Literature summary for 3.1.3.43 extracted from

Karpova, T.; Danchuk, S.; Huang, B.; Popov, K.M.
Probing a putative active site of the catalytic subunit of pyruvate dehydrogenase phosphatase 1 (PDP1c) by site-directed mutagenesis (2004), Biochim. Biophys. Acta, 1700, 43-51.

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Protein Variants

Protein Variants	Comment	Organism
D445A	almost complete loss of activity	Rattus norvegicus
D54A	almost complete loss of activity	Rattus norvegicus
N49A	38% of activity of wild type	Rattus norvegicus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
29.3	-	p-nitrophenyl phosphate	pH 7.8, wild type enzyme	Rattus norvegicus
48.9	-	p-nitrophenyl phosphate	pH 7.8, D445A mutant	Rattus norvegicus
55.1	-	p-nitrophenyl phosphate	pH 7.8, N49A mutant	Rattus norvegicus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	required for binding of catalytic subunit	Rattus norvegicus
Mg2+	required, Km-value about 0.3-0.5 mM	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
p-nitrophenyl phosphate + H2O	-	Rattus norvegicus	p-nitrophenol + phosphate	-	?

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Release 2023.1 (January 2023)