegicus	-	-	349056, 640583	2D-image
methylmalonyl-CoA	Oryctolagus cuniculus	-	40% inhibition at 0.2 mM	640579	2D-image
Mg2+	Oryctolagus cuniculus	-	at concentrations above 1.5 mM, activation below	349056	2D-image
n-Octanoate	Bos taurus, Oryctolagus cuniculus, Rattus norvegicus	-	-	349056, 640583	2D-image
n-Octanoate	Oryctolagus cuniculus	-	40% inhibition at 0.5 mM	640579	2D-image
NADP+	Oryctolagus cuniculus	-	-	349056	2D-image
NADP+	Oryctolagus cuniculus	-	40% inhibition at 1.5 mM	640579	2D-image
phenylacetate	Oryctolagus cuniculus	-	-	349056	2D-image
phenylacetate	Oryctolagus cuniculus	-	strong	640578	2D-image
Phenyllactate	Oryctolagus cuniculus	-	-	349056	2D-image
Phenyllactate	Oryctolagus cuniculus	-	strong	640578	2D-image
phenylpyruvate	Oryctolagus cuniculus	-	in vivo and in vitro	640578	2D-image
pyruvate	Oryctolagus cuniculus	-	-	349056, 640580	2D-image
pyruvate	Oryctolagus cuniculus	-	weak	640578	2D-image
thiamine	Bos taurus	-	-	640575	2D-image
thiamine diphosphate	Rattus norvegicus	-	inhibits phosphorylation of wild-type E1, mutant E1-S303A and mutant E1-D296A/S303A, but not phosphorylation of mutant E1-H292A	349090	2D-image
thiamine diphosphate	Bos taurus	-	-	640575, 640583, 94884	2D-image
thiamine diphosphate	Rattus norvegicus	-	-	640583, 702742, 94884	2D-image
thiamine diphosphate	Oryctolagus cuniculus	-	-	640583, 94884	2D-image
UDP	Oryctolagus cuniculus	-	50% inhibition at 0.25 mM, inhibition can be reversed by 2 mM Mg2+	94884	2D-image
UTP	Oryctolagus cuniculus	-	50% inhibition at 0.1 mM, inhibition can be reversed by 2 mM Mg2+	94884	2D-image
MgATP2-	Bos taurus	-	-	640575	2D-image
additional information	Oryctolagus cuniculus, Rattus norvegicus	-	no inhibition by 2-chloropropionate	349052	-
additional information	Oryctolagus cuniculus	-	no inhibition by GTP	349073	-
additional information	Bos taurus	-	no inhibition by acetyl-CoA; no inhibition by coenzyme A	640575	-
additional information	Oryctolagus cuniculus	-	no inhibition by lactate	640578	-
additional information	Rattus norvegicus	-	-	640578	-
additional information	Oryctolagus cuniculus	-	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	640579	-
additional information	Oryctolagus cuniculus	-	no inhibition by DL-leucine	640580	-
additional information	Rattus norvegicus	-	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	656230	-
additional information	Rattus norvegicus	-	clofibric acid and thiamine diphosphate do not affect the protein-protein interaction of BDK with the BCKD complex	662695	-
additional information	Bos taurus	-	no inhibition by coenzyme A; no inhibition by isovaleryl-CoA	94884	-
additional information	Oryctolagus cuniculus, Rattus norvegicus	-	no inhibition by isovaleryl-CoA	94884	-

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
Poly-L-arginine	Oryctolagus cuniculus	-	1.5 to 3fold	94884	2D-image
poly-L-lysine	Oryctolagus cuniculus	-	1.5 to 3fold	94884	2D-image
Protamine	Oryctolagus cuniculus	-	1.5 to 3fold	94884	2D-image
Histone H3	Oryctolagus cuniculus	-	1.5 to 3fold	94884	-
additional information	Mus musculus	-	tissue-specific translation of branched-chain alpha-ketoacid dehydrogenase kinase mRNA is dependent upon an upstream open reading frame in the 5'-untranslated region	662283	-
additional information	Homo sapiens	-	exercise training increases branched-chain oxoacid dehydrogenase kinase content in human skeletal muscle, mechanism, overview	690337	-
additional information	Rattus norvegicus	-	dietary supplementation of branched-chain amino acid over several weeks increases the enzyme activity in spontaneous type II diabetic rats, overview	690740	-

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.004	-	ATP	Rattus norvegicus	-	-	640581	2D-image
0.025	-	ATP	Oryctolagus cuniculus	-	pH 7.35, 20�C	349056	2D-image
0.025	-	ATP	Oryctolagus cuniculus	-	pH 7.5, 30�C	349073	2D-image
0.0126	-	MgATP2-	Bos taurus	-	pH 7.5, 30�C	640575	2D-image
0.013	-	MgATP2-	Bos taurus	-	pH 7.5, 30�C	640583	2D-image

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.0542	-	phosphate	Rattus norvegicus	-	25�C, recombinant enzyme alone	640589	2D-image
0.475	-	phosphate	Rattus norvegicus	-	25�C, reconstituted with lipoylated recombinant E2	640589	2D-image

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.5	-	2-Chloroisohexanoate	Rattus norvegicus	-	37�C	349052	2D-image
0.00092	-	2-oxoisocaproate	Bos taurus	-	pH 7.5, 30�C	640575	2D-image
0.00048	-	4-Methyl-2-oxopentanoate	Bos taurus	-	pH 7.5, 30�C	640575	2D-image
0.0089	-	4-Methyl-2-oxopentanoate	Bos taurus	-	pH 7.5, 30�C	640575	2D-image
0.00027	-	ADP	Bos taurus	-	pH 7.5, 30�C	640575	2D-image
0.13	-	ADP	Oryctolagus cuniculus	-	pH 7.35, 20�C	349056	2D-image
0.13	-	ADP	Oryctolagus cuniculus	-	pH 7.5, 30�C	349073	2D-image
0.27	-	ADP	Bos taurus	-	pH 7.5, 30�C	640583	2D-image
0.004	-	diphosphate	Bos taurus	-	pH 7.5, 30�C	640575	2D-image
4.5	-	Furfurylidenepyruvate	Bos taurus	-	-	349051	2D-image
0.0059	-	thiamine	Bos taurus	-	pH 7.5, 30�C	640575	2D-image
0.0032	-	thiamine diphosphate	Rattus norvegicus	-	20 mM K+	702742	2D-image
0.0164	-	thiamine diphosphate	Rattus norvegicus	-	100 mM K+	702742	2D-image

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.006	-	alpha-Chloroisocaproate	Rattus norvegicus	-	100 mM K+	702742	2D-image
0.031	-	alpha-Chloroisocaproate	Rattus norvegicus	-	10 mM K+	702742	2D-image
0.0046	-	thiamine diphosphate	Rattus norvegicus	-	20 mM K+	702742	2D-image
0.008	-	thiamine diphosphate	Rattus norvegicus	-	100 mM K+	702742	2D-image

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
0.0247	-	Rattus norvegicus	-	without added salt	640581
0.0268	-	Rattus norvegicus	-	liver enzyme	640585, 640598
0.0357	0.09	Rattus norvegicus	-	heart enzyme, depending on purification method	640598
0.0357	-	Rattus norvegicus	-	heart enzyme	640585
0.05	-	Rattus norvegicus	-	recombinant enzyme	640598
additional information	-	Bos taurus, Oryctolagus cuniculus, Rattus norvegicus	-	various assay methods	640583
additional information	-	Rattus norvegicus	-	-	690740

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7.1	-	Oryctolagus cuniculus	-	-	349073
7.4	-	Rattus norvegicus	-	assay at	640595, 656230
7.5	-	Oryctolagus cuniculus	-	-	349056
additional information	-	Oryctolagus cuniculus	-	in decreasing order of activity: HEPES, potassium phosphate, imidazole, 3-(N-morpholino)ethane buffer	349056
additional information	-	Oryctolagus cuniculus	-	HEPES-potassium buffer promotes higher activity than imidazole-chloride, 4-morpholinopropanesulfonic acid-potassium or potassium phosphate buffer	349073

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
6.5	8.3	Oryctolagus cuniculus	-	about half-maximal activity at pH 6.5 and 8.3	349073

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
22	-	Rattus norvegicus	-	assay at room temperature	656230
30	-	Bos taurus	-	assay at	640575
30	-	Rattus norvegicus	-	assay at	640585, 640595
37	-	Bos taurus	-	assay at	349051
37	-	Oryctolagus cuniculus	-	assay at	349073
37	-	Rattus norvegicus	-	assay at	587061
37	-	Oryctolagus cuniculus	-	assay at	640579, 640580
37	-	Rattus norvegicus	-	assay at	640581

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
8.5	-	Rattus norvegicus	-	native PAGE	640589

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
adipocyte	Rattus norvegicus	-	-	640583
BNL CL.2 cell	Mus musculus	-	liver cell line	662283
brain	Oryctolagus cuniculus	-	-	349056
brain	Mus musculus	-	-	640590, 640591
C2C12 cell	Mus musculus	-	undifferentiated myoblast cell line	662283
embryo	Mus musculus	-	-	640591
fibroblast	Mus musculus	-	-	662283
heart	Rattus norvegicus	-	-	349056, 640578, 640583, 640585, 640587, 640594, 640598, 640599, 702742
heart	Mus musculus	-	-	640590, 640591
hepatocyte	Rattus norvegicus	-	-	349052
kidney	Rattus norvegicus	-	-	349056, 587061, 640583, 640589, 640599, 94884
kidney	Bos taurus	-	-	349056, 640575, 640576, 640577, 640583, 640588, 94884
kidney	Oryctolagus cuniculus	-	cortex	349056
kidney	Oryctolagus cuniculus	-	-	640583, 94884
kidney	Mus musculus	-	-	640590, 640591
kidney	Sus scrofa	-	-	660683
liver	Bos taurus	-	-	349051, 349056, 640583
liver	Oryctolagus cuniculus	-	-	349052, 349056, 349073, 640578, 640579, 640580, 640583
liver	Rattus norvegicus	-	-	349052, 349056, 640578, 640581, 640583, 640585, 640597, 640598, 662695, 702742
liver	Mus musculus	-	-	640590, 662283
liver	Rattus norvegicus	-	enzyme activity is 3-5fold higher in female than in male rats	640595
liver	Rattus norvegicus	-	malnutrition results in changed amounts of enzyme level	640599
liver	Rattus norvegicus	-	type 2 diabetes Otsuka Long-Evans Tokushima Fatty rats and Zucker diabetic fatty rats	690740
LLC-PK1-GR101 cell	Sus scrofa	-	LLC-PK1 renal tubule cell line expressing the Rattus norvegicus glucocorticoid receptor GR	660683
muscle	Mus musculus	-	-	640590, 640591
myoblast	Mus musculus	-	-	662283
myotube	Mus musculus	-	-	662283
NIH-3T3 cell	Mus musculus	-	fibroblast cell line	662283
renal tubule	Sus scrofa	-	-	660683
skeletal muscle	Rattus norvegicus	-	-	349056, 640595
skeletal muscle	Oryctolagus cuniculus	-	-	349056
skeletal muscle	Rattus norvegicus	-	enzyme content decreases 0.7fold after running exercise for 5 weeks	640592
skeletal muscle	Mus musculus	-	-	662283
skeletal muscle	Homo sapiens	-	-	690337
testis	Mus musculus	-	-	640590
uterus	Mus musculus	-	-	640590
lung	Mus musculus	-	-	640590
additional information	Sus scrofa	-	enzyme expression analysis	660683
additional information	Mus musculus	-	tissue distribution, tissue-specific translation of branched-chain alpha-ketoacid dehydrogenase kinase mRNA is dependent upon an upstream open reading frame in the 5'-untranslated region, thus mRNA and protein level do not correlate	662283

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
mitochondrial matrix	Rattus norvegicus	-	-	5759	640581
mitochondrial matrix	Rattus norvegicus	-	2 forms: first form is bound to E2, second form is free and seems to be inactive	5759	640597
mitochondrion	Bos taurus	-	-	5739	349051, 640575, 640576, 640583, 640588, 94884
mitochondrion	Bos taurus, Oryctolagus cuniculus, Rattus norvegicus	-	part of intramitochondrial branched-chain 2-oxoacid dehydrogenase complex	5739	349056
mitochondrion	Rattus norvegicus	-	-	5739	587061, 640583, 640587, 640596, 640599, 94884
mitochondrion	Oryctolagus cuniculus	-	-	5739	640583, 94884
mitochondrion	Mus musculus	-	-	5739	640590, 640591, 662283
mitochondrion	Sus scrofa	-	-	5739	660683

PDB	SCOP	CATH	ORGANISM
3tz0, download	SCOP (3tz0)	CATH (3tz0)	Rattus norvegicus
3tz2, download	SCOP (3tz2)	CATH (3tz2)	Rattus norvegicus
3tz4, download	SCOP (3tz4)	CATH (3tz4)	Rattus norvegicus
3tz5, download	SCOP (3tz5)	CATH (3tz5)	Rattus norvegicus

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
43280	-	Rattus norvegicus	-	calculated from amino acid sequence	640587
44000	45000	Rattus norvegicus	-	SDS-PAGE	640598
460000	-	Oryctolagus cuniculus	-	gel filtration	94884
2000000	-	Oryctolagus cuniculus	-	above 2000000, gel filtration	349056, 349073

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
?	Rattus norvegicus	-	x * 44000, SDS-PAGE	640585
dimer	Rattus norvegicus	Q00972	dimerizes through direct interaction of two opposing nucleotide-binding domains, crystallographic data	640594
monomer	Bos taurus	-	1 * 43000, uncomplexed kinase, SDS-PAGE	640588

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
vapor diffusion method	Rattus norvegicus	Q00972	640594

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7	-	Bos taurus	-	loss of activity during purification at pH-values below 7	640575

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	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	Bos taurus, Oryctolagus cuniculus, Rattus norvegicus	-	640583

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
labile enzyme, best stored at -70�C in the presence of DTT	Rattus norvegicus	-	640585

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Bos taurus	-	640575
5000fold	Bos taurus	-	640588
copurifies with EC 1.2.4.4	Bos taurus	-	640576
-	Oryctolagus cuniculus	-	640578
alpha-ketoacid dehydrogenase complex	Oryctolagus cuniculus	-	349056, 349073
-	Rattus norvegicus	-	349056, 640589
alpha-ketoacid dehydrogenase complex	Rattus norvegicus	-	587061
from liver and heart, homogeneity	Rattus norvegicus	-	640583
from purified branched-chain alpha-keto acid dehydrogenase complex	Rattus norvegicus	-	640585
liver enzyme, heart enzyme and recombinant enzyme expressed in Escherichia coli	Rattus norvegicus	-	640598
partially from mitochondria	Sus scrofa	-	660683

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Mus musculus	-	640590, 640591
DNA sequence determination and analysis, promotor region footprinting, expression analysis, mechanism of the enzyme expression regulation	Mus musculus	-	662283
-	Rattus norvegicus	-	640598
cloned and expressed in Escherichia coli	Rattus norvegicus	-	640587
fragments of the enzyme cloned into firefly luciferase plasmid	Rattus norvegicus	-	640596
fusion protein with maltose-binding protein	Rattus norvegicus	-	640589, 640594
BCKD kinase transcription regulation, overview	Sus scrofa	-	660683

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
reconstitution with lipoylated recombinant E2	Rattus norvegicus	-	640589

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

DISEASE	TITLE OF PUBLICATION	LINK TO PUBMED
Carcinoma, Hepatocellular	Regulation of branched-chain alpha-keto acid dehydrogenase kinase gene expression by glucocorticoids in hepatoma cells and rat liver.	PubMed
Diabetes Mellitus	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.	PubMed
Diabetes Mellitus, Type 2	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.	PubMed
Hyperthyroidism	Experimental hyperthyroidism causes inactivation of the branched-chain alpha-ketoacid dehydrogenase complex in rat liver.	PubMed
Obesity	Obesity-related elevations in plasma leucine are associated with alterations in enzymes involved in branched-chain amino acid metabolism.	PubMed
Protein Deficiency	A new family of protein kinases--the mitochondrial protein kinases.	PubMed
Protein Deficiency	Effect of dietary protein on the liver content and subunit composition of the branched-chain alpha-ketoacid dehydrogenase complex.	PubMed
Protein Deficiency	Physiological covalent regulation of rat liver branched-chain alpha-ketoacid dehydrogenase.	PubMed
Renal Insufficiency	Differential regulation of branched-chain alpha-ketoacid dehydrogenase kinase expression by glucocorticoids and acidification in LLC-PK1-GR101 cells.	PubMed
Starvation	Effects of low-protein diet and starvation on the activity of branched-chain 2-oxo acid dehydrogenase kinase in rat liver and heart.	PubMed
Starvation	Hepatic branched-chain alpha-keto acid dehydrogenase complex in female rats: activation by exercise and starvation.	PubMed
Starvation	Regulation of branched-chain alpha-keto acid dehydrogenase kinase expression in rat liver.	PubMed

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
94884	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	PubMed
349051	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	360-366	1990	Bos taurus	PubMed
349052	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	PubMed
349056	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	PubMed
349073	Paxton, R.; Harris, R.A.	Isolation of rabbit liver branched chain alpha-ketoacid dehydrogenase and regulation by phosphorylation	J. Biol. Chem.	257	14433-14439	1982	Oryctolagus cuniculus	PubMed
349090	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	PubMed
587061	Odessey, R.	Purification of rat kidney branched-chain oxo acid dehydrogenase complex with endogenous kinase activity	Biochem. J.	204	353-356	1982	Rattus norvegicus	PubMed
640575	Lau, K.S.; Fatania, H.R.; Randle, P.J.	Regulation of the branched chain 2-oxoacid dehydrogenase kinase reaction	FEBS Lett.	144	57-62	1982	Bos taurus	PubMed
640576	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.	157	54-58	1982	Bos taurus	-
640577	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	-
640578	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	PubMed
640579	Paxton, R.; Harris, R.A.	Regulation of branched-chain alpha-ketoacid dehydrogenase kinase	Arch. Biochem. Biophys.	231	48-57	1984	Oryctolagus cuniculus	PubMed
640580	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	PubMed
640581	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	PubMed
640583	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	PubMed
640585	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	PubMed
640587	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	PubMed
640588	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	PubMed
640589	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	PubMed
640590	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	213-219	1998	Mus musculus	PubMed
640591	Doering, C.B.; Danner, D.J.	Expression of murine branched-chain alpha-keto acid dehydrogenase kinase	Methods Enzymol.	324	491-497	2000	Mus musculus	PubMed
640592	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	PubMed
640594	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	PubMed
640595	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	PubMed
640596	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	PubMed
640597	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	PubMed
640598	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	PubMed
640599	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	PubMed
656230	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	PubMed
660683	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	PubMed
662283	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	PubMed
662695	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	PubMed
690337	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	PubMed
690740	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	PubMed
702742	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	PubMed

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