Literature summary for 3.1.3.43 extracted from

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 (2001), Prog. Nucleic Acid Res. Mol. Biol., 70, 33-75.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	activation, overview	Mammalia
Mg2+	two molecules per active site of each isoform, regulation of enzyme activity via effector-altered sensitivities to Mg2+-level	Mammalia

Organism

Organism	UniProt	Comment	Textmining
Mammalia	-	two isoforms	-

Reaction

Reaction	Comment	Organism	Reaction ID
[pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate	overview on mechanism and regulation of enzyme	Mammalia	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
adipose tissue	PDP2, probably target for insulin activation	Mammalia	-
brain	PDP1	Mammalia	-
heart	PDP1	Mammalia	-
kidney	PDP1	Mammalia	-
liver	PDP1, PDP2	Mammalia	-
skeletal muscle	PDP1	Mammalia	-

Subunits

Subunits	Comment	Organism
heterodimer	isoform PDP1, composed of catalytic subunit PDP1c and regulatory subunit PDP1r of 96000 Da, overview	Mammalia

Cofactor

Cofactor	Comment	Organism	Structure
FAD	noncovalently bound to PDP1r	Mammalia

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Release 2023.1 (January 2023)