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Literature summary for 2.7.11.2 extracted from

  • Klyuyeva, A.; Tuganova, A.; Popov, K.M.
    Amino acid residues responsible for the recognition of dichloroacetate by pyruvate dehydrogenase kinase 2 (2007), FEBS Lett., 581, 2988-2992.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant PDHK2 isozymes Homo sapiens

Protein Variants

Protein Variants Comment Organism
D117A site-directed mutagenesis, the mutant enzyme shows no inhibition by dichloroacetate in contrast to the wild-type PDHK2 Homo sapiens
H115A site-directed mutagenesis, the mutant enzyme shows reduced inhibition by dichloroacetate compared to the wild-type PDHK2 Homo sapiens
I111A site-directed mutagenesis, the mutant enzyme shows reduced inhibition by dichloroacetate compared to the wild-type PDHK2 Homo sapiens
I157A site-directed mutagenesis, the mutant enzyme shows increased inhibition by dichloroacetate compared to the wild-type PDHK2 Homo sapiens
I161A site-directed mutagenesis, the mutant enzyme shows unaltered inhibition by dichloroacetate compared to the wild-type PDHK2 Homo sapiens
L53A site-directed mutagenesis, the mutant enzyme shows reduced inhibition by dichloroacetate compared to the wild-type PDHK2 Homo sapiens
R112A site-directed mutagenesis, the mutant enzyme shows unaltered inhibition by dichloroacetate compared to the wild-type PDHK2 Homo sapiens
R114A site-directed mutagenesis, the mutant enzyme shows no inhibition by dichloroacetate in contrast to the wild-type PDHK2 Homo sapiens
R154A site-directed mutagenesis, the mutant enzyme shows unaltered inhibition by dichloroacetate compared to the wild-type PDHK2 Homo sapiens
R158A site-directed mutagenesis, the mutant enzyme shows unaltered inhibition by dichloroacetate compared to the wild-type PDHK2 Homo sapiens
S83A site-directed mutagenesis, the mutant enzyme shows no inhibition by dichloroacetate in contrast to the wild-type PDHK2 Homo sapiens
Y80A site-directed mutagenesis, the mutant enzyme shows no inhibition by dichloroacetate in contrast to the wild-type PDHK2 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Dichloroacetate R114, S83, I157 and, to some extent, H115 are essential for DCA binding by PDHK, Y80 and D117 are required for the communication between the dichloroacetate-binding site and active site of PDHK2, overview Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 isozyme PDHK2
-

Subunits

Subunits Comment Organism
dimer homodimer Homo sapiens

Synonyms

Synonyms Comment Organism
PDHK
-
 Homo sapiens
pyruvate dehydrogenase kinase
-
 Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information dichloroacetate inhibition kinetics and EC50 values with wild-type and mutant PDHK2s Homo sapiens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.013
-
 recombinant isozyme PDHK2 mutant I157A Homo sapiens Dichloroacetate
1.2
-
 recombinant isozyme PDHK2 mutant R112A Homo sapiens Dichloroacetate
1.7
-
 recombinant isozyme PDHK2 mutant R154A Homo sapiens Dichloroacetate
2
-
 recombinant isozyme PDHK2 mutant R158A Homo sapiens Dichloroacetate
2.3
-
 recombinant wild-type isozyme PDHK2 Homo sapiens Dichloroacetate
2.7
-
 recombinant isozyme PDHK2 mutant I161A Homo sapiens Dichloroacetate
8.4
-
 recombinant isozyme PDHK2 mutant H115A Homo sapiens Dichloroacetate
17.1
-
 recombinant isozyme PDHK2 mutant L53A Homo sapiens Dichloroacetate
17.9
-
 recombinant isozyme PDHK2 mutant I111A Homo sapiens Dichloroacetate