Literature summary extracted from
Yang, J.; Ten Eyck, L.F.; Xuong, N.H.; Taylor, S.S.
Crystal structure of a cAMP-dependent protein kinase mutant at 1.26A: new insights into the catalytic mechanism (2004), J. Mol. Biol., 336, 473-487.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.11.11 |
expression of wild-type and mutant Y204A in Escherichia coli |
Mus musculus |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.7.11.11 |
purified recombinant wild-type and mutant PKA catalytic subunits, 0.002 ml 5 mg/ml protein in 50 mM bicine, pH 8.0, 200 mM ammonium acetate, 2 mM DTT, MgCl2, ATP, and IP20, is mixed with 0.001 ml well solution containing 8-12% v/v 2-methyl-2,4-pentanediol and 10 mM DTT, addition of 7% v/v methanol before sealing, X-ray diffraction structure determination and analysis at 1.26 A resolution, modeling |
Mus musculus |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.11.11 |
Y204A |
site-directed mutagenesis, mutation in the catalytic subunit, reduced catalytic efficiency compared to the wild-type enzyme |
Mus musculus |
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
2.7.11.11 |
IP20 |
inhibitory peptide TTYADFIASGRTGRRN, residues 5-24 of inhibitor PKI, inhibits the ATPase function of the enzyme |
Mus musculus |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.7.11.11 |
Mg2+ |
- |
Mus musculus |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.11.11 |
Mus musculus |
P05132 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.11.11 |
recombinant wild-type and mutant Y204A from Escherichia coli by ion exchange chromatography and gel filtration |
Mus musculus |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
2.7.11.11 |
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate |
catalytic mechanism, active site structure, Tyr204 is required and involved in the hydrophobic network, substrate-induced interaction of Tyr204 and Asp166, overview |
Mus musculus |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.11.11 |
ATP + Kemptide |
LRRASLG peptide substrate |
Mus musculus |
ADP + Kemptide phosphate |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.11.11 |
PKA |
- |
Mus musculus |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
2.7.11.11 |
ATP |
- |
Mus musculus |
|