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Literature summary for 3.1.3.43 extracted from

  • Vassylyev, D.G.; Symersky, J.
    Crystal structure of pyruvate dehydrogenase phosphatase 1 and its functional implications (2007), J. Mol. Biol., 370, 417-426.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.3.43

Crystallization (Commentary)

Crystallization (Comment) Organism
PDP1c, by using the sitting-drop, vapor-diffusion method Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ PDP1 is highly enhanced through Ca2+-dependent binding of PDP1c to the inner lipoyl domain L2 of the dihydrolipoyl acetyltransferase E2 Rattus norvegicus
Mg2+ required at five active site residues Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52600
-
 PDP1c Rattus norvegicus
96000
-
 PDP1r Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus O88483
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O
-
 Rattus norvegicus [pyruvate dehydrogenase (acetyl-transferring)] + phosphate
-
 ?

Synonyms

Synonyms Comment Organism
PDP1 PDP1r regulatory subunit, PDP1c catalytic subunit Rattus norvegicus
pyruvate dehydrogenase phosphatase
-
 Rattus norvegicus
[pyruvate dehydrogenase (acetyl-transferring)]-phosphatase
-
 Rattus norvegicus