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EC Tree
IUBMB Comments The enzyme has no activating compound but is specific for its substrate. It is a mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals. Phosphorylation inactivates EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring).
The taxonomic range for the selected organisms is: Arabidopsis thaliana The enzyme appears in selected viruses and cellular organisms
Synonyms
pyruvate dehydrogenase kinase, pyruvate dehydrogenase kinase 4, pdh kinase, pdhk2, pdhk1, pdk-4, pyruvate dehydrogenase kinase-4, pdhk4, pyruvate dehydrogenase kinase 2, pdk-2,
more
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kinase (phosphorylating), pyruvate dehydrogenase
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pyruvate dehydrogenase kinase
pyruvate dehydrogenase kinase (phosphorylating)
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pyruvate dehydrogenase kinase activator protein
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pyruvate dehydrogenase-kinase
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PDK
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pyruvate dehydrogenase kinase
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pyruvate dehydrogenase kinase
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ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
mechanism
ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
His121 is involved in the catalytic reaction
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phospho group transfer
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ATP:[pyruvate dehydrogenase (acetyl-transferring)] phosphotransferase
The enzyme has no activating compound but is specific for its substrate. It is a mitochondrial enzyme associated with the pyruvate dehydrogenase complex in mammals. Phosphorylation inactivates EC 1.2.4.1, pyruvate dehydrogenase (acetyl-transferring).
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ATP + pyruvate dehydrogenase
ADP + phosphorylated pyruvate dehydrogenase
ATP + [pyruvate dehydrogenase (acetyl-transferring)]
ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
ATP + [pyruvate dehydrogenase (lipoamide)]
ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
additional information
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ATP + pyruvate dehydrogenase
ADP + phosphorylated pyruvate dehydrogenase
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ATP + pyruvate dehydrogenase
ADP + phosphorylated pyruvate dehydrogenase
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ATP + pyruvate dehydrogenase
ADP + phosphorylated pyruvate dehydrogenase
pyruvate dehydrogenase kinase is a negative regulator in the mitochondrial pyruvate dehydrogenase complex and plays a pivotal role in controlling TCA cycle and cell respiration
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ATP + [pyruvate dehydrogenase (acetyl-transferring)]
ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
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phosphorylation at Ser292 by PDK1
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ATP + [pyruvate dehydrogenase (acetyl-transferring)]
ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
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reversible phosphorylation of alpha2beta2-heterotetrameric pyruvate dehydrogenase complex, i.e. E1, phosphorylation at Ser292 within the active-site loop structure of E1alpha by PDK1. Substrate mutation of Asp295 to Ala, Asn, or Leu greatly reduces phosphorylation of Ser292, while mutation of Gly297 has relatively little effect. AtPDC E1alpha S298A mutant is phosphorylated by AtPDK. Activity of the enzyme with different substrate mutants, overview
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ATP + [pyruvate dehydrogenase (lipoamide)]
ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
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ATP + [pyruvate dehydrogenase (lipoamide)]
ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
substrate is kinase-depleted pyruvate dehydrogenase complex from Zea mays
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ATP + [pyruvate dehydrogenase (lipoamide)]
ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
the enzyme is the primary regulator of flux through the mitochondrial pyruvate dehydrogenase complex
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additional information
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performs pH-dependent autophosphorylation on serine residues
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additional information
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performs pH-dependent autophosphorylation on serine residues
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additional information
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pyruvate dehydrogenase Asp295 plays an important role in stabilizing the active-site loop structure of the pyruvate dehydrogenase, facilitating transfer of the gamma-phosphate from ATP to the Ser residue at regulatory site one of E1alpha, substrate structure, overview
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ATP + pyruvate dehydrogenase
ADP + phosphorylated pyruvate dehydrogenase
ATP + [pyruvate dehydrogenase (acetyl-transferring)]
ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate
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phosphorylation at Ser292 by PDK1
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r
ATP + [pyruvate dehydrogenase (lipoamide)]
ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
ATP + pyruvate dehydrogenase
ADP + phosphorylated pyruvate dehydrogenase
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ATP + pyruvate dehydrogenase
ADP + phosphorylated pyruvate dehydrogenase
pyruvate dehydrogenase kinase is a negative regulator in the mitochondrial pyruvate dehydrogenase complex and plays a pivotal role in controlling TCA cycle and cell respiration
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ATP + [pyruvate dehydrogenase (lipoamide)]
ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
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ir
ATP + [pyruvate dehydrogenase (lipoamide)]
ADP + [pyruvate dehydrogenase (lipoamide)] phosphate
the enzyme is the primary regulator of flux through the mitochondrial pyruvate dehydrogenase complex
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ir
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ATP
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Mg2+
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0.05 - 3.5
pyruvate dehydrogenase
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additional information
additional information
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0.05
pyruvate dehydrogenase
pH 7.5, 37°C, recombinant PDK mutant L234H
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0.05
pyruvate dehydrogenase
pH 7.5, 37°C, recombinant wild-type PDK
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0.075
pyruvate dehydrogenase
pH 7.5, 37°C, recombinant PDK mutant L234A
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0.2
pyruvate dehydrogenase
pH 7.5, 37°C, recombinant PDK mutant H233A
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0.28
pyruvate dehydrogenase
pH 7.5, 37°C, recombinant PDK mutant E238A
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0.4
pyruvate dehydrogenase
pH 7.5, 37°C, recombinant PDK mutant E238Q
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3.5
pyruvate dehydrogenase
about, pH 7.5, 37°C, recombinant PDK mutant E238H
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additional information
additional information
kinetics
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additional information
additional information
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kinetics
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0.0004 - 0.55
pyruvate dehydrogenase
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0.0004
pyruvate dehydrogenase
pH 7.5, 37°C, recombinant PDK mutant E238A
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0.0005
pyruvate dehydrogenase
pH 7.5, 37°C, recombinant PDK mutant E238H
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0.07
pyruvate dehydrogenase
pH 7.5, 37°C, recombinant PDK mutant L234A
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0.28
pyruvate dehydrogenase
pH 7.5, 37°C, recombinant PDK mutant H233A
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0.39
pyruvate dehydrogenase
pH 7.5, 37°C, recombinant PDK mutant L234H
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0.55
pyruvate dehydrogenase
pH 7.5, 37°C, recombinant wild-type PDK
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7.5
assay at, pH-dependency of wild-type and mutant PDKs, overview
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37
assay at, temperature-dependency of wild-type and mutant PDKs, overview
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SwissProt
brenda
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SwissProt
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PDK_ARATH
366
0
41447
Swiss-Prot
other Location (Reliability: 3 )
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44000
2 * 44000, recombinant enzyme with maltose-binding protein cleaved off, SDS-PAGE
86000
approximately, recombinant enzyme with maltose-binding protein cleaved off, gel filtration
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dimer
2 * 44000, recombinant enzyme with maltose-binding protein cleaved off, SDS-PAGE
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E238A
site-directed mutagenesis, highly reduced activity compared to the wild-type PDK
E238H
site-directed mutagenesis, highly reduced activity compared to the wild-type PDK
E238Q
site-directed mutagenesis, highly reduced activity compared to the wild-type PDK
H121A
site-directed mutagenesis, 50% decreased trans- and autophosphorylation activity
H121Q
site-directed mutagenesis, 50% decreased trans- and autophosphorylation activity
H233A
site-directed mutagenesis, reduced activity compared to the wild-type PDK
K241A
site-directed mutagenesis, highly reduced activity compared to the wild-type PDK
L234A
site-directed mutagenesis, reduced activity compared to the wild-type PDK
L234H
site-directed mutagenesis, reduced activity compared to the wild-type PDK
additional information
construction of transgenic plants with silenced PDHK via expression of an antisense construct driven by both constitutive and seed-specific promoters leading to increased respiration rate in leaves, seed oil content, and seed weight in both cases, mutant phenotypes, overview
additional information
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construction of transgenic plants with silenced PDHK via expression of an antisense construct driven by both constitutive and seed-specific promoters leading to increased respiration rate in leaves, seed oil content, and seed weight in both cases, mutant phenotypes, overview
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recombinant from Escherichia coli as a fusion protein with the maltose-binding protein, to near homogeneity
recombinant His6-tagged wild-type and mutant PDKs from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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functional expression as maltose-binding protein fusion protein in Escherichia coli
PDK DNA sequence determination and analysis, expression of His6-tagged wild-type and mutant PDKs in Escherichia coli strain BL21(DE3)
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Thelen, J.J.; Miernyk, J.A.; Randall, D.D.
Pyruvate dehydrogenase kinase from Arabidopsis thaliana: a protein histidine kinase that phosphorylates serine residues
Biochem. J.
349
195-201
2000
Arabidopsis thaliana (Q9SBJ1), Arabidopsis thaliana
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Roche, T.E.; Baker, J.C.; Yan, X.; Hiromasa, Y.; Gong, X.; Peng, T.; Dong, J.; Turkan, A.; Kasten, S.A.
Distinct regulatory properties of pyruvate dehydrogenase kinase and phosphatase isoforms
Prog. Nucleic Acid Res. Mol. Biol.
70
33-75
2001
Arabidopsis thaliana, Bos taurus, Homo sapiens, Mammalia, Rattus norvegicus, Zea mays
brenda
Tovar-Mendez, A.; Hirani, T.A.; Miernyk, J.A.; Randall, D.D.
Analysis of the catalytic mechanism of pyruvate dehydrogenase kinase
Arch. Biochem. Biophys.
434
159-168
2005
Arabidopsis thaliana (Q9SBJ1), Arabidopsis thaliana
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Marillia, E.F.; Micallef, B.J.; Micallef, M.; Weninger, A.; Pedersen, K.K.; Zou, J.; Taylor, D.C.
Biochemical and physiological studies of Arabidopsis thaliana transgenic lines with repressed expression of the mitochondrial pyruvate dehydrogenase kinase
J. Exp. Bot.
54
259-270
2003
Arabidopsis thaliana (Q9SBJ1), Arabidopsis thaliana
brenda
Hirani, T.; Tovar-Mendez, A.; Miernyk, J.; Randall, D.
Asp295 stabilizes the active-site loop structure of pyruvate dehydrogenase, facilitating phosphorylation of Ser292 by pyruvate dehydrogenase-kinase
Enzyme Res.
2011
939068
2011
Arabidopsis thaliana
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