Literature summary for 2.7.11.11 extracted from

Gerlits, O.; Das, A.; Keshwani, M.M.; Taylor, S.; Waltman, M.J.; Langan, P.; Heller, W.T.; Kovalevsky, A.
Metal-free cAMP-dependent protein kinase can catalyze phosphoryl transfer (2014), Biochemistry, 53, 3179-3186.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Mus musculus

Crystallization (Commentary)

Crystallization (Comment)	Organism
ternary and binary complexes with no metals, Na+ or K+, ATP (orATP-gammaS), and SP20 protein, sitting drop vapor diffusion method, using 100 mM MES-NH4OH, pH 6.5, 5 mM dithiothreitol, 15-20% (w/v) PEG 4000	Mus musculus

Inhibitors

Inhibitors	Comment	Organism	Structure
PKI	-	Mus musculus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	highest activity in the presence of Mg2+	Mus musculus
additional information	not activated by Na+, K+, and Ca2+	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	P05132	-	-

Purification (Commentary)

Purification (Comment)	Organism
HisTrap column chromatography, and gel filtration	Mus musculus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + SP20 protein	i.e. TTYADFIASGRTGRRASIHD	Mus musculus	ADP + phosphorylated SP20 protein	-	?

Synonyms

Synonyms	Comment	Organism
PKAc	catalytic subunit of cAMP-dependent protein kinase	Mus musculus

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Release 2023.1 (January 2023)