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Literature summary for 2.7.11.2 extracted from

  • Klyuyeva, A.; Tuganova, A.; Popov, K.M.
    Allosteric coupling in pyruvate dehydrogenase kinase 2 (2008), Biochemistry, 47, 8358-8366.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.2

Protein Variants

Protein Variants Comment Organism
R250A catalytic activity is markedly reduced, Kd value for ATP is 32fold increased, resistant to the inhibitory effect of dichloroacetate, a synthetic analogue of pyruvate Rattus norvegicus
T302A catalytic activity is considerably reduced, Kd value for ATP is 24fold increased, resistant to the inhibitory effect of dichloroacetate, a synthetic analogue of pyruvate Rattus norvegicus
Y320F catalytic activity is slightly reduced, Kd value for ATP is decreased to 68%, resistant to the inhibitory effect of dichloroacetate, a synthetic analogue of pyruvate Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus Q64536
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-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.045
-
 PDHK2 mutant T302A Rattus norvegicus
0.17
-
 PDHK2 mutant R250A Rattus norvegicus
0.46
-
 PDHK2 mutant Y320F Rattus norvegicus
0.53
-
 wild type PDHK2 Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + pyruvate dehydrogenase Kd for ATP is 2.5 micromol, for ADP 10.6 micromol and for dichloroacetate 226 micromol Rattus norvegicus ADP + phosphorylated pyruvate dehydrogenase
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 ?

Synonyms

Synonyms Comment Organism
PDHK2
-
 Rattus norvegicus
pyruvate dehydrogenase kinase 2
-
 Rattus norvegicus

General Information

General Information Comment Organism
physiological function phosphorylation (activation) of pyruvate dehydrogenase Rattus norvegicus