Literature summary for 2.7.11.31 extracted from

Chen, L.; Jiao, Z.H.; Zheng, L.S.; Zhang, Y.Y.; Xie, S.T.; Wang, Z.X.; Wu, J.W.
Structural insight into the autoinhibition mechanism of AMP-activated protein kinase (2009), Nature, 459, 1146-1149.

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Activating Compound

Activating Compound	Comment	Organism
AMP	wild-type is activated about 2fold in the presence of 0.2 mM. The catalytic activity and substrate binding affinity of AMPK are separately regulated by AMP binding and the assembly of beta- and gamma-subunits onto the alpha-subunit	Rattus norvegicus
CaMKKbeta	phosphorylates	Rattus norvegicus
CaMKKbeta	phosphorylates	Saccharomyces cerevisiae
CaMKKbeta	phosphorylates	Schizosaccharomyces pombe
additional information	hydrophobic contacts between the kinase domain and the autoinhibitory domain have a predominant role in controlling the conformational change between low- and high activity forms of AMPK	Schizosaccharomyces pombe

Cloned(Commentary)

Cloned (Comment)	Organism
kinase domain and catalytic kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit. AMPK holoenzyme expressed in a tricistronic vector	Rattus norvegicus
kinase domain and kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit	Saccharomyces cerevisiae
kinase domain and kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit	Schizosaccharomyces pombe

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals grown by mixing proteins with ammonium formate. Crystal structure of phosphorylated kinase domain, to 2.9 A resolution. Phosphorylated kinase domain displays a closed conformation	Saccharomyces cerevisiae
crystals grown by mixing proteins with ammonium sulphate. Crystal structure of an unphosphorylated fragment of the AMPK alpha-subunit that contains both the catalytic kinase domain and an autoinhibitory domain, to 2.8 A resolution. The unphosphorylated kinase domain of catalytic kinase domain/autoinhibitory domain fragment adopts an open inactive conformation. Kinase domain/autoinhibitory domain is jammed into its active site, and the critical catalytic residues make several intra- and intermolecular contacts	Schizosaccharomyces pombe

Crystallization (Comment)

Organism

crystals grown by mixing proteins with ammonium formate. Crystal structure of phosphorylated kinase domain, to 2.9 A resolution. Phosphorylated kinase domain displays a closed conformation

Saccharomyces cerevisiae

crystals grown by mixing proteins with ammonium sulphate. Crystal structure of an unphosphorylated fragment of the AMPK alpha-subunit that contains both the catalytic kinase domain and an autoinhibitory domain, to 2.8 A resolution. The unphosphorylated kinase domain of catalytic kinase domain/autoinhibitory domain fragment adopts an open inactive conformation. Kinase domain/autoinhibitory domain is jammed into its active site, and the critical catalytic residues make several intra- and intermolecular contacts

Schizosaccharomyces pombe

Protein Variants

Protein Variants	Comment	Organism
D329K	catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity	Rattus norvegicus
E344K	mutation in the autoinhibitory domain, disruption of the hydrophilic interactions, yields a modest but marked increase in basal activity	Schizosaccharomyces pombe
F300E	catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity	Rattus norvegicus
I327D	catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity	Rattus norvegicus
L312D	mutation in the autoinhibitory domain, leads to marked enzymatic activation	Schizosaccharomyces pombe
L326D	catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity	Rattus norvegicus
L341D	mutation in the autoinhibitory domain, catalytic efficiency is increased approximately 10fold, comparable to that of the wild-type kinase domain	Schizosaccharomyces pombe
L342D	mutation in the autoinhibitory domain, catalytic efficiency is increased approximately 10fold, comparable to that of the wild-type kinase domain	Schizosaccharomyces pombe
L88A	mutation in the kinase domain, has decreased catalytic activity	Schizosaccharomyces pombe
M316E	mutation in the autoinhibitory domain, catalytic efficiency is increased approximately 10fold, comparable to that of the wild-type kinase domain	Schizosaccharomyces pombe
N330A	catalytic kinase domain/autoinhibitory domain mutant, shows little or no effect on specific activity	Rattus norvegicus
N345A	mutation in the autoinhibitory domain, has little effect	Schizosaccharomyces pombe
R149E	mutation in the kinase domain, has decreased catalytic activity	Schizosaccharomyces pombe
R263A	catalytic kinase domain/autoinhibitory domain mutant, shows little or no effect on specific activity	Rattus norvegicus
R280A	mutation in the autoinhibitory domain, has no effect on kinase activity	Schizosaccharomyces pombe
V296D	catalytic kinase domain/autoinhibitory domain mutant, shows enhanced specific activity	Rattus norvegicus

Inhibitors

Inhibitors	Comment	Organism
additional information	autoinhibition of AMPK by the autoinhibitory domain. The autoinhibitory domain in the holoenzyme has a bona fide inhibiting role in the rate of phosphoryl transfer (kcat) as it does in the catalytic kinase domain/autoinhibitory domain fragments	Rattus norvegicus
additional information	kinase domain/autoinhibitory domain fragment is inactive in the unphosphorylated state, and exhibits low basal kinase activities when phosphorylated at residue Thr 210	Saccharomyces cerevisiae
additional information	kinase domain/autoinhibitory domain fragment is inactive in the unphosphorylated state, and exhibits low basal kinase activities when phosphorylated at residue Thr 189	Schizosaccharomyces pombe

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	-	-	-
Saccharomyces cerevisiae	-	-	-
Schizosaccharomyces pombe	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
kinase domain and catalytic kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit	Rattus norvegicus
kinase domain and kinase domain/autoinhibitory domain fragments of AMPK alpha-subunit	Schizosaccharomyces pombe
kinase domain and kinase domain/autoinhibitory fragments of AMPK alpha-subunit	Saccharomyces cerevisiae

Storage Stability

Storage Stability	Organism
-80°C, glycerol	Rattus norvegicus
-80°C, glycerol	Saccharomyces cerevisiae
-80°C, glycerol	Schizosaccharomyces pombe

Subunits

Subunits	Comment	Organism
heterotrimer	wild-type	Rattus norvegicus

Synonyms

Synonyms	Comment	Organism
AMP-activated protein kinase	-	Rattus norvegicus
AMP-activated protein kinase	-	Saccharomyces cerevisiae
AMP-activated protein kinase	-	Schizosaccharomyces pombe
AMPK	-	Rattus norvegicus
AMPK	-	Saccharomyces cerevisiae
AMPK	-	Schizosaccharomyces pombe
PRKAA1	-	Rattus norvegicus
Snf1	-	Saccharomyces cerevisiae